Cross-reactive human B cell and T cell epitopes between influenza A and B viruses
Influenza A and B viruses form different genera, which were originally distinguished by antigenic differences in their nucleoproteins and matrix 1 proteins. Cross-protection between these two genera has not been observed in animal experiments, which is consistent with the low homology in viral prote...
Saved in:
| Published in | Virology journal Vol. 10; no. 1; p. 244 |
|---|---|
| Main Authors | , , , |
| Format | Journal Article |
| Language | English |
| Published |
London
Springer-Verlag
26.07.2013
BioMed Central BioMed Central Ltd |
| Subjects | |
| Online Access | Get full text |
| ISSN | 1743-422X 1743-422X |
| DOI | 10.1186/1743-422X-10-244 |
Cover
Loading…
| Abstract | Influenza A and B viruses form different genera, which were originally distinguished by antigenic differences in their nucleoproteins and matrix 1 proteins. Cross-protection between these two genera has not been observed in animal experiments, which is consistent with the low homology in viral proteins common to both viruses except for one of three polymerase proteins, polymerase basic 1 (PB1). Recently, however, antibody and CD4⁺T cell epitopes conserved between the two genera were identified in humans. A protective antibody epitope was located in the stalk region of the surface glycoprotein, hemagglutinin, and a CD4⁺T cell epitope was located in the fusion peptide of the hemagglutinin. The fusion peptide was also found to contain antibody epitopes in humans and animals. A short stretch of well-conserved peptide was also identified in the other surface glycoprotein, neuraminidase, and antibodies binding to this peptide were generated by peptide immunization in rabbits. Although PB1, the only protein which has relatively high overall sequence homology between influenza A and B viruses, is not considered an immunodominant protein in the T cell responses to influenza A virus infection, amino acid sequence comparisons show that a considerable number of previously identified T cell epitopes in the PB1 of influenza A viruses are conserved in the PB1 of influenza B viruses. These data indicate that B and T cell cross-reactivity exists between influenza A and B viruses, which may have modulatory effects on the disease process and recovery. Although the antibody titers and the specific T cell frequencies induced by natural infection or standard vaccination may not be high enough to provide cross protection in humans, it might be possible to develop immunization strategies to induce these cross-reactive responses more efficiently. |
|---|---|
| AbstractList | Doc number: 244 Abstract: Influenza A and B viruses form different genera, which were originally distinguished by antigenic differences in their nucleoproteins and matrix 1 proteins. Cross-protection between these two genera has not been observed in animal experiments, which is consistent with the low homology in viral proteins common to both viruses except for one of three polymerase proteins, polymerase basic 1 (PB1). Recently, however, antibody and CD4+ T cell epitopes conserved between the two genera were identified in humans. A protective antibody epitope was located in the stalk region of the surface glycoprotein, hemagglutinin, and a CD4+ T cell epitope was located in the fusion peptide of the hemagglutinin. The fusion peptide was also found to contain antibody epitopes in humans and animals. A short stretch of well-conserved peptide was also identified in the other surface glycoprotein, neuraminidase, and antibodies binding to this peptide were generated by peptide immunization in rabbits. Although PB1, the only protein which has relatively high overall sequence homology between influenza A and B viruses, is not considered an immunodominant protein in the T cell responses to influenza A virus infection, amino acid sequence comparisons show that a considerable number of previously identified T cell epitopes in the PB1 of influenza A viruses are conserved in the PB1 of influenza B viruses. These data indicate that B and T cell cross-reactivity exists between influenza A and B viruses, which may have modulatory effects on the disease process and recovery. Although the antibody titers and the specific T cell frequencies induced by natural infection or standard vaccination may not be high enough to provide cross protection in humans, it might be possible to develop immunization strategies to induce these cross-reactive responses more efficiently. Influenza A and B viruses form different genera, which were originally distinguished by antigenic differences in their nucleoproteins and matrix 1 proteins. Cross-protection between these two genera has not been observed in animal experiments, which is consistent with the low homology in viral proteins common to both viruses except for one of three polymerase proteins, polymerase basic 1 (PB1). Recently, however, antibody and CD4+ T cell epitopes conserved between the two genera were identified in humans. A protective antibody epitope was located in the stalk region of the surface glycoprotein, hemagglutinin, and a CD4+ T cell epitope was located in the fusion peptide of the hemagglutinin. The fusion peptide was also found to contain antibody epitopes in humans and animals. A short stretch of well-conserved peptide was also identified in the other surface glycoprotein, neuraminidase, and antibodies binding to this peptide were generated by peptide immunization in rabbits. Although PB1, the only protein which has relatively high overall sequence homology between influenza A and B viruses, is not considered an immunodominant protein in the T cell responses to influenza A virus infection, amino acid sequence comparisons show that a considerable number of previously identified T cell epitopes in the PB1 of influenza A viruses are conserved in the PB1 of influenza B viruses. These data indicate that B and T cell cross-reactivity exists between influenza A and B viruses, which may have modulatory effects on the disease process and recovery. Although the antibody titers and the specific T cell frequencies induced by natural infection or standard vaccination may not be high enough to provide cross protection in humans, it might be possible to develop immunization strategies to induce these cross-reactive responses more efficiently. Influenza A and B viruses form different genera, which were originally distinguished by antigenic differences in their nucleoproteins and matrix 1 proteins. Cross-protection between these two genera has not been observed in animal experiments, which is consistent with the low homology in viral proteins common to both viruses except for one of three polymerase proteins, polymerase basic 1 (PB1). Recently, however, antibody and CD4.sup.+ T cell epitopes conserved between the two genera were identified in humans. A protective antibody epitope was located in the stalk region of the surface glycoprotein, hemagglutinin, and a CD4.sup.+ T cell epitope was located in the fusion peptide of the hemagglutinin. The fusion peptide was also found to contain antibody epitopes in humans and animals. A short stretch of well-conserved peptide was also identified in the other surface glycoprotein, neuraminidase, and antibodies binding to this peptide were generated by peptide immunization in rabbits. Although PB1, the only protein which has relatively high overall sequence homology between influenza A and B viruses, is not considered an immunodominant protein in the T cell responses to influenza A virus infection, amino acid sequence comparisons show that a considerable number of previously identified T cell epitopes in the PB1 of influenza A viruses are conserved in the PB1 of influenza B viruses. These data indicate that B and T cell cross-reactivity exists between influenza A and B viruses, which may have modulatory effects on the disease process and recovery. Although the antibody titers and the specific T cell frequencies induced by natural infection or standard vaccination may not be high enough to provide cross protection in humans, it might be possible to develop immunization strategies to induce these cross-reactive responses more efficiently. Keywords: Influenza A virus, Influenza B virus, Cross-reactive B cell epitopes, Cross-reactive T cell epitopes, Hemagglutinin, Fusion peptide, Neuraminidase, Polymerase basic 1 Influenza A and B viruses form different genera, which were originally distinguished by antigenic differences in their nucleoproteins and matrix 1 proteins. Cross-protection between these two genera has not been observed in animal experiments, which is consistent with the low homology in viral proteins common to both viruses except for one of three polymerase proteins, polymerase basic 1 (PB1). Recently, however, antibody and CD4⁺T cell epitopes conserved between the two genera were identified in humans. A protective antibody epitope was located in the stalk region of the surface glycoprotein, hemagglutinin, and a CD4⁺T cell epitope was located in the fusion peptide of the hemagglutinin. The fusion peptide was also found to contain antibody epitopes in humans and animals. A short stretch of well-conserved peptide was also identified in the other surface glycoprotein, neuraminidase, and antibodies binding to this peptide were generated by peptide immunization in rabbits. Although PB1, the only protein which has relatively high overall sequence homology between influenza A and B viruses, is not considered an immunodominant protein in the T cell responses to influenza A virus infection, amino acid sequence comparisons show that a considerable number of previously identified T cell epitopes in the PB1 of influenza A viruses are conserved in the PB1 of influenza B viruses. These data indicate that B and T cell cross-reactivity exists between influenza A and B viruses, which may have modulatory effects on the disease process and recovery. Although the antibody titers and the specific T cell frequencies induced by natural infection or standard vaccination may not be high enough to provide cross protection in humans, it might be possible to develop immunization strategies to induce these cross-reactive responses more efficiently. Influenza A and B viruses form different genera, which were originally distinguished by antigenic differences in their nucleoproteins and matrix 1 proteins. Cross-protection between these two genera has not been observed in animal experiments, which is consistent with the low homology in viral proteins common to both viruses except for one of three polymerase proteins, polymerase basic 1 (PB1). Recently, however, antibody and CD4.sup.+ T cell epitopes conserved between the two genera were identified in humans. A protective antibody epitope was located in the stalk region of the surface glycoprotein, hemagglutinin, and a CD4.sup.+ T cell epitope was located in the fusion peptide of the hemagglutinin. The fusion peptide was also found to contain antibody epitopes in humans and animals. A short stretch of well-conserved peptide was also identified in the other surface glycoprotein, neuraminidase, and antibodies binding to this peptide were generated by peptide immunization in rabbits. Although PB1, the only protein which has relatively high overall sequence homology between influenza A and B viruses, is not considered an immunodominant protein in the T cell responses to influenza A virus infection, amino acid sequence comparisons show that a considerable number of previously identified T cell epitopes in the PB1 of influenza A viruses are conserved in the PB1 of influenza B viruses. These data indicate that B and T cell cross-reactivity exists between influenza A and B viruses, which may have modulatory effects on the disease process and recovery. Although the antibody titers and the specific T cell frequencies induced by natural infection or standard vaccination may not be high enough to provide cross protection in humans, it might be possible to develop immunization strategies to induce these cross-reactive responses more efficiently. Influenza A and B viruses form different genera, which were originally distinguished by antigenic differences in their nucleoproteins and matrix 1 proteins. Cross-protection between these two genera has not been observed in animal experiments, which is consistent with the low homology in viral proteins common to both viruses except for one of three polymerase proteins, polymerase basic 1 (PB1). Recently, however, antibody and CD4 super(+) T cell epitopes conserved between the two genera were identified in humans. A protective antibody epitope was located in the stalk region of the surface glycoprotein, hemagglutinin, and a CD4 super(+) T cell epitope was located in the fusion peptide of the hemagglutinin. The fusion peptide was also found to contain antibody epitopes in humans and animals. A short stretch of well-conserved peptide was also identified in the other surface glycoprotein, neuraminidase, and antibodies binding to this peptide were generated by peptide immunization in rabbits. Although PB1, the only protein which has relatively high overall sequence homology between influenza A and B viruses, is not considered an immunodominant protein in the T cell responses to influenza A virus infection, amino acid sequence comparisons show that a considerable number of previously identified T cell epitopes in the PB1 of influenza A viruses are conserved in the PB1 of influenza B viruses. These data indicate that B and T cell cross-reactivity exists between influenza A and B viruses, which may have modulatory effects on the disease process and recovery. Although the antibody titers and the specific T cell frequencies induced by natural infection or standard vaccination may not be high enough to provide cross protection in humans, it might be possible to develop immunization strategies to induce these cross-reactive responses more efficiently. Influenza A and B viruses form different genera, which were originally distinguished by antigenic differences in their nucleoproteins and matrix 1 proteins. Cross-protection between these two genera has not been observed in animal experiments, which is consistent with the low homology in viral proteins common to both viruses except for one of three polymerase proteins, polymerase basic 1 (PB1). Recently, however, antibody and CD4⁺ T cell epitopes conserved between the two genera were identified in humans. A protective antibody epitope was located in the stalk region of the surface glycoprotein, hemagglutinin, and a CD4⁺ T cell epitope was located in the fusion peptide of the hemagglutinin. The fusion peptide was also found to contain antibody epitopes in humans and animals. A short stretch of well-conserved peptide was also identified in the other surface glycoprotein, neuraminidase, and antibodies binding to this peptide were generated by peptide immunization in rabbits. Although PB1, the only protein which has relatively high overall sequence homology between influenza A and B viruses, is not considered an immunodominant protein in the T cell responses to influenza A virus infection, amino acid sequence comparisons show that a considerable number of previously identified T cell epitopes in the PB1 of influenza A viruses are conserved in the PB1 of influenza B viruses. These data indicate that B and T cell cross-reactivity exists between influenza A and B viruses, which may have modulatory effects on the disease process and recovery. Although the antibody titers and the specific T cell frequencies induced by natural infection or standard vaccination may not be high enough to provide cross protection in humans, it might be possible to develop immunization strategies to induce these cross-reactive responses more efficiently. Influenza A and B viruses form different genera, which were originally distinguished by antigenic differences in their nucleoproteins and matrix 1 proteins. Cross-protection between these two genera has not been observed in animal experiments, which is consistent with the low homology in viral proteins common to both viruses except for one of three polymerase proteins, polymerase basic 1 (PB1). Recently, however, antibody and CD4 + T cell epitopes conserved between the two genera were identified in humans. A protective antibody epitope was located in the stalk region of the surface glycoprotein, hemagglutinin, and a CD4 + T cell epitope was located in the fusion peptide of the hemagglutinin. The fusion peptide was also found to contain antibody epitopes in humans and animals. A short stretch of well-conserved peptide was also identified in the other surface glycoprotein, neuraminidase, and antibodies binding to this peptide were generated by peptide immunization in rabbits. Although PB1, the only protein which has relatively high overall sequence homology between influenza A and B viruses, is not considered an immunodominant protein in the T cell responses to influenza A virus infection, amino acid sequence comparisons show that a considerable number of previously identified T cell epitopes in the PB1 of influenza A viruses are conserved in the PB1 of influenza B viruses. These data indicate that B and T cell cross-reactivity exists between influenza A and B viruses, which may have modulatory effects on the disease process and recovery. Although the antibody titers and the specific T cell frequencies induced by natural infection or standard vaccination may not be high enough to provide cross protection in humans, it might be possible to develop immunization strategies to induce these cross-reactive responses more efficiently. Influenza A and B viruses form different genera, which were originally distinguished by antigenic differences in their nucleoproteins and matrix 1 proteins. Cross-protection between these two genera has not been observed in animal experiments, which is consistent with the low homology in viral proteins common to both viruses except for one of three polymerase proteins, polymerase basic 1 (PB1). Recently, however, antibody and CD4+ T cell epitopes conserved between the two genera were identified in humans. A protective antibody epitope was located in the stalk region of the surface glycoprotein, hemagglutinin, and a CD4+ T cell epitope was located in the fusion peptide of the hemagglutinin. The fusion peptide was also found to contain antibody epitopes in humans and animals. A short stretch of well-conserved peptide was also identified in the other surface glycoprotein, neuraminidase, and antibodies binding to this peptide were generated by peptide immunization in rabbits. Although PB1, the only protein which has relatively high overall sequence homology between influenza A and B viruses, is not considered an immunodominant protein in the T cell responses to influenza A virus infection, amino acid sequence comparisons show that a considerable number of previously identified T cell epitopes in the PB1 of influenza A viruses are conserved in the PB1 of influenza B viruses. These data indicate that B and T cell cross-reactivity exists between influenza A and B viruses, which may have modulatory effects on the disease process and recovery. Although the antibody titers and the specific T cell frequencies induced by natural infection or standard vaccination may not be high enough to provide cross protection in humans, it might be possible to develop immunization strategies to induce these cross-reactive responses more efficiently.Influenza A and B viruses form different genera, which were originally distinguished by antigenic differences in their nucleoproteins and matrix 1 proteins. Cross-protection between these two genera has not been observed in animal experiments, which is consistent with the low homology in viral proteins common to both viruses except for one of three polymerase proteins, polymerase basic 1 (PB1). Recently, however, antibody and CD4+ T cell epitopes conserved between the two genera were identified in humans. A protective antibody epitope was located in the stalk region of the surface glycoprotein, hemagglutinin, and a CD4+ T cell epitope was located in the fusion peptide of the hemagglutinin. The fusion peptide was also found to contain antibody epitopes in humans and animals. A short stretch of well-conserved peptide was also identified in the other surface glycoprotein, neuraminidase, and antibodies binding to this peptide were generated by peptide immunization in rabbits. Although PB1, the only protein which has relatively high overall sequence homology between influenza A and B viruses, is not considered an immunodominant protein in the T cell responses to influenza A virus infection, amino acid sequence comparisons show that a considerable number of previously identified T cell epitopes in the PB1 of influenza A viruses are conserved in the PB1 of influenza B viruses. These data indicate that B and T cell cross-reactivity exists between influenza A and B viruses, which may have modulatory effects on the disease process and recovery. Although the antibody titers and the specific T cell frequencies induced by natural infection or standard vaccination may not be high enough to provide cross protection in humans, it might be possible to develop immunization strategies to induce these cross-reactive responses more efficiently. |
| ArticleNumber | 244 |
| Audience | Academic |
| Author | Co, Mary Dawn T Babon, Jenny Aurielle B Terajima, Masanori Ennis, Francis A |
| AuthorAffiliation | 2 Division of Diabetes, Department of Medicine, University of Massachusetts Medical School, Worcester, MA, USA 1 Division of Infectious Diseases and Immunology, Department of Medicine, University of Massachusetts Medical School, 55 Lake Avenue North, Worcester, MA 01655, USA |
| AuthorAffiliation_xml | – name: 1 Division of Infectious Diseases and Immunology, Department of Medicine, University of Massachusetts Medical School, 55 Lake Avenue North, Worcester, MA 01655, USA – name: 2 Division of Diabetes, Department of Medicine, University of Massachusetts Medical School, Worcester, MA, USA |
| Author_xml | – sequence: 1 fullname: Terajima, Masanori – sequence: 2 fullname: Babon, Jenny Aurielle B – sequence: 3 fullname: Co, Mary Dawn T – sequence: 4 fullname: Ennis, Francis A |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/23886073$$D View this record in MEDLINE/PubMed |
| BookMark | eNqNkktv1DAUhSNURB-wZwWR2MAixa_YyQZpOuJRqRKCthI7y3Fupq4Se7CT4fHrcUhbJlWLKi98ZX_nyD737ic71llIkucYHWJc8LdYMJoxQr5lGGWEsUfJ3s3Rzla9m-yHcIkQJVyUT5JdQouCI0H3ki9L70LIPCjdmw2kF0OnbHqUamjbVNk6PZtKWJverSGkFfQ_AGxqbNMOYH-rdPGXO0o3xg8BwtPkcaPaAM-u9oPk_MP7s-Wn7OTzx-Pl4iSrBBZ9BgyqouJ5rUiT5xoLXhSsyVWtEVRlrnVJalzTWPNG0Aa0piXNS8xB4JwoSg-Sd5Pveqg6qDXY3qtWrr3plP8lnTJyfmPNhVy5jaSC8ByLaLCcDCrj7jGY32jXyTFSOUYqMZIx8ejy-uoZ3n0fIPSyM2GMTFlwQ4iCnDKcC_QAlOGSckrIg1DOS1ogHNFXt9BLN3gbox8pQVCJRfGPWqkWZGyei1_So6lcxAfykjE2eh3eQcVVQ2d0nL3GxPOZ4M1MEJkefvYrNYQgj0-_ztkX2w27Cfp6GCPAJ0CPM-mhkdr0qjdujN-0Y-Lj1N_VA3RLeO39HwmeJCGidgV-K7X7NS8nTaOcVCtvgjw_JQjnCBFcRJr-AbAAGLs |
| CitedBy_id | crossref_primary_10_1016_j_vaccine_2015_01_070 crossref_primary_10_1093_infdis_jiv181 crossref_primary_10_7554_eLife_91849_3 crossref_primary_10_1056_NEJMc1400874 crossref_primary_10_3389_fimmu_2018_00116 crossref_primary_10_1093_infdis_jiv260 crossref_primary_10_3389_fcimb_2017_00307 crossref_primary_10_1016_j_jtbi_2016_11_008 crossref_primary_10_1155_2018_3143189 crossref_primary_10_3390_v14061172 crossref_primary_10_3390_vaccines7040169 crossref_primary_10_1016_j_vaccine_2021_06_072 crossref_primary_10_1073_pnas_1911083116 crossref_primary_10_1073_pnas_2012327118 crossref_primary_10_3390_vaccines12010095 crossref_primary_10_1016_j_clim_2014_08_003 crossref_primary_10_1073_pnas_2111064119 crossref_primary_10_1021_acssynbio_9b00111 crossref_primary_10_1098_rspb_2021_2358 crossref_primary_10_18527_2500_2236_2016_3_1_1_12 crossref_primary_10_1093_infdis_jiy184 crossref_primary_10_1016_j_clim_2016_03_008 crossref_primary_10_18527_2024117079 crossref_primary_10_3390_v12091013 crossref_primary_10_18527_2500_2236_2020_7_1_24_33 crossref_primary_10_3390_v14061323 crossref_primary_10_1371_journal_pone_0191574 crossref_primary_10_2217_fmb_15_120 crossref_primary_10_3389_fcimb_2019_00344 crossref_primary_10_1038_s41590_019_0320_6 crossref_primary_10_1093_aje_kwy145 crossref_primary_10_3390_pathogens13020097 crossref_primary_10_1093_infdis_jiaa268 crossref_primary_10_1093_infdis_jiab532 crossref_primary_10_1128_JVI_01883_18 crossref_primary_10_3389_fpubh_2022_825645 crossref_primary_10_3390_vaccines6020018 crossref_primary_10_7554_eLife_91849 crossref_primary_10_18527_2500_2236_2016_3_1_31_41 |
| Cites_doi | 10.2174/092986609788681715 10.1073/pnas.1218509110 10.1126/science.1222908 10.4149/av_2012_03_169 10.1016/j.vaccine.2008.09.015 10.1016/j.micinf.2008.07.002 10.1073/pnas.1116200109 10.1016/j.humimm.2010.02.014 10.1038/nm.2612 10.1016/j.vaccine.2012.10.039 10.1586/erv.10.123 10.1128/JVI.01047-08 10.1073/pnas.80.3.840 10.1016/j.chroma.2006.04.003 10.1128/JVI.02165-08 10.1073/pnas.79.15.4800 10.1073/pnas.1007465107 10.1038/nm1210-1389 10.1128/JVI.73.3.2136-2142.1999 10.1186/1471-2148-8-172 10.1371/journal.pone.0058810 10.1073/pnas.1008672107 10.1016/j.vaccine.2009.10.103 10.1111/j.1365-3083.2007.02042.x 10.1021/ac0621120 10.1371/journal.pone.0043603 10.4049/jimmunol.151.11.5930 10.1016/j.bbrc.2010.11.030 10.1016/S1074-7613(01)00139-X 10.1016/j.antiviral.2013.03.021 10.1126/science.1192517 10.1016/0042-6822(89)90615-6 10.1128/mBio.00018-10 10.1016/j.vaccine.2006.12.038 10.1002/rmv.1713 10.1128/JVI.67.6.2972-2980.1993 10.1128/JB.89.1.170-174.1965 10.1093/infdis/jis652 10.4049/jimmunol.160.7.3363 10.1016/0042-6822(86)90378-8 10.1016/j.humimm.2009.06.004 10.1128/JVI.06325-11 10.1002/eji.200737254 10.4049/jimmunol.158.3.1222 10.1099/vir.0.026187-0 10.1128/JVI.2.7.761-762.1968 10.1093/oxfordjournals.molbev.a004105 10.1073/pnas.0609330104 10.1128/JVI.00147-12 10.1186/1743-422X-7-351 10.1371/journal.pone.0001190 10.1007/s002510050594 10.1172/JCI63689 10.1093/cid/cir121 10.1172/JCI65208 10.1128/JVI.01563-08 10.1016/j.vaccine.2010.06.075 10.4149/av_2011_01_61 10.1128/MMBR.56.1.152-179.1992 10.1016/S0198-8859(00)00105-1 10.1016/S1534-5807(03)00190-4 |
| ContentType | Journal Article |
| Copyright | Terajima et al.; licensee BioMed Central Ltd. 2013 COPYRIGHT 2013 BioMed Central Ltd. 2013 Terajima et al.; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Copyright ©2013 Terajima et al.; licensee BioMed Central Ltd. 2013 Terajima et al.; licensee BioMed Central Ltd. |
| Copyright_xml | – notice: Terajima et al.; licensee BioMed Central Ltd. 2013 – notice: COPYRIGHT 2013 BioMed Central Ltd. – notice: 2013 Terajima et al.; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. – notice: Copyright ©2013 Terajima et al.; licensee BioMed Central Ltd. 2013 Terajima et al.; licensee BioMed Central Ltd. |
| DBID | FBQ C6C AAYXX CITATION CGR CUY CVF ECM EIF NPM ISR 3V. 7U9 7X7 7XB 88E 8FI 8FJ 8FK ABUWG AFKRA AZQEC BENPR CCPQU DWQXO FYUFA GHDGH H94 K9. M0S M1P PHGZM PHGZT PIMPY PJZUB PKEHL PPXIY PQEST PQQKQ PQUKI PRINS 7X8 7S9 L.6 5PM |
| DOI | 10.1186/1743-422X-10-244 |
| DatabaseName | AGRIS Springer Nature OA Free Journals CrossRef Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed Gale In Context: Science ProQuest Central (Corporate) Virology and AIDS Abstracts Health & Medical Collection ProQuest Central (purchase pre-March 2016) Medical Database (Alumni Edition) Hospital Premium Collection Hospital Premium Collection (Alumni Edition) ProQuest Central (Alumni) (purchase pre-March 2016) ProQuest Central (Alumni) ProQuest Central UK/Ireland ProQuest Central Essentials ProQuest Central ProQuest One ProQuest Central Health Research Premium Collection Health Research Premium Collection (Alumni) AIDS and Cancer Research Abstracts ProQuest Health & Medical Complete (Alumni) ProQuest Health & Medical Collection Medical Database ProQuest Central Premium ProQuest One Academic (New) Publicly Available Content Database ProQuest Health & Medical Research Collection ProQuest One Academic Middle East (New) ProQuest One Health & Nursing ProQuest One Academic Eastern Edition (DO NOT USE) ProQuest One Academic ProQuest One Academic UKI Edition ProQuest Central China MEDLINE - Academic AGRICOLA AGRICOLA - Academic PubMed Central (Full Participant titles) |
| DatabaseTitle | CrossRef MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) Publicly Available Content Database ProQuest One Academic Middle East (New) ProQuest Central Essentials ProQuest Health & Medical Complete (Alumni) ProQuest Central (Alumni Edition) ProQuest One Community College ProQuest One Health & Nursing ProQuest Central China ProQuest Central Health Research Premium Collection Health and Medicine Complete (Alumni Edition) ProQuest Central Korea Health & Medical Research Collection AIDS and Cancer Research Abstracts ProQuest Central (New) ProQuest Medical Library (Alumni) Virology and AIDS Abstracts ProQuest One Academic Eastern Edition ProQuest Hospital Collection Health Research Premium Collection (Alumni) ProQuest Hospital Collection (Alumni) ProQuest Health & Medical Complete ProQuest Medical Library ProQuest One Academic UKI Edition ProQuest One Academic ProQuest One Academic (New) ProQuest Central (Alumni) MEDLINE - Academic AGRICOLA AGRICOLA - Academic |
| DatabaseTitleList | Publicly Available Content Database MEDLINE AIDS and Cancer Research Abstracts AGRICOLA MEDLINE - Academic |
| Database_xml | – sequence: 1 dbid: C6C name: Springer Nature OA Free Journals url: http://www.springeropen.com/ sourceTypes: Publisher – sequence: 2 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 3 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database – sequence: 4 dbid: BENPR name: ProQuest Central url: https://www.proquest.com/central sourceTypes: Aggregation Database – sequence: 5 dbid: FBQ name: AGRIS url: http://www.fao.org/agris/Centre.asp?Menu_1ID=DB&Menu_2ID=DB1&Language=EN&Content=http://www.fao.org/agris/search?Language=EN sourceTypes: Publisher |
| DeliveryMethod | fulltext_linktorsrc |
| Discipline | Medicine Biology |
| EISSN | 1743-422X |
| EndPage | 244 |
| ExternalDocumentID | PMC3726517 oai_biomedcentral_com_1743_422X_10_244 3035596071 A534694441 23886073 10_1186_1743_422X_10_244 US201500218743 |
| Genre | Journal Article Review Research Support, N.I.H., Extramural |
| GrantInformation_xml | – fundername: NIAID NIH HHS grantid: U19 AI-057319 |
| GroupedDBID | --- -A0 123 29Q 2VQ 2WC 3V. 4.4 53G 5VS 7X7 88E 8FI 8FJ AAFWJ AAJSJ ABDBF ABPTK ABUWG ABVAZ ACGFO ACGFS ACIHN ACPRK ACRMQ ADBBV ADINQ ADRAZ AEAQA AENEX AFGXO AFKRA AFNRJ AFPKN AHBYD AHMBA AHSBF AHYZX ALMA_UNASSIGNED_HOLDINGS AMKLP AMTXH AOIJS BAPOH BAWUL BCNDV BENPR BFQNJ BMC BPHCQ BVXVI C1A C24 C6C CCPQU CS3 DIK E3Z EAD EAP EAS EBD EBS EJD EMB EMK EMOBN ESX F5P FBQ FYUFA GROUPED_DOAJ GX1 HMCUK HYE IAO IFM IGS IHR INH INR IPNFZ ISR ITC KQ8 M1P M48 M~E NXXTH O5R O5S OK1 P2P PIMPY PQQKQ PROAC PSQYO RBZ RIG RNS ROL RPM RSV SBL SOJ SV3 TR2 TUS UKHRP WOQ WOW XSB 0R~ AAHBH AASML ACMJI ACUHS ADUKV EBLON H13 OVT PGMZT PHGZM PHGZT PJZUB PPXIY PUEGO AAYXX ALIPV CITATION CGR CUY CVF ECM EIF NPM PMFND 7U9 7XB 8FK AZQEC DWQXO H94 K9. PKEHL PQEST PQUKI PRINS 7X8 7S9 L.6 5PM |
| ID | FETCH-LOGICAL-b717t-e4eb8b65da2f55c176884f5adc0eb95cc92d1d3eb96f73fecc3935916e7152a33 |
| IEDL.DBID | M48 |
| ISSN | 1743-422X |
| IngestDate | Thu Aug 21 18:01:59 EDT 2025 Wed May 22 07:14:07 EDT 2024 Fri Sep 05 04:37:55 EDT 2025 Thu Sep 04 21:44:56 EDT 2025 Thu Sep 04 20:40:07 EDT 2025 Sun Sep 07 03:35:26 EDT 2025 Tue Jun 17 22:04:56 EDT 2025 Tue Jun 10 21:01:07 EDT 2025 Fri Jun 27 05:44:31 EDT 2025 Mon Jul 21 05:16:46 EDT 2025 Tue Jul 01 01:44:39 EDT 2025 Thu Apr 24 23:13:04 EDT 2025 Sat Sep 06 07:30:08 EDT 2025 Wed Dec 27 19:18:28 EST 2023 |
| IsDoiOpenAccess | true |
| IsOpenAccess | true |
| IsPeerReviewed | true |
| IsScholarly | true |
| Issue | 1 |
| Keywords | Cross-reactive T cell epitopes Influenza A virus Hemagglutinin Polymerase basic 1 Neuraminidase Influenza B virus Cross-reactive B cell epitopes Fusion peptide |
| Language | English |
| License | http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
| LinkModel | DirectLink |
| MergedId | FETCHMERGED-LOGICAL-b717t-e4eb8b65da2f55c176884f5adc0eb95cc92d1d3eb96f73fecc3935916e7152a33 |
| Notes | http://dx.doi.org/10.1186/1743-422X-10-244 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 ObjectType-Review-3 content type line 23 ObjectType-Article-2 ObjectType-Feature-1 |
| OpenAccessLink | https://www.proquest.com/docview/1417209178?pq-origsite=%requestingapplication% |
| PMID | 23886073 |
| PQID | 1417209178 |
| PQPubID | 55248 |
| PageCount | 1 |
| ParticipantIDs | pubmedcentral_primary_oai_pubmedcentral_nih_gov_3726517 biomedcentral_primary_oai_biomedcentral_com_1743_422X_10_244 proquest_miscellaneous_1753415704 proquest_miscellaneous_1419363224 proquest_miscellaneous_1416693801 proquest_journals_1417209178 gale_infotracmisc_A534694441 gale_infotracacademiconefile_A534694441 gale_incontextgauss_ISR_A534694441 pubmed_primary_23886073 crossref_citationtrail_10_1186_1743_422X_10_244 crossref_primary_10_1186_1743_422X_10_244 springer_journals_10_1186_1743_422X_10_244 fao_agris_US201500218743 |
| ProviderPackageCode | CITATION AAYXX |
| PublicationCentury | 2000 |
| PublicationDate | 2013-07-26 |
| PublicationDateYYYYMMDD | 2013-07-26 |
| PublicationDate_xml | – month: 07 year: 2013 text: 2013-07-26 day: 26 |
| PublicationDecade | 2010 |
| PublicationPlace | London |
| PublicationPlace_xml | – name: London – name: England |
| PublicationTitle | Virology journal |
| PublicationTitleAbbrev | Virol J |
| PublicationTitleAlternate | Virol J |
| PublicationYear | 2013 |
| Publisher | Springer-Verlag BioMed Central BioMed Central Ltd |
| Publisher_xml | – name: Springer-Verlag – name: BioMed Central – name: BioMed Central Ltd |
| References | X Liu (2230_CR34) 2013; 8 G Marcelin (2230_CR50) 2012; 22 M Wang (2230_CR60) 2007; 25 AT Heiny (2230_CR22) 2007; 2 M Yamashita (2230_CR6) 1989; 171 CJ Wei (2230_CR46) 2010; 329 PM Colman (2230_CR52) 1993; 67 G Bommakanti (2230_CR48) 2010; 107 N Prabhu (2230_CR30) 2009; 83 BT Edelson (2230_CR57) 2001; 14 V Garcia-Canas (2230_CR66) 2006; 1123 S Tong (2230_CR3) 2012; 109 GA Stoloff (2230_CR64) 2007; 37 M DiBrino (2230_CR62) 1993; 151 HH Bui (2230_CR23) 2007; 104 V Garcia-Canas (2230_CR67) 2007; 79 RG Webster (2230_CR8) 1992; 56 CD O'Donnell (2230_CR17) 2012; 86 M Terajima (2230_CR61) 2008; 82 J Janulikova (2230_CR33) 2012; 56 J Alexander (2230_CR70) 2010; 28 C Gianfrani (2230_CR39) 2000; 61 D Jackson (2230_CR13) 2011; 92 Z Stanekova (2230_CR32) 2011; 55 M Gammelin (2230_CR7) 1990; 7 M Krystal (2230_CR26) 1982; 79 AM Hashem (2230_CR31) 2010; 403 KK McKinstry (2230_CR36) 2012; 122 RL Atmar (2230_CR2) 2007 S Southwood (2230_CR59) 1998; 160 TM Wilkinson (2230_CR38) 2012; 18 JA Babon (2230_CR65) 2009; 70 KM Grebe (2230_CR24) 2008; 10 SL Epstein (2230_CR25) 2010; 9 C Dreyfus (2230_CR41) 2012; 337 S Chun (2230_CR27) 2008; 26 MS Miller (2230_CR45) 2013; 207 JA Babon (2230_CR35) 2012; 86 DM Eckert (2230_CR42) 2010; 107 ED Kilbourne (2230_CR53) 1968; 2 B Krossoy (2230_CR9) 1999; 73 Y Suzuki (2230_CR10) 2002; 19 X Zhu (2230_CR4) 2013; 110 FG Hayden (2230_CR5) 2002 Z Stanekova (2230_CR20) 2010; 7 S Kemdirim (2230_CR18) 1986; 152 KJ Cross (2230_CR28) 2009; 16 A Sette (2230_CR58) 1999; 50 SL Epstein (2230_CR16) 1997; 158 PC Doherty (2230_CR69) 2008; 118 JL Schulman (2230_CR15) 1965; 89 J Sui (2230_CR49) 2011; 52 KA Richards (2230_CR68) 2012; 31 J Steel (2230_CR47) 2010; 1 J Alexander (2230_CR55) 2010; 71 RWH Ruigrok (2230_CR14) 1998 LY Lee (2230_CR63) 2008; 118 NJ Cox (2230_CR1) 2000 JA Mould (2230_CR19) 2003; 5 JD O'Brien (2230_CR11) 2008; 8 MZ Atassi (2230_CR29) 1983; 80 F Krammer (2230_CR44) 2012; 7 E Kosor Krnic (2230_CR40) 2008; 67 NS Laursen (2230_CR21) 2013; 98 I Kosik (2230_CR56) 2012 P Palese (2230_CR12) 2007 GJ Nabel (2230_CR43) 2010; 16 K Boonnak (2230_CR37) 2012; 122 C Gravel (2230_CR51) 2010; 28 E Assarsson (2230_CR54) 2008; 82 7504010 - J Immunol. 1993 Dec 1;151(11):5930-5 20647428 - Science. 2010 Aug 27;329(5995):1060-4 23527030 - PLoS One. 2013;8(3):e58810 11371353 - Immunity. 2001 May;14(5):503-12 2763462 - Virology. 1989 Aug;171(2):458-66 21135852 - Nat Med. 2010 Dec;16(12):1389-91 9971796 - J Virol. 1999 Mar;73(3):2136-42 22820287 - J Clin Invest. 2012 Aug;122(8):2847-56 3754992 - Virology. 1986 Jul 15;152(1):126-35 20615991 - Proc Natl Acad Sci U S A. 2010 Aug 3;107(31):13701-6 6187004 - Proc Natl Acad Sci U S A. 1983 Feb;80(3):840-4 22878502 - Science. 2012 Sep 14;337(6100):1343-8 11919291 - Mol Biol Evol. 2002 Apr;19(4):501-9 17668898 - Eur J Immunol. 2007 Sep;37(9):2441-9 22820285 - J Clin Invest. 2012 Aug;122(8):2768-70 22371588 - Proc Natl Acad Sci U S A. 2012 Mar 13;109(11):4269-74 20926635 - J Gen Virol. 2011 Jan;92(Pt 1):1-17 17254671 - Vaccine. 2007 Apr 12;25(15):2823-31 18541033 - BMC Evol Biol. 2008;8:172 18842709 - J Virol. 2008 Dec;82(24):12241-51 22674976 - J Virol. 2012 Aug;86(16):8625-33 22294447 - Arch Virol. 2012 May;157(5):811-7 10773346 - Hum Immunol. 2000 May;61(5):438-52 19524006 - Hum Immunol. 2009 Sep;70(9):711-21 18614638 - J Virol. 2008 Sep;82(18):9283-7 9013963 - J Immunol. 1997 Feb 1;158(3):1222-30 19007587 - Vaccine. 2008 Nov 11;26(48):6068-76 9531296 - J Immunol. 1998 Apr 1;160(7):3363-73 20156506 - Hum Immunol. 2010 May;71(5):468-74 21118546 - Virol J. 2010;7:351 14255658 - J Bacteriol. 1965 Jan;89:170-4 23043596 - Acta Virol. 2012;56(3):169-76 20660754 - Proc Natl Acad Sci U S A. 2010 Aug 3;107(31):13563-4 21087110 - Expert Rev Vaccines. 2010 Nov;9(11):1325-41 23297216 - Proc Natl Acad Sci U S A. 2013 Jan 22;110(4):1458-63 18802496 - J Clin Invest. 2008 Oct;118(10):3478-90 22286307 - Nat Med. 2012 Feb;18(2):274-80 22718815 - J Virol. 2012 Sep;86(17):9233-43 18052968 - Scand J Immunol. 2008 Jan;67(1):86-94 6956892 - Proc Natl Acad Sci U S A. 1982 Aug;79(15):4800-4 19895924 - Vaccine. 2010 Jan 8;28(3):664-72 16677659 - J Chromatogr A. 2006 Aug 11;1123(2):225-32 23087428 - J Infect Dis. 2013 Jan 1;207(1):98-105 23099328 - Vaccine. 2012 Dec 17;31(1):219-25 18030326 - PLoS One. 2007;2(11):e1190 21460314 - Clin Infect Dis. 2011 Apr 15;52(8):1003-9 21434706 - Acta Virol. 2011;55(1):61-7 22438243 - Rev Med Virol. 2012 Jul;22(4):267-79 21078301 - Biochem Biophys Res Commun. 2010 Dec 10;403(2):247-51 17361989 - Anal Chem. 2007 Apr 15;79(8):3164-72 20621113 - Vaccine. 2010 Aug 16;28(36):5774-84 20689752 - MBio. 2010 May 18;1(1):null 10602880 - Immunogenetics. 1999 Nov;50(3-4):201-12 5723531 - J Virol. 1968 Jul;2(7):761-2 1579108 - Microbiol Rev. 1992 Mar;56(1):152-79 12852861 - Dev Cell. 2003 Jul;5(1):175-84 17200302 - Proc Natl Acad Sci U S A. 2007 Jan 2;104(1):246-51 18662798 - Microbes Infect. 2008 Jul;10(9):1024-9 23583287 - Antiviral Res. 2013 Jun;98(3):476-83 22928001 - PLoS One. 2012;7(8):e43603 18802488 - J Clin Invest. 2008 Oct;118(10):3273-5 8497041 - J Virol. 1993 Jun;67(6):2972-80 19601906 - Protein Pept Lett. 2009;16(7):766-78 19109379 - J Virol. 2009 Mar;83(6):2553-62 2319943 - Mol Biol Evol. 1990 Mar;7(2):194-200 |
| References_xml | – volume: 16 start-page: 766 year: 2009 ident: 2230_CR28 publication-title: Protein Pept Lett doi: 10.2174/092986609788681715 – volume: 110 start-page: 1458 year: 2013 ident: 2230_CR4 publication-title: Proc Natl Acad Sci U S A doi: 10.1073/pnas.1218509110 – volume: 337 start-page: 1343 year: 2012 ident: 2230_CR41 publication-title: Science doi: 10.1126/science.1222908 – volume: 56 start-page: 169 year: 2012 ident: 2230_CR33 publication-title: Acta Virol doi: 10.4149/av_2012_03_169 – volume: 26 start-page: 6068 year: 2008 ident: 2230_CR27 publication-title: Vaccine doi: 10.1016/j.vaccine.2008.09.015 – volume: 10 start-page: 1024 year: 2008 ident: 2230_CR24 publication-title: Microbes Infect doi: 10.1016/j.micinf.2008.07.002 – start-page: 585 volume-title: Virus Taxonomy Classification and Nomenclature of Viruses year: 2000 ident: 2230_CR1 – volume: 109 start-page: 4269 year: 2012 ident: 2230_CR3 publication-title: Proc Natl Acad Sci U S A doi: 10.1073/pnas.1116200109 – volume: 71 start-page: 468 year: 2010 ident: 2230_CR55 publication-title: Hum Immunol doi: 10.1016/j.humimm.2010.02.014 – start-page: 1648 volume-title: Fields Virology year: 2007 ident: 2230_CR12 – volume: 18 start-page: 274 year: 2012 ident: 2230_CR38 publication-title: Nat Med doi: 10.1038/nm.2612 – volume: 31 start-page: 219 year: 2012 ident: 2230_CR68 publication-title: Vaccine doi: 10.1016/j.vaccine.2012.10.039 – volume: 9 start-page: 1325 year: 2010 ident: 2230_CR25 publication-title: Expert Rev Vaccines doi: 10.1586/erv.10.123 – volume: 82 start-page: 9283 year: 2008 ident: 2230_CR61 publication-title: J Virol doi: 10.1128/JVI.01047-08 – volume: 80 start-page: 840 year: 1983 ident: 2230_CR29 publication-title: Proc Natl Acad Sci U S A doi: 10.1073/pnas.80.3.840 – volume: 1123 start-page: 225 year: 2006 ident: 2230_CR66 publication-title: J Chromatogr A doi: 10.1016/j.chroma.2006.04.003 – volume: 83 start-page: 2553 year: 2009 ident: 2230_CR30 publication-title: J Virol doi: 10.1128/JVI.02165-08 – volume: 79 start-page: 4800 year: 1982 ident: 2230_CR26 publication-title: Proc Natl Acad Sci U S A doi: 10.1073/pnas.79.15.4800 – volume: 107 start-page: 13701 year: 2010 ident: 2230_CR48 publication-title: Proc Natl Acad Sci U S A doi: 10.1073/pnas.1007465107 – volume: 16 start-page: 1389 year: 2010 ident: 2230_CR43 publication-title: Nat Med doi: 10.1038/nm1210-1389 – volume: 73 start-page: 2136 year: 1999 ident: 2230_CR9 publication-title: J Virol doi: 10.1128/JVI.73.3.2136-2142.1999 – volume: 8 start-page: 172 year: 2008 ident: 2230_CR11 publication-title: BMC Evol Biol doi: 10.1186/1471-2148-8-172 – volume: 8 start-page: e58810 year: 2013 ident: 2230_CR34 publication-title: PLoS One doi: 10.1371/journal.pone.0058810 – volume: 107 start-page: 13563 year: 2010 ident: 2230_CR42 publication-title: Proc Natl Acad Sci U S A doi: 10.1073/pnas.1008672107 – volume: 28 start-page: 664 year: 2010 ident: 2230_CR70 publication-title: Vaccine doi: 10.1016/j.vaccine.2009.10.103 – volume-title: Arch Virol year: 2012 ident: 2230_CR56 – volume: 67 start-page: 86 year: 2008 ident: 2230_CR40 publication-title: Scand J Immunol doi: 10.1111/j.1365-3083.2007.02042.x – volume: 79 start-page: 3164 year: 2007 ident: 2230_CR67 publication-title: Anal Chem doi: 10.1021/ac0621120 – volume: 7 start-page: e43603 year: 2012 ident: 2230_CR44 publication-title: PLoS One doi: 10.1371/journal.pone.0043603 – volume: 151 start-page: 5930 year: 1993 ident: 2230_CR62 publication-title: J Immunol doi: 10.4049/jimmunol.151.11.5930 – volume: 403 start-page: 247 year: 2010 ident: 2230_CR31 publication-title: Biochem Biophys Res Commun doi: 10.1016/j.bbrc.2010.11.030 – volume: 14 start-page: 503 year: 2001 ident: 2230_CR57 publication-title: Immunity doi: 10.1016/S1074-7613(01)00139-X – start-page: 29 volume-title: Textbook of INFLUENZA year: 1998 ident: 2230_CR14 – volume: 98 start-page: 476 year: 2013 ident: 2230_CR21 publication-title: Antiviral Res doi: 10.1016/j.antiviral.2013.03.021 – volume: 329 start-page: 1060 year: 2010 ident: 2230_CR46 publication-title: Science doi: 10.1126/science.1192517 – volume: 118 start-page: 3478 year: 2008 ident: 2230_CR63 publication-title: J Clin Invest – volume: 7 start-page: 194 year: 1990 ident: 2230_CR7 publication-title: Mol Biol Evol – volume: 171 start-page: 458 year: 1989 ident: 2230_CR6 publication-title: Virology doi: 10.1016/0042-6822(89)90615-6 – volume: 1 start-page: e00018 year: 2010 ident: 2230_CR47 publication-title: MBio doi: 10.1128/mBio.00018-10 – volume: 118 start-page: 3273 year: 2008 ident: 2230_CR69 publication-title: J Clin Invest – volume: 25 start-page: 2823 year: 2007 ident: 2230_CR60 publication-title: Vaccine doi: 10.1016/j.vaccine.2006.12.038 – volume: 22 start-page: 267 year: 2012 ident: 2230_CR50 publication-title: Rev Med Virol doi: 10.1002/rmv.1713 – volume: 67 start-page: 2972 year: 1993 ident: 2230_CR52 publication-title: J Virol doi: 10.1128/JVI.67.6.2972-2980.1993 – volume: 89 start-page: 170 year: 1965 ident: 2230_CR15 publication-title: J Bacteriol doi: 10.1128/JB.89.1.170-174.1965 – volume: 207 start-page: 98 year: 2013 ident: 2230_CR45 publication-title: J Infect Dis doi: 10.1093/infdis/jis652 – volume: 160 start-page: 3363 year: 1998 ident: 2230_CR59 publication-title: J Immunol doi: 10.4049/jimmunol.160.7.3363 – volume: 152 start-page: 126 year: 1986 ident: 2230_CR18 publication-title: Virology doi: 10.1016/0042-6822(86)90378-8 – volume: 70 start-page: 711 year: 2009 ident: 2230_CR65 publication-title: Hum Immunol doi: 10.1016/j.humimm.2009.06.004 – volume: 86 start-page: 9233 year: 2012 ident: 2230_CR35 publication-title: J Virol doi: 10.1128/JVI.06325-11 – volume: 37 start-page: 2441 year: 2007 ident: 2230_CR64 publication-title: Eur J Immunol doi: 10.1002/eji.200737254 – volume: 158 start-page: 1222 year: 1997 ident: 2230_CR16 publication-title: J Immunol doi: 10.4049/jimmunol.158.3.1222 – start-page: 891 volume-title: Clinical Virology year: 2002 ident: 2230_CR5 – volume: 92 start-page: 1 year: 2011 ident: 2230_CR13 publication-title: J Gen Virol doi: 10.1099/vir.0.026187-0 – volume: 2 start-page: 761 year: 1968 ident: 2230_CR53 publication-title: J Virol doi: 10.1128/JVI.2.7.761-762.1968 – volume: 19 start-page: 501 year: 2002 ident: 2230_CR10 publication-title: Mol Biol Evol doi: 10.1093/oxfordjournals.molbev.a004105 – volume: 104 start-page: 246 year: 2007 ident: 2230_CR23 publication-title: Proc Natl Acad Sci U S A doi: 10.1073/pnas.0609330104 – volume: 86 start-page: 8625 year: 2012 ident: 2230_CR17 publication-title: J Virol doi: 10.1128/JVI.00147-12 – start-page: 1340 volume-title: Manual of Clinical Microbiology. Volume 2 year: 2007 ident: 2230_CR2 – volume: 7 start-page: 351 year: 2010 ident: 2230_CR20 publication-title: Virol J doi: 10.1186/1743-422X-7-351 – volume: 2 start-page: e1190 year: 2007 ident: 2230_CR22 publication-title: PLoS ONE doi: 10.1371/journal.pone.0001190 – volume: 50 start-page: 201 year: 1999 ident: 2230_CR58 publication-title: Immunogenetics doi: 10.1007/s002510050594 – volume: 122 start-page: 2847 year: 2012 ident: 2230_CR36 publication-title: J Clin Invest doi: 10.1172/JCI63689 – volume: 52 start-page: 1003 year: 2011 ident: 2230_CR49 publication-title: Clin Infect Dis doi: 10.1093/cid/cir121 – volume: 122 start-page: 2768 year: 2012 ident: 2230_CR37 publication-title: J Clin Invest doi: 10.1172/JCI65208 – volume: 82 start-page: 12241 year: 2008 ident: 2230_CR54 publication-title: J Virol doi: 10.1128/JVI.01563-08 – volume: 28 start-page: 5774 year: 2010 ident: 2230_CR51 publication-title: Vaccine doi: 10.1016/j.vaccine.2010.06.075 – volume: 55 start-page: 61 year: 2011 ident: 2230_CR32 publication-title: Acta Virol doi: 10.4149/av_2011_01_61 – volume: 56 start-page: 152 year: 1992 ident: 2230_CR8 publication-title: Microbiol Rev doi: 10.1128/MMBR.56.1.152-179.1992 – volume: 61 start-page: 438 year: 2000 ident: 2230_CR39 publication-title: Hum Immunol doi: 10.1016/S0198-8859(00)00105-1 – volume: 5 start-page: 175 year: 2003 ident: 2230_CR19 publication-title: Dev Cell doi: 10.1016/S1534-5807(03)00190-4 – reference: 20926635 - J Gen Virol. 2011 Jan;92(Pt 1):1-17 – reference: 23043596 - Acta Virol. 2012;56(3):169-76 – reference: 23297216 - Proc Natl Acad Sci U S A. 2013 Jan 22;110(4):1458-63 – reference: 22820287 - J Clin Invest. 2012 Aug;122(8):2847-56 – reference: 19601906 - Protein Pept Lett. 2009;16(7):766-78 – reference: 12852861 - Dev Cell. 2003 Jul;5(1):175-84 – reference: 5723531 - J Virol. 1968 Jul;2(7):761-2 – reference: 18030326 - PLoS One. 2007;2(11):e1190 – reference: 21434706 - Acta Virol. 2011;55(1):61-7 – reference: 20615991 - Proc Natl Acad Sci U S A. 2010 Aug 3;107(31):13701-6 – reference: 2319943 - Mol Biol Evol. 1990 Mar;7(2):194-200 – reference: 23087428 - J Infect Dis. 2013 Jan 1;207(1):98-105 – reference: 9971796 - J Virol. 1999 Mar;73(3):2136-42 – reference: 20689752 - MBio. 2010 May 18;1(1):null – reference: 21460314 - Clin Infect Dis. 2011 Apr 15;52(8):1003-9 – reference: 21078301 - Biochem Biophys Res Commun. 2010 Dec 10;403(2):247-51 – reference: 18541033 - BMC Evol Biol. 2008;8:172 – reference: 20647428 - Science. 2010 Aug 27;329(5995):1060-4 – reference: 23527030 - PLoS One. 2013;8(3):e58810 – reference: 17254671 - Vaccine. 2007 Apr 12;25(15):2823-31 – reference: 18802496 - J Clin Invest. 2008 Oct;118(10):3478-90 – reference: 22878502 - Science. 2012 Sep 14;337(6100):1343-8 – reference: 2763462 - Virology. 1989 Aug;171(2):458-66 – reference: 20660754 - Proc Natl Acad Sci U S A. 2010 Aug 3;107(31):13563-4 – reference: 18802488 - J Clin Invest. 2008 Oct;118(10):3273-5 – reference: 18052968 - Scand J Immunol. 2008 Jan;67(1):86-94 – reference: 23583287 - Antiviral Res. 2013 Jun;98(3):476-83 – reference: 3754992 - Virology. 1986 Jul 15;152(1):126-35 – reference: 22820285 - J Clin Invest. 2012 Aug;122(8):2768-70 – reference: 22718815 - J Virol. 2012 Sep;86(17):9233-43 – reference: 19524006 - Hum Immunol. 2009 Sep;70(9):711-21 – reference: 1579108 - Microbiol Rev. 1992 Mar;56(1):152-79 – reference: 10602880 - Immunogenetics. 1999 Nov;50(3-4):201-12 – reference: 20621113 - Vaccine. 2010 Aug 16;28(36):5774-84 – reference: 21087110 - Expert Rev Vaccines. 2010 Nov;9(11):1325-41 – reference: 6187004 - Proc Natl Acad Sci U S A. 1983 Feb;80(3):840-4 – reference: 22928001 - PLoS One. 2012;7(8):e43603 – reference: 10773346 - Hum Immunol. 2000 May;61(5):438-52 – reference: 14255658 - J Bacteriol. 1965 Jan;89:170-4 – reference: 11371353 - Immunity. 2001 May;14(5):503-12 – reference: 22371588 - Proc Natl Acad Sci U S A. 2012 Mar 13;109(11):4269-74 – reference: 6956892 - Proc Natl Acad Sci U S A. 1982 Aug;79(15):4800-4 – reference: 22438243 - Rev Med Virol. 2012 Jul;22(4):267-79 – reference: 18662798 - Microbes Infect. 2008 Jul;10(9):1024-9 – reference: 9013963 - J Immunol. 1997 Feb 1;158(3):1222-30 – reference: 21118546 - Virol J. 2010;7:351 – reference: 20156506 - Hum Immunol. 2010 May;71(5):468-74 – reference: 16677659 - J Chromatogr A. 2006 Aug 11;1123(2):225-32 – reference: 19007587 - Vaccine. 2008 Nov 11;26(48):6068-76 – reference: 8497041 - J Virol. 1993 Jun;67(6):2972-80 – reference: 19895924 - Vaccine. 2010 Jan 8;28(3):664-72 – reference: 7504010 - J Immunol. 1993 Dec 1;151(11):5930-5 – reference: 19109379 - J Virol. 2009 Mar;83(6):2553-62 – reference: 17361989 - Anal Chem. 2007 Apr 15;79(8):3164-72 – reference: 23099328 - Vaccine. 2012 Dec 17;31(1):219-25 – reference: 17200302 - Proc Natl Acad Sci U S A. 2007 Jan 2;104(1):246-51 – reference: 11919291 - Mol Biol Evol. 2002 Apr;19(4):501-9 – reference: 22286307 - Nat Med. 2012 Feb;18(2):274-80 – reference: 21135852 - Nat Med. 2010 Dec;16(12):1389-91 – reference: 18842709 - J Virol. 2008 Dec;82(24):12241-51 – reference: 18614638 - J Virol. 2008 Sep;82(18):9283-7 – reference: 22294447 - Arch Virol. 2012 May;157(5):811-7 – reference: 22674976 - J Virol. 2012 Aug;86(16):8625-33 – reference: 17668898 - Eur J Immunol. 2007 Sep;37(9):2441-9 – reference: 9531296 - J Immunol. 1998 Apr 1;160(7):3363-73 |
| SSID | ssj0032679 |
| Score | 2.1873682 |
| SecondaryResourceType | review_article |
| Snippet | Influenza A and B viruses form different genera, which were originally distinguished by antigenic differences in their nucleoproteins and matrix 1 proteins.... Doc number: 244 Abstract: Influenza A and B viruses form different genera, which were originally distinguished by antigenic differences in their nucleoproteins... |
| SourceID | pubmedcentral biomedcentral proquest gale pubmed crossref springer fao |
| SourceType | Open Access Repository Aggregation Database Index Database Enrichment Source Publisher |
| StartPage | 244 |
| SubjectTerms | amino acid sequences animal experimentation antibodies B cells B-lymphocytes Biomedical and Life Sciences Biomedicine cross immunity cross reaction Cross Reactions Development and progression epitopes Epitopes, B-Lymphocyte - immunology Epitopes, T-Lymphocyte - immunology Genetic aspects glycoproteins Health aspects hemagglutinins Humans Infections Influenza Influenza A virus Influenza A virus - immunology Influenza B virus - immunology Influenza viruses Medical research Mortality nucleoproteins peptides Physiological aspects Prevention rabbits Review Risk factors sequence homology sialidase T cells T-lymphocytes vaccination Vaccines Viral proteins Viral Proteins - immunology Virology viruses |
| SummonAdditionalLinks | – databaseName: Health & Medical Collection dbid: 7X7 link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfV3faxQxEA62ovgiWrXdWiWKIArhLtlssguCXIulChW0Pbi3kM0m9aDsXbt3gv71TrLZs3vae1suX9jbzGTmm_yYQehNmTNe5s6RPKeWcE0ZKQpekooKyZiUVWF8oHj6VZyM-ZdJNokLbk08VtnZxGCoq5nxa-QDysHVgnOT-cf5FfFVo_zuaiyhsYXuhtRloM9ysgq4gJmEXHuedBPO2KTbpszFYPWbt0Pg4tbuu1_23NSW07N_TfYNn7V-nnJtUzX4quNH6GEkmXjUasVjdMfWO-heW3by1w66fxo31J-gb0f-9QSYY7B7OJTsw4fYr-djXVf4vH20c5j5c9vgeK4LT9viJr81HgXcIf45vV42tnmKxsefzo9OSKyyQEoI5RbEclvmpcgqzVyWGQrxR85dpisztGWRGVOwilYpPAsnUwciD7d5qbASfL9O02dou57Vdg9hTm2hqdMQsgw5dbKgprRAyIyrSmupS9CH3iCreZtRQ_kc1_0WEL3yMlJeRgoiFZBRggadTJSJGcx9IY1LFSKZXPynx7tVj-5dt2P3QMxKX4BxVeMz5peCPAECWIJee9krny-j9gdyLvSyadTns-9qlKVcFBxIZYLeRpCbwb8yOt5vgKHxKbZ6yIMeEia06Td3KqaiQWnUX_VP0KtVs-_pD8nVdrYMGCGKFDjHRkyRCrDifAMGQljgdXIImN1Ws1ejBwwvF-AWEiR7Ot8TZb-lnv4IactTyURGZYLed7PjxufdIpT9zWPxHD1goTyJJEwcoO3F9dK-AJK4KF8GS_AHitRfMw priority: 102 providerName: ProQuest – databaseName: Springer Nature OA Free Journals dbid: C6C link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwlV3da9swEBdrx8ZeytZ91Gs3tDEYG4hGsqwP2EsaVrpBB1sbyJuQbakLFCfUyWD963uS7RBnbWFvBv2EbZ3u9DuddIfQh1wxnivviVLUEW4pI1rznJRUSMakLHURHMXTH-JkzL9Pskm73xHuwqzH76kSh4EwE87YJNgLWIq20MOMpiKGZcWos7nAQaTugpC39Nq4zX7ZW4S2vJ39a5DXVqTN05IbIdO4Eh0_RTsthcTDRubP0ANX7aJHTVHJv7vo8WkbLn-Ofo7C6wnwwmjVcCzIh49w2K3HtirxefPo5qDXc1fj9tQWnjalS64tHkbcEf4zvVrWrn6Bxsdfz0cnpK2hQHJw1BbEcZerXGSlZT7LCgreheI-s2UxcLnOikKzkpYpPAsvUw8CjXd1qXASVnabpi_RdjWr3B7CnDptqbfgkAw49VLTIndAtwpf5s5Rn6AvvUE28yZfhgkZrPstoEwmyMgEGRnwQ0BGCTrsZGKKNj95KJNxaaKfosQtPT6tenTvuhu7B2I29gJMpxmfsbDRE-gNwBL0PsjehGwYVThuc2GXdW2-nf0ywyzlQnOgjAn62IL8DL6qsO3tBRiakECrhzzoIUFdi35zN8VMay5q8L-ARwJzkypB71bNoWc4Ale52TJihNApMIp7MRqUA2jZPRhwUIG1yQFgXjUzezV6wN-UAKOfINmb8z1R9luq6e-YlDyVTGRUJuhzpx1rv3eHUF7_D3gfPWGxFIkkTByg7cXV0r0BQrjI30ZbcAOxJFUG priority: 102 providerName: Springer Nature |
| Title | Cross-reactive human B cell and T cell epitopes between influenza A and B viruses |
| URI | https://link.springer.com/article/10.1186/1743-422X-10-244 https://www.ncbi.nlm.nih.gov/pubmed/23886073 https://www.proquest.com/docview/1417209178 https://www.proquest.com/docview/1416693801 https://www.proquest.com/docview/1419363224 https://www.proquest.com/docview/1753415704 http://dx.doi.org/10.1186/1743-422X-10-244 https://pubmed.ncbi.nlm.nih.gov/PMC3726517 |
| Volume | 10 |
| hasFullText | 1 |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfV1tb9MwELboJhBfEIyXZYzKICQEUljtOHYigVBbbRpInWBbpX6znMQelaq0a1rE-PWcnaQspd23VH7ctD7f3XN-uUPobRJRlkTG-FFEtM8UoX4cs8TPCBeUCpHFqQ0UB2f8dMi-jcLRv-vR1QAWG0M7W09qOJ98_H198wUU_rNT-IgfWVLtM0pH1qaAu2qhXfBL3IZiA7baUwCe4jLvrdD1puWGb1i7_T5pOK2WUdP_DfgtD7Z-unJti9V5rpPH6FFFOXG3nCNP0D2d76H7ZRHKmz30YFBtrz9FP_r29T7wSGcFsSvgh3vYru5jlWf4snzUM7ADM13g6pQXHpelTv4o3HW4Hv41ni8LXTxDw5Pjy_6pX9Vc8BMI7Ba-ZjqJEh5mipowTAlEIxEzocrSjk7iME1jmpEsgGduRGBgAri7vYRrAUxABcFztJNPc72PMCM6VsQoCGA6jBgRkzTRQM9SkyVaE-OhT41BlrMyv4a0Ga-bLaB80spIWhlJiFtARh46qmUi0yqfuS2rMZEuron4hh7vVz3qd23H7oOYpboCUyuHF9QuDFk6BDAPvbGylzZ7Rm6P51ypZVHIrxfnshsGjMcMKKaH3lUgM4VflarqtgMMjU241UAeNpCg3mmzuZ5istYOiNeAdwLTE5GHXq-abU97ZC7X06XDcB4HwEDuxMQBB5vO7sBAQAssT3QA86Kc2avRA74XcXASHhKNOd8QZbMlH_90ScwDQXlIhIc-1Npx6-9tEcrBdqG8RA-pK1QifMoP0c5ivtSvgC4ukjZqiZFoo93e8dn3c_jU5_22W3ppO_vwF93lY4g |
| linkProvider | Scholars Portal |
| linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwtV1bb9MwFLZGJy4vCMZlgQEGgRBIUWvHsRMJhNqxqWVrBVsr9c04iT0qTWlZWtD4UfxGjnMpS2F921sUHyuJz8l3vuPLOQi9jALKosAYNwiIdpki1A1DFrkJ4YJSIZIwtoFif8C7I_Zp7I830O_qLIzdVllhYg7UyTS2c-RNwsDVgnMTwYfZd9dWjbKrq1UJjcIsDvT5TwjZsve9j6DfV5Tu7w13u25ZVcCNIHSZu5rpKIi4nyhqfD8mwLcDZnyVxC0dhX4chzQhiQfX3AjPwCfmp1cJ1wJ8nbIToAD5m8yeaG2gzc7e4PNRhf3AhfLsfpbmu4zScbUwGvDm8p5FPnCqKyfsT2uO8ZpR03-dxAUvubqDc2UZN_eO-3fQ7ZLW4nZhh3fRhk630PWi0OX5FrrRL5fw76Evu_bxLnDVHGlxXiQQd7BdQcAqTfCwuNQzwJqZznC5kwxPinIqvxRu53Id_GNytsh0dh-NrkQDD1AjnaZ6G2FGdKiIURAktRgxIiRxpIECxiaJtCbGQe9qgyxnRQ4PabNq11vA2KTVkbQ6khAbgY4c1Kx0IuMyZ7ot3XEq89gp4P_p8WbZo3rW5bLboGapTgDO5eiY2sknS7lAzEEvrO6lzdCR2i1AJ2qRZbJ3fCTbvsd4yIDGOuh1KWSm8FaxKk9UwNDYpF41yZ2aJEBIXG-uTEyWEJbJvz-cg54vm21Puy0v1dNFLsN56AHLWSsTehz8BlsjA0EzMEnRApmHhWUvRw84ZcDBETlI1Gy-psp6Szr5lidK9wTlPhEOelv9HRc-7xKlPFo_Fs_Qze6wfygPe4ODx-gWzYujCJfyHdSYny30E6Co8-hpiQsYfb1qKPoDunuelA |
| linkToPdf | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwlV3db9MwED-xISZeJhgfCwwwCAmBFLV2HDuWeOkK1QZsArZKfbOcxB6VprRa2knw13POR7WUbRJvkfyzkvjsu9_57DuAt2nCeJo4FyYJtSE3lIVK8TTMqZCMSZmrzDuKR8fiYMy_TOJJs-FWtqfd25BkfafBZ2kqFr157uolnoiep9EhZ2zitQgaqA24y73h88FaMWw1MTITqdrQ5DW91u64n3dM04Yzs3_V9BU7tX6Gci2QWtmn0QPYboglGdQz4SHcscUO3KtLTf7ega2jJoj-CH4M_etDZIuVriNVmT6yT_wePjFFTk7rRzvH1T63JWnOcpFpXdDkjyGDCrdPLqcXy9KWj2E8-nw6PAibygphiu7bIrTcpkkq4twwF8cZRZ8j4S42eda3qYqzTLGc5hE-Cycjh2KubvBSYSXaexNFT2CzmBV2FwinVhnqDLopfU6dVDRLLZKwzOWptdQF8LEzyHpeZ9HQPq91twWlrb2MtJeRRu8EZRRAr5WJzpqs5b54xrmuvJdEXNPj_apH-66bsbsoZm3OUKHq8Qnz2z-e9CAsgDde9trnyCj8IZwzsyxLfXjyUw_iiAvFkUgG8K4BuRl-VWaaOw04ND6tVge510HiIs66ze0U040SKdErQ3aJ01omAbxeNfue_mBcYWfLCiOEipBn3IpRkUDNzW_BoNuKXE72EfO0ntmr0UNWlwg0BQHIzpzviLLbUkx_VanKI8lETGUAH9rVceX3bhDKs_8Bv4Kt759G-tvh8dfncJ9VtUpkyMQebC4ulvYFMsZF-rJSC38BFFZgOg |
| openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Cross-reactive+human+B+cell+and+T+cell+epitopes+between+influenza+A+and+B+viruses&rft.jtitle=Virology+journal&rft.au=Terajima%2C+Masanori&rft.au=Babon%2C+Jenny+Aurielle+B&rft.au=Co%2C+Mary+Dawn+T&rft.au=Ennis%2C+Francis+A&rft.date=2013-07-26&rft.pub=Springer-Verlag&rft.issn=1743-422X&rft.eissn=1743-422X&rft.volume=10&rft.issue=1&rft_id=info:doi/10.1186%2F1743-422X-10-244&rft.externalDocID=US201500218743 |
| thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1743-422X&client=summon |
| thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1743-422X&client=summon |
| thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1743-422X&client=summon |