Characterization and antiviral activity of a newly identified defensin-like peptide, HEdefensin, in the hard tick Haemaphysalis longicornis
Tick defensins are antimicrobial peptides that play a major role in the innate immunity of ticks by providing a direct antimicrobial defense. In this study, we identified and characterized a defensin-like encoding gene, HEdefensin, from the expressed sequence tags (EST) database of hemolymph from th...
Saved in:
Published in | Developmental and comparative immunology Vol. 68; pp. 98 - 107 |
---|---|
Main Authors | , , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
United States
Elsevier Ltd
01.03.2017
Elsevier Science Ltd |
Subjects | |
Online Access | Get full text |
Cover
Loading…
Abstract | Tick defensins are antimicrobial peptides that play a major role in the innate immunity of ticks by providing a direct antimicrobial defense. In this study, we identified and characterized a defensin-like encoding gene, HEdefensin, from the expressed sequence tags (EST) database of hemolymph from the hard tick Haemaphysalis longicornis. Expression of the gene in whole adult ticks and in different organs was upregulated during blood feeding, though not after Langat virus (LGTV) challenge. A synthetic HEdefensin peptide demonstrated significant virucidal activity against LGTV but not against an adenovirus in co-incubation virucidal assays. Moreover, the RNAi-mediated gene silencing of HEdefensin did not significantly affect the virus titer as compared to the control group. The data reported here have established the in vitro virucidal activity of the peptide against LGTV. However, its role in the innate antiviral immunity of H. longicornis remains to be explored, and further studies are needed to fully evaluate the potential biological activities of the peptide against bacteria, fungi or parasites.
[Display omitted]
•The HEdefensin gene was identified from the hemolymph EST database of H. longicornis.•The HEdefensin peptide has virucidal activity against LGTV in vitro.•The HEdefensin gene may not be involved in antiviral immunity against LGTV in vivo. |
---|---|
AbstractList | Tick defensins are antimicrobial peptides that play a major role in the innate immunity of ticks by providing a direct antimicrobial defense. In this study, we identified and characterized a defensin-like encoding gene, HEdefensin, from the expressed sequence tags (EST) database of hemolymph from the hard tick Haemaphysalis longicornis. Expression of the gene in whole adult ticks and in different organs was upregulated during blood feeding, though not after Langat virus (LGTV) challenge. A synthetic HEdefensin peptide demonstrated significant virucidal activity against LGTV but not against an adenovirus in co-incubation virucidal assays. Moreover, the RNAi-mediated gene silencing of HEdefensin did not significantly affect the virus titer as compared to the control group. The data reported here have established the in vitro virucidal activity of the peptide against LGTV. However, its role in the innate antiviral immunity of H. longicornis remains to be explored, and further studies are needed to fully evaluate the potential biological activities of the peptide against bacteria, fungi or parasites.Tick defensins are antimicrobial peptides that play a major role in the innate immunity of ticks by providing a direct antimicrobial defense. In this study, we identified and characterized a defensin-like encoding gene, HEdefensin, from the expressed sequence tags (EST) database of hemolymph from the hard tick Haemaphysalis longicornis. Expression of the gene in whole adult ticks and in different organs was upregulated during blood feeding, though not after Langat virus (LGTV) challenge. A synthetic HEdefensin peptide demonstrated significant virucidal activity against LGTV but not against an adenovirus in co-incubation virucidal assays. Moreover, the RNAi-mediated gene silencing of HEdefensin did not significantly affect the virus titer as compared to the control group. The data reported here have established the in vitro virucidal activity of the peptide against LGTV. However, its role in the innate antiviral immunity of H. longicornis remains to be explored, and further studies are needed to fully evaluate the potential biological activities of the peptide against bacteria, fungi or parasites. Tick defensins are antimicrobial peptides that play a major role in the innate immunity of ticks by providing a direct antimicrobial defense. In this study, we identified and characterized a defensin-like encoding gene, HEdefensin, from the expressed sequence tags (EST) database of hemolymph from the hard tick Haemaphysalis longicornis. Expression of the gene in whole adult ticks and in different organs was upregulated during blood feeding, though not after Langat virus (LGTV) challenge. A synthetic HEdefensin peptide demonstrated significant virucidal activity against LGTV but not against an adenovirus in co-incubation virucidal assays. Moreover, the RNAi-mediated gene silencing of HEdefensin did not significantly affect the virus titer as compared to the control group. The data reported here have established the in vitro virucidal activity of the peptide against LGTV. However, its role in the innate antiviral immunity of H. longicornis remains to be explored, and further studies are needed to fully evaluate the potential biological activities of the peptide against bacteria, fungi or parasites. Tick defensins are antimicrobial peptides that play a major role in the innate immunity of ticks by providing a direct antimicrobial defense. In this study, we identified and characterized a defensin-like encoding gene, HEdefensin, from the expressed sequence tags (EST) database of hemolymph from the hard tick Haemaphysalis longicornis. Expression of the gene in whole adult ticks and in different organs was upregulated during blood feeding, though not after Langat virus (LGTV) challenge. A synthetic HEdefensin peptide demonstrated significant virucidal activity against LGTV but not against an adenovirus in co-incubation virucidal assays. Moreover, the RNAi-mediated gene silencing of HEdefensin did not significantly affect the virus titer as compared to the control group. The data reported here have established the in vitro virucidal activity of the peptide against LGTV. However, its role in the innate antiviral immunity of H. longicornis remains to be explored, and further studies are needed to fully evaluate the potential biological activities of the peptide against bacteria, fungi or parasites. [Display omitted] •The HEdefensin gene was identified from the hemolymph EST database of H. longicornis.•The HEdefensin peptide has virucidal activity against LGTV in vitro.•The HEdefensin gene may not be involved in antiviral immunity against LGTV in vivo. Tick defensins are antimicrobial peptides that play a major role in the innate immunity of ticks by providing a direct antimicrobial defense. In this study, we identified and characterized a defensin-like encoding gene, HEdefensin, from the expressed sequence tags (EST) database of hemolymph from the hard tick Haemaphysalis longicornis. Expression of the gene in whole adult ticks and in different organs was upregulated during blood feeding, though not after Langat virus (LGTV) challenge. A synthetic HEdefensin peptide demonstrated significant virucidal activity against LGTV but not against an adenovirus in co-incubation virucidal assays. Moreover, the RNAi-mediated gene silencing of HEdefensin did not significantly affect the virus titer as compared to the control group. The data reported here have established the in vitro virucidal activity of the peptide against LGTV. However, its role in the innate antiviral immunity of H. longicornis remains to be explored, and further studies are needed to fully evaluate the potential biological activities of the peptide against bacteria, fungi or parasites. |
Author | Yoshii, Kentaro Fujisaki, Kozo Talactac, Melbourne Rio Kusakisako, Kodai Tanaka, Tetsuya Maeda, Hiroki Galay, Remil Linggatong Mochizuki, Masami Yada, Yurika Hernandez, Emmanuel Pacia |
Author_xml | – sequence: 1 givenname: Melbourne Rio surname: Talactac fullname: Talactac, Melbourne Rio organization: Laboratory of Infectious Diseases, Joint Faculty of Veterinary Medicine, Kagoshima University, 1-21-24 Korimoto, Kagoshima 890-0065, Japan – sequence: 2 givenname: Yurika surname: Yada fullname: Yada, Yurika organization: Laboratory of Infectious Diseases, Joint Faculty of Veterinary Medicine, Kagoshima University, 1-21-24 Korimoto, Kagoshima 890-0065, Japan – sequence: 3 givenname: Kentaro surname: Yoshii fullname: Yoshii, Kentaro organization: Laboratory of Public Health, Graduate School of Veterinary Medicine, Hokkaido University, Kita-ku Kita-18 Nishi-9, Sapporo, Hokkaido 060-0818, Japan – sequence: 4 givenname: Emmanuel Pacia surname: Hernandez fullname: Hernandez, Emmanuel Pacia organization: Laboratory of Infectious Diseases, Joint Faculty of Veterinary Medicine, Kagoshima University, 1-21-24 Korimoto, Kagoshima 890-0065, Japan – sequence: 5 givenname: Kodai surname: Kusakisako fullname: Kusakisako, Kodai organization: Laboratory of Infectious Diseases, Joint Faculty of Veterinary Medicine, Kagoshima University, 1-21-24 Korimoto, Kagoshima 890-0065, Japan – sequence: 6 givenname: Hiroki surname: Maeda fullname: Maeda, Hiroki organization: Laboratory of Infectious Diseases, Joint Faculty of Veterinary Medicine, Kagoshima University, 1-21-24 Korimoto, Kagoshima 890-0065, Japan – sequence: 7 givenname: Remil Linggatong surname: Galay fullname: Galay, Remil Linggatong organization: Department of Veterinary Paraclinical Sciences, College of Veterinary Medicine, University of the Philippines Los Baños, Los Baños, Laguna 4031, Philippines – sequence: 8 givenname: Kozo surname: Fujisaki fullname: Fujisaki, Kozo organization: National Agricultural and Food Research Organization, 3-1-5 Kannondai, Tsukuba, Ibaraki 305-0856, Japan – sequence: 9 givenname: Masami surname: Mochizuki fullname: Mochizuki, Masami organization: Laboratory of Infectious Diseases, Joint Faculty of Veterinary Medicine, Kagoshima University, 1-21-24 Korimoto, Kagoshima 890-0065, Japan – sequence: 10 givenname: Tetsuya surname: Tanaka fullname: Tanaka, Tetsuya email: k6199431@kadai.jp organization: Laboratory of Infectious Diseases, Joint Faculty of Veterinary Medicine, Kagoshima University, 1-21-24 Korimoto, Kagoshima 890-0065, Japan |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/27871830$$D View this record in MEDLINE/PubMed |
BookMark | eNqFkcFuEzEQhi1URNPCA3BBlrhw6C727jpri1MVFYJUiQtI3CzXniWTbrzBdorCK_DSTElz6aFYsjzS__1je_4zdhKnCIy9lqKWQs7fr-vgsW6orKWshWyfsZnUvamE0OaEzYTsVNUK9f2UneW8FrS0FC_YadPrXupWzNifxcol5wsk_O0KTpG7GGgXvMPkRk4SVWXPp4E7HuHXuOcYgPQBIfAAA8SMsRrxFvgWtoXEC768OgoXHCMvK-B0TeAF_S1fOti47Wqf3YiZj1P8gX5KEfNL9nxwY4ZXD-c5-_bx6utiWV1_-fR5cXld-U6LUind9EbdzJtWqfkgg2ll8B10yjgF2igVnBqo6AnpVOukFn2jlRcArZHD0J6zd4e-2zT93EEudoPZwzi6CNMu24bm1DTCKPNfVOquUcaIVhL69hG6nnYp0keoYdPR07u5IurNA7W72UCw24Qbl_b2mAgB_QHwaco5wWA9ln_JlORwtFLY--zt2lL29j57K6Wl7MkpHzmPzZ_yfDh4gOZ9h5Bs9gjRQ8AEvtgw4RPuvxFtxjo |
CitedBy_id | crossref_primary_10_1111_imb_12497 crossref_primary_10_1016_j_dci_2021_104012 crossref_primary_10_1002_psc_3223 crossref_primary_10_1186_s40249_022_00996_8 crossref_primary_10_3389_fcimb_2017_00339 crossref_primary_10_1002_psc_3534 crossref_primary_10_1111_1748_5967_12468 crossref_primary_10_3390_v13050912 crossref_primary_10_1016_j_jip_2018_07_005 crossref_primary_10_3389_fphys_2018_01728 crossref_primary_10_1007_s10493_020_00584_1 crossref_primary_10_1016_j_gene_2017_07_079 crossref_primary_10_3389_fcimb_2017_00293 crossref_primary_10_3389_fmicb_2021_778309 |
Cites_doi | 10.1303/aez.10.30 10.1016/j.peptides.2011.07.027 10.1042/bj20031429 10.1186/1472-6882-12-214 10.1038/415389a 10.1186/s13071-016-1344-5 10.1016/j.dci.2015.12.015 10.1186/1756-3305-4-63 10.1093/dnares/12.1.53 10.1016/j.molimm.2008.06.025 10.3389/fcimb.2013.00026 10.1016/S0965-1748(01)00031-5 10.1073/pnas.94.21.11502 10.1016/0022-1910(95)00085-2 10.1016/j.peptides.2005.08.018 10.2741/3200 10.1017/S0031182004005967 10.1038/nchembio.1393 10.1016/j.clim.2009.12.004 10.1016/j.jinsphys.2010.05.019 10.1292/jvms.09-0167 10.1371/journal.pone.0128576 10.1186/1743-422X-9-6 10.1111/j.0105-2896.2004.0124.x 10.1128/IAI.00256-07 10.1016/j.dci.2014.04.005 10.1016/S0145-305X(99)00015-4 10.1371/journal.pone.0018550 10.1186/s13071-014-0554-y 10.1007/s00436-015-4365-7 10.1016/S0966-842X(00)01823-0 10.1016/j.jip.2015.10.009 10.1023/A:1025399610947 10.1126/science.286.5439.498 10.1016/j.vaccine.2005.07.067 10.1007/s00436-010-2053-1 10.1016/S0065-3527(03)60007-2 10.1007/s00018-011-0710-x 10.1007/s10529-005-0936-5 |
ContentType | Journal Article |
Copyright | 2016 Elsevier Ltd Copyright © 2016 Elsevier Ltd. All rights reserved. Copyright Elsevier Science Ltd. Mar 2017 |
Copyright_xml | – notice: 2016 Elsevier Ltd – notice: Copyright © 2016 Elsevier Ltd. All rights reserved. – notice: Copyright Elsevier Science Ltd. Mar 2017 |
DBID | AAYXX CITATION CGR CUY CVF ECM EIF NPM 7QL 7T5 C1K H94 7X8 7S9 L.6 |
DOI | 10.1016/j.dci.2016.11.013 |
DatabaseName | CrossRef Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed Bacteriology Abstracts (Microbiology B) Immunology Abstracts Environmental Sciences and Pollution Management AIDS and Cancer Research Abstracts MEDLINE - Academic AGRICOLA AGRICOLA - Academic |
DatabaseTitle | CrossRef MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) AIDS and Cancer Research Abstracts Immunology Abstracts Bacteriology Abstracts (Microbiology B) Environmental Sciences and Pollution Management MEDLINE - Academic AGRICOLA AGRICOLA - Academic |
DatabaseTitleList | MEDLINE - Academic AIDS and Cancer Research Abstracts AGRICOLA MEDLINE |
Database_xml | – sequence: 1 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: 2 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database |
DeliveryMethod | fulltext_linktorsrc |
Discipline | Medicine Biology |
EISSN | 1879-0089 |
EndPage | 107 |
ExternalDocumentID | 27871830 10_1016_j_dci_2016_11_013 S0145305X16304220 |
Genre | Research Support, Non-U.S. Gov't Journal Article |
GroupedDBID | --- --K --M .GJ .~1 0R~ 1B1 1RT 1~. 1~5 29F 4.4 457 4G. 53G 5GY 5RE 5VS 7-5 71M 8P~ 9JM AAAJQ AACTN AAEDT AAEDW AAIAV AAIKJ AAKOC AALRI AAOAW AAQFI AAQXK AARKO AAXUO ABBQC ABFNM ABGSF ABJNI ABKYH ABLVK ABMAC ABMZM ABRWV ABUDA ABXDB ABYKQ ACDAQ ACGFO ACGFS ACIUM ACPRK ACRLP ADBBV ADEZE ADMUD ADUVX AEBSH AEHWI AEKER AENEX AESVU AEXOQ AFKWA AFRAH AFTJW AFXIZ AGEKW AGHFR AGRDE AGUBO AGYEJ AHHHB AIEXJ AIKHN AITUG AJBFU AJOXV AJRQY ALMA_UNASSIGNED_HOLDINGS AMFUW AMRAJ ANZVX ASPBG AVWKF AXJTR AZFZN BKOJK BLXMC BNPGV C45 CJTIS CNWQP CS3 DOVZS EBS EFJIC EFLBG EJD EO8 EO9 EP2 EP3 F5P FDB FEDTE FGOYB FIRID FNPLU FYGXN G-2 G-Q GBLVA HLV HMG HVGLF HZ~ IHE J1W K-O KOM L7B LCYCR LUGTX LW9 M41 MO0 N9A O-L O9- OAUVE OVD OZT P-8 P-9 P2P PC. Q38 QYZTP R2- RIG ROL RPZ SAB SDF SDG SES SEW SIN SNL SPCBC SSH SSI SSU SSZ T5K TEORI WUQ ZGI ~G- ~KM AAHBH AATTM AAXKI AAYWO AAYXX ABWVN ACIEU ACMHX ACRPL ACVFH ADCNI ADNMO ADSLC AEIPS AEUPX AFJKZ AFPUW AGCQF AGQPQ AGRNS AGWPP AIGII AIIUN AKBMS AKRWK AKYEP ANKPU APXCP CITATION CGR CUY CVF ECM EIF NPM 7QL 7T5 C1K EFKBS H94 7X8 7S9 L.6 |
ID | FETCH-LOGICAL-c480t-582795b623556f1d931dc4e459a5e8955da5fe897b62453a1807285c0ee391ff3 |
IEDL.DBID | .~1 |
ISSN | 0145-305X 1879-0089 |
IngestDate | Thu Jul 10 18:42:56 EDT 2025 Fri Jul 11 10:06:54 EDT 2025 Wed Aug 13 09:20:34 EDT 2025 Thu Apr 03 07:02:21 EDT 2025 Thu Apr 24 23:03:23 EDT 2025 Tue Jul 01 01:13:05 EDT 2025 Fri Feb 23 02:16:42 EST 2024 |
IsPeerReviewed | true |
IsScholarly | true |
Keywords | PBS dsRNA HEdefensin Langat virus RNAi Haemaphysalis longicornis Luc Antimicrobial peptide |
Language | English |
License | Copyright © 2016 Elsevier Ltd. All rights reserved. |
LinkModel | DirectLink |
MergedId | FETCHMERGED-LOGICAL-c480t-582795b623556f1d931dc4e459a5e8955da5fe897b62453a1807285c0ee391ff3 |
Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23 |
PMID | 27871830 |
PQID | 2024480465 |
PQPubID | 2047473 |
PageCount | 10 |
ParticipantIDs | proquest_miscellaneous_2000220959 proquest_miscellaneous_1842599031 proquest_journals_2024480465 pubmed_primary_27871830 crossref_citationtrail_10_1016_j_dci_2016_11_013 crossref_primary_10_1016_j_dci_2016_11_013 elsevier_sciencedirect_doi_10_1016_j_dci_2016_11_013 |
ProviderPackageCode | CITATION AAYXX |
PublicationCentury | 2000 |
PublicationDate | March 2017 2017-03-00 20170301 |
PublicationDateYYYYMMDD | 2017-03-01 |
PublicationDate_xml | – month: 03 year: 2017 text: March 2017 |
PublicationDecade | 2010 |
PublicationPlace | United States |
PublicationPlace_xml | – name: United States – name: Oxford |
PublicationTitle | Developmental and comparative immunology |
PublicationTitleAlternate | Dev Comp Immunol |
PublicationYear | 2017 |
Publisher | Elsevier Ltd Elsevier Science Ltd |
Publisher_xml | – name: Elsevier Ltd – name: Elsevier Science Ltd |
References | Aung, Boldbaatar, Liao, Umemiya-Shirafuji, Nakao, Matsuoka, Tanaka, Fujisaki (bib2) 2011; 108 Maeda, Kurisu, Miyata, Kusakisako, Galay, Talactac, Mochizuki, Fujisaki, Tanaka (bib26) 2015; 114 Rahman, Tsuji, Boldbaatar, Battur, Liao, Umemiya-Shirafuji, You, Tanaka, Fujisaki (bib31) 2010; 72 Galay, Aung, Umemiya-Shirafuji, Maeda, Matsuo, Kawaguchi, Miyoshi, Suzuki, Xuan, Mochizuki, Fujisaki, Tanaka (bib14) 2013; 216 Nuttall, Labuda (bib30) 2003; 60 Reed, Muench (bib33) 1938; 27 Bulet, Stocklin, Menin (bib5) 2004; 198 Yeung, Gellatly, Hancock (bib45) 2011; 13 Rumyantsev, Chanock, Murphy, Pletnev (bib34) 2006; 2 Kato, Ohtoko, Ohtake, Kimura (bib23) 2005; 12 Tonk, Cabezas-Cruz, Valdés, Rego, Rudenko, Golovchenko, Bell-Sakyi, de la Fuente, Grubhoffer (bib42) 2014; 2 Chrudimská, Slaninová, Rudenko, Rů žek, Grubhoffer (bib9) 2011; 4 Lehane, Wu, Lehane (bib25) 1997; 94 Isogai, Isogai, Okumura, Hori, Tsuruta, Kurebayashi (bib20) 2010; 53 Lai, Lomas, Jonczy, Turner, Rees (bib24) 2004; 379 Fujisaki (bib13) 1978; 18 Chrudimská, Cerovsky, Slaninová, Rego, Grubhoffer (bib8) 2014; 46 Tonk, Cabezas-Cruz, Valdés, Rego, Chrudimská, Strnad, Šíma, Bell-Sakyi, Franta, Vilcinskas, Grubhoffer, Rahnamaeian (bib41) 2014; 7 Zasloff (bib48) 2002; 415 Altmann, Brandt, Jahrling, Blaney (bib1) 2012; 9 Tian, Gao, Rodriguez, Mendoza, Ma, Zhu (bib40) 2008; 45 Boldbaatar, Umemiya-Shirafuji, Liao, Tanaka, Xuan, Fujisaki (bib3) 2010; 56 Sagaram, Pandurangi, Kaur, Smith, Shah (bib35) 2011; 6 Guani-Guerra, Santos-Mendoza, Lugo-Reyes, Teran (bib16) 2010; 1 Hancock, Diamond (bib18) 2000; 2000 Fujisaki, Kitaoka, Morii (bib12) 1975; 10 de la Fuente, Estrada-Pena, Venzal, Kocan, Sonenshine (bib10) 2008; 13 Bulet, Hetru, Dimarcq, Hoffmann (bib4) 1999; 5 Talactac, Yoshii, Maeda, Kusakisako, Hernandez, Fujisaki, Galay, Tanaka, Mochizuki (bib36) 2016; 9 Rajamuthiah, Jayamani, Conery, Fuchs, Kim, Johnston, Vilcinskas, Ausubel, Mylonakis (bib32) 2015; 10 Chen, Xu, Peng, Fang, Yin, Xu, Cen (bib6) 2006; 4 Mlera, Offerdahl, Martens, Porcella, Melik, Bloom (bib28) 2015; 3 Tanaka, Maeda, Matsuo, Boldbattar, Umemiya-Shirafuji, Kume, Suzuki, Xuan, Tsuji, Fujisaki (bib38) 2012; 34 Zandi, Teoh, Sam, Wong, Mustafa, Abubakar (bib47) 2012; 12 Tanaka, Maeda, Galay, Boldbattar, Umemiya-Shirafuji, Suzuki, Xuan, Tsuji, Fujisaki (bib37) 2012; 3 Hajdušek, Síma, Ayllón, Jalovecká, Perner, de la Fuente, Kopacek (bib17) 2013; 3 Chernysh, Cociancich, Briand, Hetru, Bulet (bib7) 1996; 42 Maeda, Miyata, Kusakisako, Galay, Talactac, Umemiya-Shirafuji, Mochizuki, Fujisaki, Tanaka (bib27) 2016; 57 Tonk, Knorr, Cabezas-Cruz, Valdés, Kollewe, Vilcinskas (bib43) 2015; 132 Zandi, Teoh, Sam, Wong, Mustafa, Abubakar (bib46) 2011; 23 Tang, Yuan, Osapay, Osapay, Tran, Miller, Ouellette, Selsted (bib39) 1999; 5439 Hilchie, Wuerth, Hancock (bib19) 2013; 12 Jongejan, Uilenberg (bib21) 2004; 129 Nakajima, Taylor, Yamakawa (bib29) 2002; 1 De Smet, Contreras (bib11) 2005; 18 Johns, Sonenshine, Hynes (bib22) 2001; 31 Tsuji, Battsetseg, Boldbaatar, Miyoshi, Xuan, Oliver, Fujisaki (bib44) 2007; 75 Zandi (10.1016/j.dci.2016.11.013_bib47) 2012; 12 Chrudimská (10.1016/j.dci.2016.11.013_bib9) 2011; 4 Talactac (10.1016/j.dci.2016.11.013_bib36) 2016; 9 Sagaram (10.1016/j.dci.2016.11.013_bib35) 2011; 6 de la Fuente (10.1016/j.dci.2016.11.013_bib10) 2008; 13 Altmann (10.1016/j.dci.2016.11.013_bib1) 2012; 9 Hancock (10.1016/j.dci.2016.11.013_bib18) 2000; 2000 Hilchie (10.1016/j.dci.2016.11.013_bib19) 2013; 12 Isogai (10.1016/j.dci.2016.11.013_bib20) 2010; 53 Yeung (10.1016/j.dci.2016.11.013_bib45) 2011; 13 Guani-Guerra (10.1016/j.dci.2016.11.013_bib16) 2010; 1 Lai (10.1016/j.dci.2016.11.013_bib24) 2004; 379 Fujisaki (10.1016/j.dci.2016.11.013_bib13) 1978; 18 Hajdušek (10.1016/j.dci.2016.11.013_bib17) 2013; 3 Tanaka (10.1016/j.dci.2016.11.013_bib37) 2012; 3 Jongejan (10.1016/j.dci.2016.11.013_bib21) 2004; 129 Chen (10.1016/j.dci.2016.11.013_bib6) 2006; 4 Galay (10.1016/j.dci.2016.11.013_bib14) 2013; 216 Lehane (10.1016/j.dci.2016.11.013_bib25) 1997; 94 Bulet (10.1016/j.dci.2016.11.013_bib5) 2004; 198 Mlera (10.1016/j.dci.2016.11.013_bib28) 2015; 3 Maeda (10.1016/j.dci.2016.11.013_bib26) 2015; 114 Rajamuthiah (10.1016/j.dci.2016.11.013_bib32) 2015; 10 Chernysh (10.1016/j.dci.2016.11.013_bib7) 1996; 42 Rumyantsev (10.1016/j.dci.2016.11.013_bib34) 2006; 2 Nakajima (10.1016/j.dci.2016.11.013_bib29) 2002; 1 Bulet (10.1016/j.dci.2016.11.013_bib4) 1999; 5 Tonk (10.1016/j.dci.2016.11.013_bib41) 2014; 7 Aung (10.1016/j.dci.2016.11.013_bib2) 2011; 108 Tonk (10.1016/j.dci.2016.11.013_bib43) 2015; 132 Zandi (10.1016/j.dci.2016.11.013_bib46) 2011; 23 Boldbaatar (10.1016/j.dci.2016.11.013_bib3) 2010; 56 Rahman (10.1016/j.dci.2016.11.013_bib31) 2010; 72 Tonk (10.1016/j.dci.2016.11.013_bib42) 2014; 2 Maeda (10.1016/j.dci.2016.11.013_bib27) 2016; 57 Nuttall (10.1016/j.dci.2016.11.013_bib30) 2003; 60 Tanaka (10.1016/j.dci.2016.11.013_bib38) 2012; 34 De Smet (10.1016/j.dci.2016.11.013_bib11) 2005; 18 Kato (10.1016/j.dci.2016.11.013_bib23) 2005; 12 Reed (10.1016/j.dci.2016.11.013_bib33) 1938; 27 Tang (10.1016/j.dci.2016.11.013_bib39) 1999; 5439 Tian (10.1016/j.dci.2016.11.013_bib40) 2008; 45 Chrudimská (10.1016/j.dci.2016.11.013_bib8) 2014; 46 Tsuji (10.1016/j.dci.2016.11.013_bib44) 2007; 75 Fujisaki (10.1016/j.dci.2016.11.013_bib12) 1975; 10 Johns (10.1016/j.dci.2016.11.013_bib22) 2001; 31 Zasloff (10.1016/j.dci.2016.11.013_bib48) 2002; 415 |
References_xml | – volume: 42 start-page: 81 year: 1996 end-page: 89 ident: bib7 article-title: The inducible antibacterial peptides of the hemipteran insect publication-title: J. Insect Physiol. – volume: 72 start-page: 149 year: 2010 end-page: 156 ident: bib31 article-title: Structural characterization and cytolytic activity of a potent antimicrobial motif in longicin, a defensin-like peptide in the tick publication-title: J. Vet. Med. Sci. – volume: 57 start-page: 38 year: 2016 end-page: 47 ident: bib27 article-title: A novel C-type lectin with triple carbohydrate recognition domains has critical roles for the hard tick publication-title: Dev. Comp. Immunol. – volume: 94 start-page: 11502 year: 1997 end-page: 11507 ident: bib25 article-title: Midgut-specific immune molecules are produced by the blood-sucking insect publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 60 start-page: 233 year: 2003 end-page: 272 ident: bib30 article-title: Dynamics of infection in tick vectors and at the tick-host interface publication-title: Adv. Virus Res. – volume: 27 start-page: 493 year: 1938 end-page: 497 ident: bib33 article-title: A simple method of estimating fifty percent endpoints publication-title: Am. J. Hyg. – volume: 34 start-page: 242 year: 2012 end-page: 250 ident: bib38 article-title: Parasiticidal activity of publication-title: Peptides – volume: 75 start-page: 3633 year: 2007 end-page: 3640 ident: bib44 article-title: vector tick defensin against publication-title: Infect. Immun. – volume: 5 start-page: 329 year: 1999 end-page: 344 ident: bib4 article-title: Antimicrobial peptides in insects: structure and function publication-title: Dev. Comp. Immunol. – volume: 12 start-page: 53 year: 2005 end-page: 62 ident: bib23 article-title: Vector-capping: a simple method for preparing a high-quality full-length cDNA library publication-title: DNA Res. – volume: 3 year: 2012 ident: bib37 article-title: Tick longicin implicated in the arthropod transmission of Toxoplasma gondii publication-title: J. Vet. Sci. Technol. – volume: 2 start-page: 46 year: 2014 end-page: 52 ident: bib42 article-title: Identification and partial characterisation of new members of the publication-title: Gene – volume: 2 start-page: 133 year: 2006 end-page: 143 ident: bib34 article-title: Comparison of live and inactivated tick-borne encephalitis virus vaccines for safety, immunogenicity and efficacy in rhesus monkeys publication-title: Vaccine – volume: 53 start-page: 1 year: 2010 end-page: 7 ident: bib20 article-title: Tertiary structure-related activity of tick defensin (persulcatusin) in the taiga tick, publication-title: Exp. Appl. Acarol. – volume: 46 start-page: 165 year: 2014 end-page: 170 ident: bib8 article-title: Defensin from the ornate sheep tick publication-title: Dev. Comp. Immunol. – volume: 10 start-page: e128576 year: 2015 ident: bib32 article-title: A Defensin from the model beetle publication-title: PLoS ONE – volume: 2000 start-page: 402 year: 2000 end-page: 410 ident: bib18 article-title: The role of cationic antimicrobial peptides in innate host defences publication-title: Trends Microbiol. – volume: 415 start-page: 389 year: 2002 end-page: 395 ident: bib48 article-title: Antimicrobial peptides of multicellular organisms publication-title: Nature – volume: 1 start-page: 135 year: 2002 end-page: 140 ident: bib29 article-title: Involvement of antibacterial peptide defensin in tick midgut defense publication-title: Exp. Appl. Acarol. – volume: 1 start-page: 1 year: 2010 end-page: 11 ident: bib16 article-title: Antimicrobial peptides: general overview and clinical implications in human health and disease publication-title: Clin. Immunol. – volume: 379 start-page: 681 year: 2004 end-page: 685 ident: bib24 article-title: Two novel non-cationic defensin-like antimicrobial peptides from haemolymph of the female tick, publication-title: Biochem. J. – volume: 114 start-page: 1793 year: 2015 end-page: 1802 ident: bib26 article-title: Identification of the publication-title: Parasitol. Res. – volume: 9 start-page: 59 year: 2016 ident: bib36 article-title: Virucidal activity of publication-title: Parasit. Vectors – volume: 23 start-page: 5534 year: 2011 end-page: 5539 ident: bib46 article-title: antiviral activity of fisetin, rutin and naringenin against dengue virus type-2 publication-title: J. Med. Plants Res. – volume: 18 start-page: 27 year: 1978 end-page: 38 ident: bib13 article-title: Development of acquired resistance and precipitating antibody in rabbits experimentally infested with females of publication-title: Natl. Inst. Anim. Health Q. – volume: 3 start-page: 614 year: 2015 end-page: 615 ident: bib28 article-title: Development of a model system for tick-borne flavivirus persistence in HEK 293T cells publication-title: MBio – volume: 7 start-page: 554 year: 2014 ident: bib41 article-title: Defensins from the tick publication-title: Parasit. Vectors – volume: 129 start-page: S3 year: 2004 end-page: S14 ident: bib21 article-title: The global importance of ticks publication-title: Parasitology – volume: 31 start-page: 747 year: 2001 end-page: 751 ident: bib22 article-title: Identification of a defensin from the hemolymph of the American dog tick, publication-title: Insect Biochem. Mol. Biol. – volume: 45 start-page: 3909 year: 2008 end-page: 3916 ident: bib40 article-title: Gene expression, antiparasitic activity, and functional evolution of the drosomycin family publication-title: Mol. Immunol. – volume: 6 start-page: e18550 year: 2011 ident: bib35 article-title: Structure–activity determinants in antifungal plant defensins MsDef1 and MtDef4 with different modes of action against publication-title: PLoS One – volume: 132 start-page: 208 year: 2015 end-page: 215 ident: bib43 article-title: defensins are primarily active against Gram-positive bacteria publication-title: J. Inv. Pathol. – volume: 56 start-page: 1587 year: 2010 end-page: 1598 ident: bib3 article-title: Multiple vitellogenins from the publication-title: J. Insect Physiol. – volume: 12 start-page: 214 year: 2012 ident: bib47 article-title: Novel antiviral activity of baicalein against dengue virus publication-title: BMC Complement. Altern. Med. – volume: 3 start-page: 26 year: 2013 ident: bib17 article-title: Interaction of the tick immune system with transmitted pathogens publication-title: Front. Cell. Infect. Microbiol. – volume: 198 start-page: 169 year: 2004 end-page: 184 ident: bib5 article-title: Anti-microbial peptides: from invertebrates to vertebrates publication-title: Immunol. Rev. – volume: 5439 start-page: 498 year: 1999 end-page: 502 ident: bib39 article-title: A cyclic antimicrobial peptide produced in primate leukocytes by the ligation of two truncated alpha-defensins publication-title: Science – volume: 4 start-page: 63 year: 2011 end-page: 72 ident: bib9 article-title: Functional characterization of two defensin isoforms of the hard tick publication-title: Parasit. Vectors – volume: 12 start-page: 761 year: 2013 end-page: 768 ident: bib19 article-title: Immune modulation by multifaceted cationic host defense (antimicrobial) peptides publication-title: Nat. Chem. Biol. – volume: 13 start-page: 2161 year: 2011 end-page: 2176 ident: bib45 article-title: Multifunctional cationic host defence peptides and their clinical applications publication-title: Cell. Mol. Life Sci. – volume: 18 start-page: 1337 year: 2005 end-page: 1347 ident: bib11 article-title: Human antimicrobial peptides: defensins, cathelicidins and histatins publication-title: Biotechnol. Lett. – volume: 216 start-page: 1905 year: 2013 end-page: 1915 ident: bib14 article-title: Multiple ferritins are vital to successful blood feeding and reproduction of the hard tick publication-title: J. Exp. Biol. – volume: 9 start-page: 6 year: 2012 ident: bib1 article-title: Antiviral activity of the EB peptide against zoonotic poxviruses publication-title: Virol. J. – volume: 10 start-page: 30 year: 1975 end-page: 39 ident: bib12 article-title: Hemocyte types and their primary cultures in the argasid tick, publication-title: Appl. Entomol. Zool. – volume: 4 start-page: 931 year: 2006 end-page: 940 ident: bib6 article-title: Recent advances in the research and development of human defensins publication-title: Peptides – volume: 13 start-page: 6938 year: 2008 end-page: 6946 ident: bib10 article-title: Overview: ticks as vectors of pathogens that cause disease in humans and animals publication-title: Front. Biosci. – volume: 108 start-page: 273 year: 2011 end-page: 285 ident: bib2 article-title: Identification and characterization of class B scavenger receptor CD36 from the hard tick, publication-title: Parasitol. Res. – volume: 10 start-page: 30 year: 1975 ident: 10.1016/j.dci.2016.11.013_bib12 article-title: Hemocyte types and their primary cultures in the argasid tick, Ornithodoros moubata Murray (Ixodoidea) publication-title: Appl. Entomol. Zool. doi: 10.1303/aez.10.30 – volume: 34 start-page: 242 year: 2012 ident: 10.1016/j.dci.2016.11.013_bib38 article-title: Parasiticidal activity of Haemaphysalis longicornis longicin P4 peptide against Toxoplasma gondii publication-title: Peptides doi: 10.1016/j.peptides.2011.07.027 – volume: 379 start-page: 681 year: 2004 ident: 10.1016/j.dci.2016.11.013_bib24 article-title: Two novel non-cationic defensin-like antimicrobial peptides from haemolymph of the female tick, Amblyomma hebraeum publication-title: Biochem. J. doi: 10.1042/bj20031429 – volume: 2 start-page: 46 year: 2014 ident: 10.1016/j.dci.2016.11.013_bib42 article-title: Identification and partial characterisation of new members of the Ixodes ricinus defensin family publication-title: Gene – volume: 12 start-page: 214 year: 2012 ident: 10.1016/j.dci.2016.11.013_bib47 article-title: Novel antiviral activity of baicalein against dengue virus publication-title: BMC Complement. Altern. Med. doi: 10.1186/1472-6882-12-214 – volume: 415 start-page: 389 year: 2002 ident: 10.1016/j.dci.2016.11.013_bib48 article-title: Antimicrobial peptides of multicellular organisms publication-title: Nature doi: 10.1038/415389a – volume: 9 start-page: 59 year: 2016 ident: 10.1016/j.dci.2016.11.013_bib36 article-title: Virucidal activity of Haemaphysalis longicornis longicin P4 peptide against tick-borne encephalitis virus surrogate Langat virus publication-title: Parasit. Vectors doi: 10.1186/s13071-016-1344-5 – volume: 57 start-page: 38 year: 2016 ident: 10.1016/j.dci.2016.11.013_bib27 article-title: A novel C-type lectin with triple carbohydrate recognition domains has critical roles for the hard tick Haemaphysalis longicornis against Gram-negative bacteria publication-title: Dev. Comp. Immunol. doi: 10.1016/j.dci.2015.12.015 – volume: 3 year: 2012 ident: 10.1016/j.dci.2016.11.013_bib37 article-title: Tick longicin implicated in the arthropod transmission of Toxoplasma gondii publication-title: J. Vet. Sci. Technol. – volume: 4 start-page: 63 year: 2011 ident: 10.1016/j.dci.2016.11.013_bib9 article-title: Functional characterization of two defensin isoforms of the hard tick Ixodes ricinus publication-title: Parasit. Vectors doi: 10.1186/1756-3305-4-63 – volume: 12 start-page: 53 year: 2005 ident: 10.1016/j.dci.2016.11.013_bib23 article-title: Vector-capping: a simple method for preparing a high-quality full-length cDNA library publication-title: DNA Res. doi: 10.1093/dnares/12.1.53 – volume: 27 start-page: 493 year: 1938 ident: 10.1016/j.dci.2016.11.013_bib33 article-title: A simple method of estimating fifty percent endpoints publication-title: Am. J. Hyg. – volume: 45 start-page: 3909 year: 2008 ident: 10.1016/j.dci.2016.11.013_bib40 article-title: Gene expression, antiparasitic activity, and functional evolution of the drosomycin family publication-title: Mol. Immunol. doi: 10.1016/j.molimm.2008.06.025 – volume: 3 start-page: 26 year: 2013 ident: 10.1016/j.dci.2016.11.013_bib17 article-title: Interaction of the tick immune system with transmitted pathogens publication-title: Front. Cell. Infect. Microbiol. doi: 10.3389/fcimb.2013.00026 – volume: 53 start-page: 1 year: 2010 ident: 10.1016/j.dci.2016.11.013_bib20 article-title: Tertiary structure-related activity of tick defensin (persulcatusin) in the taiga tick, Ixodes persulcatus publication-title: Exp. Appl. Acarol. – volume: 31 start-page: 747 year: 2001 ident: 10.1016/j.dci.2016.11.013_bib22 article-title: Identification of a defensin from the hemolymph of the American dog tick, Dermacentor variabilis publication-title: Insect Biochem. Mol. Biol. doi: 10.1016/S0965-1748(01)00031-5 – volume: 23 start-page: 5534 year: 2011 ident: 10.1016/j.dci.2016.11.013_bib46 article-title: In vitro antiviral activity of fisetin, rutin and naringenin against dengue virus type-2 publication-title: J. Med. Plants Res. – volume: 94 start-page: 11502 year: 1997 ident: 10.1016/j.dci.2016.11.013_bib25 article-title: Midgut-specific immune molecules are produced by the blood-sucking insect Stomoxys calcitrans publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.94.21.11502 – volume: 42 start-page: 81 year: 1996 ident: 10.1016/j.dci.2016.11.013_bib7 article-title: The inducible antibacterial peptides of the hemipteran insect Palomena prasina: identification of a unique family of proline-rich peptides and of a novel insect defensin publication-title: J. Insect Physiol. doi: 10.1016/0022-1910(95)00085-2 – volume: 4 start-page: 931 year: 2006 ident: 10.1016/j.dci.2016.11.013_bib6 article-title: Recent advances in the research and development of human defensins publication-title: Peptides doi: 10.1016/j.peptides.2005.08.018 – volume: 13 start-page: 6938 year: 2008 ident: 10.1016/j.dci.2016.11.013_bib10 article-title: Overview: ticks as vectors of pathogens that cause disease in humans and animals publication-title: Front. Biosci. doi: 10.2741/3200 – volume: 129 start-page: S3 year: 2004 ident: 10.1016/j.dci.2016.11.013_bib21 article-title: The global importance of ticks publication-title: Parasitology doi: 10.1017/S0031182004005967 – volume: 18 start-page: 27 year: 1978 ident: 10.1016/j.dci.2016.11.013_bib13 article-title: Development of acquired resistance and precipitating antibody in rabbits experimentally infested with females of Haemaphysalis longicornis (Ixodoidea: ixodidae) publication-title: Natl. Inst. Anim. Health Q. – volume: 12 start-page: 761 year: 2013 ident: 10.1016/j.dci.2016.11.013_bib19 article-title: Immune modulation by multifaceted cationic host defense (antimicrobial) peptides publication-title: Nat. Chem. Biol. doi: 10.1038/nchembio.1393 – volume: 216 start-page: 1905 year: 2013 ident: 10.1016/j.dci.2016.11.013_bib14 article-title: Multiple ferritins are vital to successful blood feeding and reproduction of the hard tick Haemaphysalis longicornis publication-title: J. Exp. Biol. – volume: 1 start-page: 1 year: 2010 ident: 10.1016/j.dci.2016.11.013_bib16 article-title: Antimicrobial peptides: general overview and clinical implications in human health and disease publication-title: Clin. Immunol. doi: 10.1016/j.clim.2009.12.004 – volume: 56 start-page: 1587 year: 2010 ident: 10.1016/j.dci.2016.11.013_bib3 article-title: Multiple vitellogenins from the Haemaphysalis longicornis tick are crucial for ovarian development publication-title: J. Insect Physiol. doi: 10.1016/j.jinsphys.2010.05.019 – volume: 72 start-page: 149 year: 2010 ident: 10.1016/j.dci.2016.11.013_bib31 article-title: Structural characterization and cytolytic activity of a potent antimicrobial motif in longicin, a defensin-like peptide in the tick Haemaphysalis longicornis publication-title: J. Vet. Med. Sci. doi: 10.1292/jvms.09-0167 – volume: 10 start-page: e128576 year: 2015 ident: 10.1016/j.dci.2016.11.013_bib32 article-title: A Defensin from the model beetle Tribolium castaneum acts synergistically with telavancin and daptomycin against multidrug resistant Staphylococcus aureus publication-title: PLoS ONE doi: 10.1371/journal.pone.0128576 – volume: 9 start-page: 6 year: 2012 ident: 10.1016/j.dci.2016.11.013_bib1 article-title: Antiviral activity of the EB peptide against zoonotic poxviruses publication-title: Virol. J. doi: 10.1186/1743-422X-9-6 – volume: 198 start-page: 169 year: 2004 ident: 10.1016/j.dci.2016.11.013_bib5 article-title: Anti-microbial peptides: from invertebrates to vertebrates publication-title: Immunol. Rev. doi: 10.1111/j.0105-2896.2004.0124.x – volume: 75 start-page: 3633 year: 2007 ident: 10.1016/j.dci.2016.11.013_bib44 article-title: Babesial vector tick defensin against Babesia sp. parasites publication-title: Infect. Immun. doi: 10.1128/IAI.00256-07 – volume: 46 start-page: 165 year: 2014 ident: 10.1016/j.dci.2016.11.013_bib8 article-title: Defensin from the ornate sheep tick Dermacentor marginatus and its effect on Lyme borreliosis spirochetes publication-title: Dev. Comp. Immunol. doi: 10.1016/j.dci.2014.04.005 – volume: 5 start-page: 329 year: 1999 ident: 10.1016/j.dci.2016.11.013_bib4 article-title: Antimicrobial peptides in insects: structure and function publication-title: Dev. Comp. Immunol. doi: 10.1016/S0145-305X(99)00015-4 – volume: 6 start-page: e18550 year: 2011 ident: 10.1016/j.dci.2016.11.013_bib35 article-title: Structure–activity determinants in antifungal plant defensins MsDef1 and MtDef4 with different modes of action against Fusarium graminearum publication-title: PLoS One doi: 10.1371/journal.pone.0018550 – volume: 7 start-page: 554 year: 2014 ident: 10.1016/j.dci.2016.11.013_bib41 article-title: Defensins from the tick Ixodes scapularis are effective against phytopathogenic fungi and the human bacterial pathogen Listeria grayi publication-title: Parasit. Vectors doi: 10.1186/s13071-014-0554-y – volume: 114 start-page: 1793 year: 2015 ident: 10.1016/j.dci.2016.11.013_bib26 article-title: Identification of the Babesia-responsive leucine-rich repeat domain-containing protein from the hard tick Haemaphysalis longicornis publication-title: Parasitol. Res. doi: 10.1007/s00436-015-4365-7 – volume: 2000 start-page: 402 year: 2000 ident: 10.1016/j.dci.2016.11.013_bib18 article-title: The role of cationic antimicrobial peptides in innate host defences publication-title: Trends Microbiol. doi: 10.1016/S0966-842X(00)01823-0 – volume: 132 start-page: 208 year: 2015 ident: 10.1016/j.dci.2016.11.013_bib43 article-title: Tribolium castaneum defensins are primarily active against Gram-positive bacteria publication-title: J. Inv. Pathol. doi: 10.1016/j.jip.2015.10.009 – volume: 1 start-page: 135 year: 2002 ident: 10.1016/j.dci.2016.11.013_bib29 article-title: Involvement of antibacterial peptide defensin in tick midgut defense publication-title: Exp. Appl. Acarol. doi: 10.1023/A:1025399610947 – volume: 5439 start-page: 498 year: 1999 ident: 10.1016/j.dci.2016.11.013_bib39 article-title: A cyclic antimicrobial peptide produced in primate leukocytes by the ligation of two truncated alpha-defensins publication-title: Science doi: 10.1126/science.286.5439.498 – volume: 3 start-page: 614 year: 2015 ident: 10.1016/j.dci.2016.11.013_bib28 article-title: Development of a model system for tick-borne flavivirus persistence in HEK 293T cells publication-title: MBio – volume: 2 start-page: 133 year: 2006 ident: 10.1016/j.dci.2016.11.013_bib34 article-title: Comparison of live and inactivated tick-borne encephalitis virus vaccines for safety, immunogenicity and efficacy in rhesus monkeys publication-title: Vaccine doi: 10.1016/j.vaccine.2005.07.067 – volume: 108 start-page: 273 year: 2011 ident: 10.1016/j.dci.2016.11.013_bib2 article-title: Identification and characterization of class B scavenger receptor CD36 from the hard tick, Haemaphysalis longicornis publication-title: Parasitol. Res. doi: 10.1007/s00436-010-2053-1 – volume: 60 start-page: 233 year: 2003 ident: 10.1016/j.dci.2016.11.013_bib30 article-title: Dynamics of infection in tick vectors and at the tick-host interface publication-title: Adv. Virus Res. doi: 10.1016/S0065-3527(03)60007-2 – volume: 13 start-page: 2161 year: 2011 ident: 10.1016/j.dci.2016.11.013_bib45 article-title: Multifunctional cationic host defence peptides and their clinical applications publication-title: Cell. Mol. Life Sci. doi: 10.1007/s00018-011-0710-x – volume: 18 start-page: 1337 year: 2005 ident: 10.1016/j.dci.2016.11.013_bib11 article-title: Human antimicrobial peptides: defensins, cathelicidins and histatins publication-title: Biotechnol. Lett. doi: 10.1007/s10529-005-0936-5 |
SSID | ssj0000810 |
Score | 2.2568567 |
Snippet | Tick defensins are antimicrobial peptides that play a major role in the innate immunity of ticks by providing a direct antimicrobial defense. In this study, we... |
SourceID | proquest pubmed crossref elsevier |
SourceType | Aggregation Database Index Database Enrichment Source Publisher |
StartPage | 98 |
SubjectTerms | adults Animals Antiinfectives and antibacterials Antimicrobial peptide Antimicrobial peptides Antiviral activity antiviral properties Arachnids bacteria Biological activity Cells, Cultured Cloning, Molecular Containment of Biohazards Defensins Defensins - genetics Defensins - metabolism Disease Models, Animal Ectoparasites Encephalitis Viruses, Tick-Borne - immunology Encephalitis, Tick-Borne - immunology Expressed sequence tags Fungi Gene expression Gene silencing Genes Haemaphysalis longicornis HEdefensin hematophagy Hemolymph Hemolymph - metabolism Humans Immunity Immunity, Innate - genetics Immunology Innate immunity Insect Proteins - genetics Insect Proteins - metabolism Ixodidae - immunology Langat virus Organs Parasites Peptides RNA-mediated interference Sequence Alignment Ticks viral load Viruses |
Title | Characterization and antiviral activity of a newly identified defensin-like peptide, HEdefensin, in the hard tick Haemaphysalis longicornis |
URI | https://dx.doi.org/10.1016/j.dci.2016.11.013 https://www.ncbi.nlm.nih.gov/pubmed/27871830 https://www.proquest.com/docview/2024480465 https://www.proquest.com/docview/1842599031 https://www.proquest.com/docview/2000220959 |
Volume | 68 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV09b9swECWCFC26BG365TQJWKBTEcWkxJOpMTASqC2SqQG8EaRIAmpc2YidIUv-QP507_ThIoMzdDAgmJRA68i7R_PdO8a-osODqJxMoCpwgxKlSxxG-iRaDFcWPMRWwPTyKi-v1Y8ZzHbYdMiFIVpl7_s7n9566_6bcf82x8u6HhMtCXC2zhBRkJAV7duVmtAsP334R_PAkCc6GiMk1Hs42Ww5Xr6qid2Vn5KQp8y2xaZt2LONQRdv2F4PHvlZN763bCc0--xlV07yfp-9uuwPyt-xx-lGiLnLs-S28fihWhG3-AhKZ6CqEXwRueUIref3vPYdcyh47kMkYnuTzOubwJfEfPHhhJfnQ8MJrxuO2JFT0hbH4dzw0oY_JH69IklFPl806FMp6Wv1nl1fnP-alklfdyGplBbrBHQ6KcAhMALIo_RFJn2lgoLCQtAFgLcQ8WKCXdAEVmoxSTVUIoSskDFmH9hus2jCJ8YpTcTmRSU8IPRx2orcO-1yJ532XqQjJoY3bqpelJxqY8zNwD77bdBIhoyEmxWDRhqxb5tblp0ix3Od1WBG82RaGYwYz912OJjc9Gt6he0IhbRQOYzYl00zrkY6YrFNWNytjKRTTQzwmdzeJ21Fh-j_1xH72E2nzQ9J0X-ikxUH_zfuz-x1SrCj5cgdst317V04QtC0dsftqjhmL86-_yyv_gLpqRTQ |
linkProvider | Elsevier |
linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwtV1Lb9QwEB6VIh4XBOXRhQJGggtqunYSZ50DB1RapbTbUyvtzdixI4Vus6tmK7QX_gA_hz_ITB6LOGwPSD1EimIncTz2zOf4mxmA96jwZBFbEcg8xQVKIWxg0dIHhUFzZaSTRRPAdHyaZOfx14mcbMDv3heGaJWd7m91eqOtuyvDrjeH87IcEi1J4midIKKgQFa8Y1Ye--UPXLfVn46-oJA_hOHhwdl-FnSpBYI8VnwRSBWOUmnR9kuZFMKlkXB57GOZGulVKqUzssCTEVbBtxih-ChUMufeR6koigifewfuYpGitAl7P__yStDG8pY3KQNqXr-V2pDKXF4SnSzZo8ihIlpnDNeB3cboHT6GRx1aZZ_bDnkCG77agntt_srlFtwfdzvzT-HX_iryc-vYyUzl8KDkFFf4CPKfoDQVbFYwwxDLT5esdC1VyTvmfEFM-iqYlheezYlq4_wuyw76gl1WVgzBKiMvMYbNuWCZ8ZcUbbumGI5sOqtQiZOXWf0Mzm9FGs9hs5pVfhsY-aWYJM25k4i1rDI8cVbZxAqrnOPhAHjf4zrvoqBTMo6p7ulu3zUKSZOQcHWkUUgD-Li6Zd6GALmpctyLUf8zjjWaqJtu2-lFrjslUmM5Yi_F40QO4N2qGKc_7emYys-uay1oGxURRSTW1wmbKEf0w3cAL9rhtPqQEBU2anX-8v_a_RYeZGfjE31ydHr8Ch6GhHkagt4ObC6urv1rRGwL-6aZIQy-3faU_AMFjE6g |
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=Characterization+and+antiviral+activity+of+a+newly+identified+defensin-like+peptide%2C+HEdefensin%2C+in+the+hard+tick+Haemaphysalis+longicornis&rft.jtitle=Developmental+and+comparative+immunology&rft.au=Talactac%2C+Melbourne+Rio&rft.au=Yada%2C+Yurika&rft.au=Yoshii%2C+Kentaro&rft.au=Hernandez%2C+Emmanuel+Pacia&rft.date=2017-03-01&rft.pub=Elsevier+Science+Ltd&rft.issn=0145-305X&rft.eissn=1879-0089&rft.volume=68&rft.spage=98&rft_id=info:doi/10.1016%2Fj.dci.2016.11.013&rft.externalDBID=NO_FULL_TEXT |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0145-305X&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0145-305X&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0145-305X&client=summon |