Polyclonal Broadly Neutralizing Antibody Activity Characterized by CD4 Binding Site and V3-Glycan Antibodies in a Subset of HIV-1 Virus Controllers
Broadly neutralizing antibodies (bNAbs), known to mediate immune control of HIV-1 infection, only develop in a small subset of HIV-1 infected individuals. Despite being traditionally associated with patients with high viral loads, bNAbs have also been observed in therapy naïve HIV-1+ patients natura...
Saved in:
| Published in | Frontiers in immunology Vol. 12; p. 670561 |
|---|---|
| Main Authors | , , , , , , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Switzerland
Frontiers Media S.A
23.12.2021
|
| Subjects | |
| Online Access | Get full text |
Cover
Loading…
| Abstract | Broadly neutralizing antibodies (bNAbs), known to mediate immune control of HIV-1 infection, only develop in a small subset of HIV-1 infected individuals. Despite being traditionally associated with patients with high viral loads, bNAbs have also been observed in therapy naïve HIV-1+ patients naturally controlling virus replication [Virus Controllers (VCs)]. Thus, dissecting the bNAb response in VCs will provide key information about what constitutes an effective humoral response to natural HIV-1 infection. In this study, we identified a polyclonal bNAb response to natural HIV-1 infection targeting CD4 binding site (CD4bs), V3-glycan, gp120-gp41 interface and membrane-proximal external region (MPER) epitopes on the HIV-1 envelope (Env). The polyclonal antiviral antibody (Ab) response also included antibody-dependent cellular phagocytosis of clade AE, B and C viruses, consistent with both the Fv and Fc domain contributing to function. Sequence analysis of
from one of the VCs revealed features consistent with potential immune pressure and virus escape from V3-glycan targeting bNAbs. Epitope mapping of the polyclonal bNAb response in VCs with bNAb activity highlighted the presence of gp120-gp41 interface and CD4bs antibody classes with similar binding profiles to known potent bNAbs. Thus, these findings reveal the induction of a broad and polyfunctional humoral response in VCs in response to natural HIV-1 infection. |
|---|---|
| AbstractList | Broadly neutralizing antibodies (bNAbs), known to mediate immune control of HIV-1 infection, only develop in a small subset of HIV-1 infected individuals. Despite being traditionally associated with patients with high viral loads, bNAbs have also been observed in therapy naïve HIV-1+ patients naturally controlling virus replication [Virus Controllers (VCs)]. Thus, dissecting the bNAb response in VCs will provide key information about what constitutes an effective humoral response to natural HIV-1 infection. In this study, we identified a polyclonal bNAb response to natural HIV-1 infection targeting CD4 binding site (CD4bs), V3-glycan, gp120-gp41 interface and membrane-proximal external region (MPER) epitopes on the HIV-1 envelope (Env). The polyclonal antiviral antibody (Ab) response also included antibody-dependent cellular phagocytosis of clade AE, B and C viruses, consistent with both the Fv and Fc domain contributing to function. Sequence analysis of
envs
from one of the VCs revealed features consistent with potential immune pressure and virus escape from V3-glycan targeting bNAbs. Epitope mapping of the polyclonal bNAb response in VCs with bNAb activity highlighted the presence of gp120-gp41 interface and CD4bs antibody classes with similar binding profiles to known potent bNAbs. Thus, these findings reveal the induction of a broad and polyfunctional humoral response in VCs in response to natural HIV-1 infection. Broadly neutralizing antibodies (bNAbs), known to mediate immune control of HIV-1 infection, only develop in a small subset of HIV-1 infected individuals. Despite being traditionally associated with patients with high viral loads, bNAbs have also been observed in therapy naïve HIV-1+ patients naturally controlling virus replication [Virus Controllers (VCs)]. Thus, dissecting the bNAb response in VCs will provide key information about what constitutes an effective humoral response to natural HIV-1 infection. In this study, we identified a polyclonal bNAb response to natural HIV-1 infection targeting CD4 binding site (CD4bs), V3-glycan, gp120-gp41 interface and membrane-proximal external region (MPER) epitopes on the HIV-1 envelope (Env). The polyclonal antiviral antibody (Ab) response also included antibody-dependent cellular phagocytosis of clade AE, B and C viruses, consistent with both the Fv and Fc domain contributing to function. Sequence analysis of envs from one of the VCs revealed features consistent with potential immune pressure and virus escape from V3-glycan targeting bNAbs. Epitope mapping of the polyclonal bNAb response in VCs with bNAb activity highlighted the presence of gp120-gp41 interface and CD4bs antibody classes with similar binding profiles to known potent bNAbs. Thus, these findings reveal the induction of a broad and polyfunctional humoral response in VCs in response to natural HIV-1 infection. Broadly neutralizing antibodies (bNAbs), known to mediate immune control of HIV-1 infection, only develop in a small subset of HIV-1 infected individuals. Despite being traditionally associated with patients with high viral loads, bNAbs have also been observed in therapy naïve HIV-1+ patients naturally controlling virus replication [Virus Controllers (VCs)]. Thus, dissecting the bNAb response in VCs will provide key information about what constitutes an effective humoral response to natural HIV-1 infection. In this study, we identified a polyclonal bNAb response to natural HIV-1 infection targeting CD4 binding site (CD4bs), V3-glycan, gp120-gp41 interface and membrane-proximal external region (MPER) epitopes on the HIV-1 envelope (Env). The polyclonal antiviral antibody (Ab) response also included antibody-dependent cellular phagocytosis of clade AE, B and C viruses, consistent with both the Fv and Fc domain contributing to function. Sequence analysis of envs from one of the VCs revealed features consistent with potential immune pressure and virus escape from V3-glycan targeting bNAbs. Epitope mapping of the polyclonal bNAb response in VCs with bNAb activity highlighted the presence of gp120-gp41 interface and CD4bs antibody classes with similar binding profiles to known potent bNAbs. Thus, these findings reveal the induction of a broad and polyfunctional humoral response in VCs in response to natural HIV-1 infection.Broadly neutralizing antibodies (bNAbs), known to mediate immune control of HIV-1 infection, only develop in a small subset of HIV-1 infected individuals. Despite being traditionally associated with patients with high viral loads, bNAbs have also been observed in therapy naïve HIV-1+ patients naturally controlling virus replication [Virus Controllers (VCs)]. Thus, dissecting the bNAb response in VCs will provide key information about what constitutes an effective humoral response to natural HIV-1 infection. In this study, we identified a polyclonal bNAb response to natural HIV-1 infection targeting CD4 binding site (CD4bs), V3-glycan, gp120-gp41 interface and membrane-proximal external region (MPER) epitopes on the HIV-1 envelope (Env). The polyclonal antiviral antibody (Ab) response also included antibody-dependent cellular phagocytosis of clade AE, B and C viruses, consistent with both the Fv and Fc domain contributing to function. Sequence analysis of envs from one of the VCs revealed features consistent with potential immune pressure and virus escape from V3-glycan targeting bNAbs. Epitope mapping of the polyclonal bNAb response in VCs with bNAb activity highlighted the presence of gp120-gp41 interface and CD4bs antibody classes with similar binding profiles to known potent bNAbs. Thus, these findings reveal the induction of a broad and polyfunctional humoral response in VCs in response to natural HIV-1 infection. Broadly neutralizing antibodies (bNAbs), known to mediate immune control of HIV-1 infection, only develop in a small subset of HIV-1 infected individuals. Despite being traditionally associated with patients with high viral loads, bNAbs have also been observed in therapy naïve HIV-1+ patients naturally controlling virus replication [Virus Controllers (VCs)]. Thus, dissecting the bNAb response in VCs will provide key information about what constitutes an effective humoral response to natural HIV-1 infection. In this study, we identified a polyclonal bNAb response to natural HIV-1 infection targeting CD4 binding site (CD4bs), V3-glycan, gp120-gp41 interface and membrane-proximal external region (MPER) epitopes on the HIV-1 envelope (Env). The polyclonal antiviral antibody (Ab) response also included antibody-dependent cellular phagocytosis of clade AE, B and C viruses, consistent with both the Fv and Fc domain contributing to function. Sequence analysis of from one of the VCs revealed features consistent with potential immune pressure and virus escape from V3-glycan targeting bNAbs. Epitope mapping of the polyclonal bNAb response in VCs with bNAb activity highlighted the presence of gp120-gp41 interface and CD4bs antibody classes with similar binding profiles to known potent bNAbs. Thus, these findings reveal the induction of a broad and polyfunctional humoral response in VCs in response to natural HIV-1 infection. |
| Author | Acharya, Priyamvada Mudrak, Sarah V Mansouri, Katayoun Dennison, S Moses Janowska, Katarzyna LaBranche, Celia C Hope, Thomas J Goodman, Derrick Zhang, Lu Eaton, Amanda Nyanhete, Tinashe E Tomaras, Georgia D Montefiori, David C Hora, Bhavna Georgiev, Ivelin S Edwards, Robert J Spreng, Rachel L Bradley, Todd Saunders, Kevin O |
| AuthorAffiliation | 2 Duke Human Vaccine Institute, Duke University School of Medicine , Durham, NC , United States 8 Department of Molecular Genetics and Microbiology, Duke University School of Medicine , Durham, NC , United States 7 Vanderbilt Vaccine Center, Vanderbilt University Medical Center , Nashville, TN , United States 1 Center for Human Systems Immunology, Duke University School of Medicine , Durham, NC , United States 4 Department of Medicine, Duke University School of Medicine , Durham, NC , United States 3 Department of Immunology, Duke University School of Medicine , Durham, NC , United States 5 Department of Surgery, Duke University School of Medicine , Durham, NC , United States 6 Department of Cell and Molecular Biology, Feinberg School of Medicine, Northwestern University , Chicago, IL , United States |
| AuthorAffiliation_xml | – name: 8 Department of Molecular Genetics and Microbiology, Duke University School of Medicine , Durham, NC , United States – name: 1 Center for Human Systems Immunology, Duke University School of Medicine , Durham, NC , United States – name: 4 Department of Medicine, Duke University School of Medicine , Durham, NC , United States – name: 2 Duke Human Vaccine Institute, Duke University School of Medicine , Durham, NC , United States – name: 5 Department of Surgery, Duke University School of Medicine , Durham, NC , United States – name: 6 Department of Cell and Molecular Biology, Feinberg School of Medicine, Northwestern University , Chicago, IL , United States – name: 3 Department of Immunology, Duke University School of Medicine , Durham, NC , United States – name: 7 Vanderbilt Vaccine Center, Vanderbilt University Medical Center , Nashville, TN , United States |
| Author_xml | – sequence: 1 givenname: Tinashe E surname: Nyanhete fullname: Nyanhete, Tinashe E organization: Department of Immunology, Duke University School of Medicine, Durham, NC, United States – sequence: 2 givenname: Robert J surname: Edwards fullname: Edwards, Robert J organization: Department of Medicine, Duke University School of Medicine, Durham, NC, United States – sequence: 3 givenname: Celia C surname: LaBranche fullname: LaBranche, Celia C organization: Department of Surgery, Duke University School of Medicine, Durham, NC, United States – sequence: 4 givenname: Katayoun surname: Mansouri fullname: Mansouri, Katayoun organization: Duke Human Vaccine Institute, Duke University School of Medicine, Durham, NC, United States – sequence: 5 givenname: Amanda surname: Eaton fullname: Eaton, Amanda organization: Department of Surgery, Duke University School of Medicine, Durham, NC, United States – sequence: 6 givenname: S Moses surname: Dennison fullname: Dennison, S Moses organization: Department of Surgery, Duke University School of Medicine, Durham, NC, United States – sequence: 7 givenname: Kevin O surname: Saunders fullname: Saunders, Kevin O organization: Department of Surgery, Duke University School of Medicine, Durham, NC, United States – sequence: 8 givenname: Derrick surname: Goodman fullname: Goodman, Derrick organization: Department of Surgery, Duke University School of Medicine, Durham, NC, United States – sequence: 9 givenname: Katarzyna surname: Janowska fullname: Janowska, Katarzyna organization: Duke Human Vaccine Institute, Duke University School of Medicine, Durham, NC, United States – sequence: 10 givenname: Rachel L surname: Spreng fullname: Spreng, Rachel L organization: Department of Medicine, Duke University School of Medicine, Durham, NC, United States – sequence: 11 givenname: Lu surname: Zhang fullname: Zhang, Lu organization: Department of Surgery, Duke University School of Medicine, Durham, NC, United States – sequence: 12 givenname: Sarah V surname: Mudrak fullname: Mudrak, Sarah V organization: Department of Surgery, Duke University School of Medicine, Durham, NC, United States – sequence: 13 givenname: Thomas J surname: Hope fullname: Hope, Thomas J organization: Department of Cell and Molecular Biology, Feinberg School of Medicine, Northwestern University, Chicago, IL, United States – sequence: 14 givenname: Bhavna surname: Hora fullname: Hora, Bhavna organization: Department of Medicine, Duke University School of Medicine, Durham, NC, United States – sequence: 15 givenname: Todd surname: Bradley fullname: Bradley, Todd organization: Department of Medicine, Duke University School of Medicine, Durham, NC, United States – sequence: 16 givenname: Ivelin S surname: Georgiev fullname: Georgiev, Ivelin S organization: Vanderbilt Vaccine Center, Vanderbilt University Medical Center, Nashville, TN, United States – sequence: 17 givenname: David C surname: Montefiori fullname: Montefiori, David C organization: Department of Surgery, Duke University School of Medicine, Durham, NC, United States – sequence: 18 givenname: Priyamvada surname: Acharya fullname: Acharya, Priyamvada organization: Department of Surgery, Duke University School of Medicine, Durham, NC, United States – sequence: 19 givenname: Georgia D surname: Tomaras fullname: Tomaras, Georgia D organization: Department of Molecular Genetics and Microbiology, Duke University School of Medicine, Durham, NC, United States |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/35003053$$D View this record in MEDLINE/PubMed |
| BookMark | eNpVks1OGzEUhUcVVaGUB-im8rKbSf2fmU2lEFqIhNpKtNla9vhOMHJsanuQhtfoC3dCAIE3tu4957N1fd5XByEGqKqPBM8Ya9ovvdtuhxnFlMzkHAtJ3lRHREpeM0r5wYvzYXWS8w2eFm8ZY-JddcgExgwLdlT9-xX92PkYtEenKWrrR_QDhpK0d_cubNAiFGeiHdGiK-7OlREtr3XSXYHk7sEiMxXOODp1we7kV64A0sGiNavPJ7IOTwQHGbmANLoaTIaCYo8uVuuaoLVLQ0bLGEqK3kPKH6q3vfYZTh734-rP92-_lxf15c_z1XJxWXdcilKzToJpGy2MprKVcyo4F5y0preWWtk3rKVgBFDdCmzAdEz01kwewqnu55QdV6s910Z9o26T2-o0qqideijEtFE6Fdd5ULyTBHpBObGcM8AGa-DQY2MbkPNGTKyve9btYLZgOwi7Eb6Cvu4Ed6028U418-lPaDMBPj8CUvw7QC5q63IH3usAcciKStIIwhjhk5TspV2KOSfon68hWO2yoR6yoXbZUPtsTJ5PL9_37HhKAvsPI1i52A |
| CitedBy_id | crossref_primary_10_1002_jmv_29381 crossref_primary_10_3390_cells13010033 crossref_primary_10_3389_fimmu_2023_1049673 |
| Cites_doi | 10.1186/s12977-016-0297-2 10.3389/fimmu.2019.01021 10.1086/514111 10.1186/1742-4690-11-41 10.1016/j.immuni.2018.07.009 10.1186/s12977-016-0279-4 10.1128/JVI.00734-12 10.1172/jci.insight.94355 10.1128/JVI.02853-13 10.1371/journal.ppat.1006987 10.1093/molbev/msp259 10.1128/JVI.02660-07 10.1128/JVI.00049-16 10.1371/journal.ppat.1003618 10.1128/JVI.01552-17 10.1126/scitranslmed.aal2144 10.1038/nature14411 10.1128/JVI.00828-17 10.1097/00002030-199813000-00005 10.1084/jem.20130221 10.1097/COH.0000000000000554 10.1128/JVI.00802-14 10.1007/BF01731581 10.1093/cid/cix057 10.1086/516508 10.1128/JVI.02482-10 10.1371/journal.pone.0193773 10.1128/JVI.01482-09 10.1073/pnas.1111497108 10.1128/JVI.05601-11 10.1038/s41586-018-0517-0 10.1007/978-1-59745-170-3_26 10.1007/s11904-019-00432-x 10.1126/science.1187659 10.1038/nature07930 10.1371/journal.ppat.1005817 10.1128/JVI.80.10.4758-4770.2006 10.1128/JVI.01843-17 10.1097/QAD.0b013e328329f97d 10.1371/journal.ppat.1004658 10.1038/s41598-019-46462-8 10.1016/j.jim.2011.09.007 10.1186/s12977-018-0443-0 10.1086/654816 10.1002/jcc.20084 10.1198/sbr.2009.0008 10.1086/314773 10.1038/nm.4187 10.1128/JVI.00138-10 10.1097/QAI.0b013e3182100c1b 10.1089/aid.2015.0324 10.1016/j.celrep.2019.12.087 10.1093/nar/22.22.4673 10.1128/JVI.00094-19 10.1128/JVI.03765-13 10.1038/s41467-019-14196-w 10.1093/oxfordjournals.molbev.a040454 10.1186/s12977-018-0453-y 10.1038/nri3478 10.1016/j.cell.2016.02.022 10.4049/jimmunol.1800323 10.1128/JVI.02084-18 10.1086/651144 10.1371/journal.ppat.1006148 |
| ContentType | Journal Article |
| Copyright | Copyright © 2021 Nyanhete, Edwards, LaBranche, Mansouri, Eaton, Dennison, Saunders, Goodman, Janowska, Spreng, Zhang, Mudrak, Hope, Hora, Bradley, Georgiev, Montefiori, Acharya and Tomaras. Copyright © 2021 Nyanhete, Edwards, LaBranche, Mansouri, Eaton, Dennison, Saunders, Goodman, Janowska, Spreng, Zhang, Mudrak, Hope, Hora, Bradley, Georgiev, Montefiori, Acharya and Tomaras 2021 Nyanhete, Edwards, LaBranche, Mansouri, Eaton, Dennison, Saunders, Goodman, Janowska, Spreng, Zhang, Mudrak, Hope, Hora, Bradley, Georgiev, Montefiori, Acharya and Tomaras |
| Copyright_xml | – notice: Copyright © 2021 Nyanhete, Edwards, LaBranche, Mansouri, Eaton, Dennison, Saunders, Goodman, Janowska, Spreng, Zhang, Mudrak, Hope, Hora, Bradley, Georgiev, Montefiori, Acharya and Tomaras. – notice: Copyright © 2021 Nyanhete, Edwards, LaBranche, Mansouri, Eaton, Dennison, Saunders, Goodman, Janowska, Spreng, Zhang, Mudrak, Hope, Hora, Bradley, Georgiev, Montefiori, Acharya and Tomaras 2021 Nyanhete, Edwards, LaBranche, Mansouri, Eaton, Dennison, Saunders, Goodman, Janowska, Spreng, Zhang, Mudrak, Hope, Hora, Bradley, Georgiev, Montefiori, Acharya and Tomaras |
| DBID | CGR CUY CVF ECM EIF NPM AAYXX CITATION 7X8 5PM DOA |
| DOI | 10.3389/fimmu.2021.670561 |
| DatabaseName | Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed CrossRef MEDLINE - Academic PubMed Central (Full Participant titles) DOAJ Directory of Open Access Journals |
| DatabaseTitle | MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) CrossRef MEDLINE - Academic |
| DatabaseTitleList | CrossRef MEDLINE - Academic MEDLINE |
| Database_xml | – sequence: 1 dbid: DOA name: DOAJ Directory of Open Access Journals url: https://www.doaj.org/ sourceTypes: Open Website – 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 |
| DeliveryMethod | fulltext_linktorsrc |
| Discipline | Biology |
| EISSN | 1664-3224 |
| ExternalDocumentID | oai_doaj_org_article_4c61ef5241d443e0b0ae4ef0bd8e6785 10_3389_fimmu_2021_670561 35003053 |
| Genre | Journal Article Research Support, N.I.H., Extramural |
| GrantInformation_xml | – fundername: NIAID NIH HHS grantid: R01 AI131722 – fundername: NIAID NIH HHS grantid: P01 AI120756 – fundername: NIAID NIH HHS grantid: R01 AI145687 – fundername: NIAID NIH HHS grantid: P30 AI064518 – fundername: NIAID NIH HHS grantid: R56 AI052779 – fundername: NIAID NIH HHS grantid: UM1 AI100645 – fundername: ; |
| GroupedDBID | 53G 5VS 9T4 AAFWJ AAKDD ACGFO ACGFS ACXDI ADBBV ADRAZ AENEX AFPKN ALMA_UNASSIGNED_HOLDINGS AOIJS BAWUL BCNDV CGR CUY CVF DIK EBS ECM EIF EMOBN GROUPED_DOAJ GX1 HYE IAO IEA IHR IHW IPNFZ KQ8 M48 M~E NPM OK1 PGMZT RIG RNS RPM AAYXX CITATION 7X8 ITC 5PM |
| ID | FETCH-LOGICAL-c465t-3c6eb98a5ba2696725445419bfdd2d6f8392eb5e2a950bebc35fdb6eb142af723 |
| IEDL.DBID | RPM |
| ISSN | 1664-3224 |
| IngestDate | Thu Jul 04 21:07:46 EDT 2024 Tue Sep 17 21:18:03 EDT 2024 Sat Aug 31 16:36:16 EDT 2024 Thu Sep 26 17:39:24 EDT 2024 Wed Oct 02 05:22:51 EDT 2024 |
| IsDoiOpenAccess | true |
| IsOpenAccess | true |
| IsPeerReviewed | true |
| IsScholarly | true |
| Keywords | negative-stain electron microscopy antibody-dependent cellular phagocytosis (ADCP) CD4-binding site antibodies neutralization fingerprinting assay broadly neutralizing antibodies HIV-1 Virus Controllers |
| Language | English |
| License | Copyright © 2021 Nyanhete, Edwards, LaBranche, Mansouri, Eaton, Dennison, Saunders, Goodman, Janowska, Spreng, Zhang, Mudrak, Hope, Hora, Bradley, Georgiev, Montefiori, Acharya and Tomaras. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
| LinkModel | DirectLink |
| MergedId | FETCHMERGED-LOGICAL-c465t-3c6eb98a5ba2696725445419bfdd2d6f8392eb5e2a950bebc35fdb6eb142af723 |
| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 These authors share senior authorship Present address: Todd Bradley, Children’s Mercy Kansas City, MO, United States Edited by: Markus Haug, Norwegian University of Science and Technology, Norway Reviewed by: Steven William De Taeye, Academic Medical Center, Netherlands; Ujjwal Rathore, University of California, San Francisco, United States This article was submitted to Viral Immunology, a section of the journal Frontiers in Immunology |
| OpenAccessLink | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8733328/ |
| PMID | 35003053 |
| PQID | 2618513314 |
| PQPubID | 23479 |
| ParticipantIDs | doaj_primary_oai_doaj_org_article_4c61ef5241d443e0b0ae4ef0bd8e6785 pubmedcentral_primary_oai_pubmedcentral_nih_gov_8733328 proquest_miscellaneous_2618513314 crossref_primary_10_3389_fimmu_2021_670561 pubmed_primary_35003053 |
| PublicationCentury | 2000 |
| PublicationDate | 2021-12-23 |
| PublicationDateYYYYMMDD | 2021-12-23 |
| PublicationDate_xml | – month: 12 year: 2021 text: 2021-12-23 day: 23 |
| PublicationDecade | 2020 |
| PublicationPlace | Switzerland |
| PublicationPlace_xml | – name: Switzerland |
| PublicationTitle | Frontiers in immunology |
| PublicationTitleAlternate | Front Immunol |
| PublicationYear | 2021 |
| Publisher | Frontiers Media S.A |
| Publisher_xml | – name: Frontiers Media S.A |
| References | Anthony (B54) 2017; 91 Butler (B1) 2019; 16 Bonsignori (B63) 2016; 165 Gouy (B36) 2010; 27 Gilbert (B41) 2010; 202 Hancock (B48) 2015; 11 Deshpande (B53) 2016; 13 Dennison (B31) 2018; 201 Diskin (B62) 2013; 210 Martin-Gayo (B59) 2020; 30 Huang (B39) 2009; 1 McCoy (B56) 2018; 15 Yasmeen (B50) 2014; 11 Lynch (B23) 2012; 86 Henderson (B27) 2020; 11 deCamp (B40) 2014; 88 Pettersen (B33) 2004; 25 Euler (B11) 2010; 201 Carotenuto (B16) 1998; 12 Gonzalez (B15) 2018; 13 Sanders (B51) 2013; 9 Wills (B25) 2018; 92 Bianchi (B58) 2018; 49 Doria-Rose (B8) 2010; 84 Zhang (B3) 1997; 176 Tay (B26) 2019; 93 Rusert (B9) 2016; 22 Richardson (B45) 2018; 14 Payne (B46) 2014; 88 Hutchinson (B13) 2019; 10 Tay (B24) 2016; 12 Silver (B55) 2019; 93 Salazar-Gonzalez (B34) 2008; 82 Caskey (B64) 2015; 522 Todd (B19) 2012; 375 Bailey (B7) 2006; 80 Sajadi (B4) 2011; 57 Scheid (B60) 2009; 458 Cornelissen (B42) 2016; 32 Kimura (B38) 1980; 16 Whittle (B28) 2011; 108 Saitou (B37) 1987; 4 Montefiori (B18) 2009; 485 Landais (B57) 2018; 15 Freund (B14) 2017; 9 Lambotte (B6) 2009; 23 Thompson (B35) 1994; 22 Medina-Ramirez (B12) 2011; 85 Nyanhete (B47) 2019; 9 Cecilia (B5) 1999; 179 Seaton (B21) 2017; 2 Liu (B29) 2014; 88 van den Kerkhof (B52) 2016; 13 Moris (B2) 2019; 14 Doria-Rose (B32) 2017; 13 Yates (B20) 2018; 92 Sanchez-Merino (B43) 2016; 90 Wu (B22) 2010; 329 Freel (B49) 2010; 84 Dugast (B44) 2017; 64 Walker (B10) 2013; 13 Pilgrim (B17) 1997; 176 Liu (B30) 2011; 85 Kouyos (B61) 2018; 561 |
| References_xml | – volume: 13 start-page: 60 year: 2016 ident: B53 article-title: HIV-1 Clade C Escapes Broadly Neutralizing Autologous Antibodies With N332 Glycan Specificity by Distinct Mechanisms publication-title: Retrovirology doi: 10.1186/s12977-016-0297-2 contributor: fullname: Deshpande – volume: 10 year: 2019 ident: B13 article-title: Unusual Cysteine Content in V1 Region of Gp120 From an Elite Suppressor That Produces Broadly Neutralizing Antibodies publication-title: Front Immunol doi: 10.3389/fimmu.2019.01021 contributor: fullname: Hutchinson – volume: 176 year: 1997 ident: B3 article-title: Augmented Serum Neutralizing Activity Against Primary Human Immunodeficiency Virus Type 1 (HIV-1) Isolates in Two Groups of HIV-1-Infected Long-Term Nonprogressors publication-title: J Infect Dis doi: 10.1086/514111 contributor: fullname: Zhang – volume: 11 start-page: 41 year: 2014 ident: B50 article-title: Differential Binding of Neutralizing and Non-Neutralizing Antibodies to Native-Like Soluble HIV-1 Env Trimers, Uncleaved Env Proteins, and Monomeric Subunits publication-title: Retrovirology doi: 10.1186/1742-4690-11-41 contributor: fullname: Yasmeen – volume: 49 start-page: 288 year: 2018 ident: B58 article-title: Electron-Microscopy-Based Epitope Mapping Defines Specificities of Polyclonal Antibodies Elicited During HIV-1 BG505 Envelope Trimer Immunization publication-title: Immunity doi: 10.1016/j.immuni.2018.07.009 contributor: fullname: Bianchi – volume: 13 start-page: 48 year: 2016 ident: B52 article-title: HIV-1 Escapes From N332-Directed Antibody Neutralization in an Elite Neutralizer by Envelope Glycoprotein Elongation and Introduction of Unusual Disulfide Bonds publication-title: Retrovirology doi: 10.1186/s12977-016-0279-4 contributor: fullname: van den Kerkhof – volume: 86 year: 2012 ident: B23 article-title: The Development of CD4 Binding Site Antibodies During HIV-1 Infection publication-title: J Virol doi: 10.1128/JVI.00734-12 contributor: fullname: Lynch – volume: 2 start-page: e94355 year: 2017 ident: B21 article-title: Computational Analysis of Antibody Dynamics Identifies Recent HIV-1 Infection publication-title: JCI Insight doi: 10.1172/jci.insight.94355 contributor: fullname: Seaton – volume: 88 year: 2014 ident: B40 article-title: Global Panel of HIV-1 Env Reference Strains for Standardized Assessments of Vaccine-Elicited Neutralizing Antibodies publication-title: J Virol doi: 10.1128/JVI.02853-13 contributor: fullname: deCamp – volume: 14 start-page: e1006987 year: 2018 ident: B45 article-title: HIV-Specific Fc Effector Function Early in Infection Predicts the Development of Broadly Neutralizing Antibodies publication-title: PloS Pathog doi: 10.1371/journal.ppat.1006987 contributor: fullname: Richardson – volume: 27 year: 2010 ident: B36 article-title: SeaView Version 4: A Multiplatform Graphical User Interface for Sequence Alignment and Phylogenetic Tree Building publication-title: Mol Biol Evol doi: 10.1093/molbev/msp259 contributor: fullname: Gouy – volume: 82 year: 2008 ident: B34 article-title: Deciphering Human Immunodeficiency Virus Type 1 Transmission and Early Envelope Diversification by Single-Genome Amplification and Sequencing publication-title: J Virol doi: 10.1128/JVI.02660-07 contributor: fullname: Salazar-Gonzalez – volume: 90 year: 2016 ident: B43 article-title: Detection of Broadly Neutralizing Activity Within the First Months of HIV-1 Infection publication-title: J Virol doi: 10.1128/JVI.00049-16 contributor: fullname: Sanchez-Merino – volume: 9 start-page: e1003618 year: 2013 ident: B51 article-title: A Next-Generation Cleaved, Soluble HIV-1 Env Trimer, BG505 SOSIP.664 Gp140, Expresses Multiple Epitopes for Broadly Neutralizing But Not Non-Neutralizing Antibodies publication-title: PloS Pathog doi: 10.1371/journal.ppat.1003618 contributor: fullname: Sanders – volume: 92 year: 2018 ident: B25 article-title: HIV-1-Specific IgA Monoclonal Antibodies From an HIV-1 Vaccinee Mediate Galactosylceramide Blocking and Phagocytosis publication-title: J Virol doi: 10.1128/JVI.01552-17 contributor: fullname: Wills – volume: 9 year: 2017 ident: B14 article-title: Coexistence of Potent HIV-1 Broadly Neutralizing Antibodies and Antibody-Sensitive Viruses in a Viremic Controller publication-title: Sci Transl Med doi: 10.1126/scitranslmed.aal2144 contributor: fullname: Freund – volume: 522 year: 2015 ident: B64 article-title: Viraemia Suppressed in HIV-1-Infected Humans by Broadly Neutralizing Antibody 3BNC117 publication-title: Nature doi: 10.1038/nature14411 contributor: fullname: Caskey – volume: 91 start-page: e00828-17 year: 2017 ident: B54 article-title: Cooperation Between Strain-Specific and Broadly Neutralizing Responses Limited Viral Escape and Prolonged the Exposure of the Broadly Neutralizing Epitope publication-title: J Virol doi: 10.1128/JVI.00828-17 contributor: fullname: Anthony – volume: 12 year: 1998 ident: B16 article-title: Neutralizing Antibodies Are Positively Associated With CD4+ T-Cell Counts and T-Cell Function in Long-Term AIDS-Free Infection publication-title: Aids doi: 10.1097/00002030-199813000-00005 contributor: fullname: Carotenuto – volume: 210 year: 2013 ident: B62 article-title: Restricting HIV-1 Pathways for Escape Using Rationally Designed Anti-HIV-1 Antibodies publication-title: J Exp Med doi: 10.1084/jem.20130221 contributor: fullname: Diskin – volume: 14 year: 2019 ident: B2 article-title: A Role for Antibodies in Natural HIV Control publication-title: Curr Opin HIV AIDS doi: 10.1097/COH.0000000000000554 contributor: fullname: Moris – volume: 88 year: 2014 ident: B46 article-title: Transcriptional and Post-Transcriptional Regulation of Cytokine Gene Expression in HIV-1 Antigen-Specific CD8+ T Cells That Mediate Virus Inhibition publication-title: J Virol doi: 10.1128/JVI.00802-14 contributor: fullname: Payne – volume: 16 year: 1980 ident: B38 article-title: A Simple Method for Estimating Evolutionary Rates of Base Substitutions Through Comparative Studies of Nucleotide Sequences publication-title: J Mol Evol doi: 10.1007/BF01731581 contributor: fullname: Kimura – volume: 64 year: 2017 ident: B44 article-title: Virus-Driven Inflammation Is Associated With the Development of Bnabs in Spontaneous Controllers of HIV publication-title: Clin Infect Dis doi: 10.1093/cid/cix057 contributor: fullname: Dugast – volume: 176 year: 1997 ident: B17 article-title: Neutralizing Antibody Responses to Human Immunodeficiency Virus Type 1 in Primary Infection and Long-Term-Nonprogressive Infection publication-title: J Infect Dis doi: 10.1086/516508 contributor: fullname: Pilgrim – volume: 85 year: 2011 ident: B12 article-title: Broadly Cross-Neutralizing Antibodies in HIV-1 Patients With Undetectable Viremia publication-title: J Virol doi: 10.1128/JVI.02482-10 contributor: fullname: Medina-Ramirez – volume: 13 start-page: e0193773 year: 2018 ident: B15 article-title: Characterization of Broadly Neutralizing Antibody Responses to HIV-1 in a Cohort of Long Term Non-Progressors publication-title: PloS One doi: 10.1371/journal.pone.0193773 contributor: fullname: Gonzalez – volume: 84 year: 2010 ident: B8 article-title: Breadth of Human Immunodeficiency Virus-Specific Neutralizing Activity in Sera: Clustering Analysis and Association With Clinical Variables publication-title: J Virol doi: 10.1128/JVI.01482-09 contributor: fullname: Doria-Rose – volume: 108 year: 2011 ident: B28 article-title: Broadly Neutralizing Human Antibody That Recognizes the Receptor-Binding Pocket of Influenza Virus Hemagglutinin publication-title: Proc Natl Acad Sci USA doi: 10.1073/pnas.1111497108 contributor: fullname: Whittle – volume: 85 year: 2011 ident: B30 article-title: Dynamic Antibody Specificities and Virion Concentrations in Circulating Immune Complexes in Acute to Chronic HIV-1 Infection publication-title: J Virol doi: 10.1128/JVI.05601-11 contributor: fullname: Liu – volume: 561 year: 2018 ident: B61 article-title: Tracing HIV-1 Strains That Imprint Broadly Neutralizing Antibody Responses publication-title: Nature doi: 10.1038/s41586-018-0517-0 contributor: fullname: Kouyos – volume: 485 start-page: 395 year: 2009 ident: B18 article-title: Measuring HIV Neutralization in a Luciferase Reporter Gene Assay publication-title: Methods Mol Biol doi: 10.1007/978-1-59745-170-3_26 contributor: fullname: Montefiori – volume: 16 year: 2019 ident: B1 article-title: The Antibodiome-Mapping the Humoral Immune Response to HIV publication-title: Curr HIV/AIDS Rep doi: 10.1007/s11904-019-00432-x contributor: fullname: Butler – volume: 329 year: 2010 ident: B22 article-title: Rational Design of Envelope Identifies Broadly Neutralizing Human Monoclonal Antibodies to HIV-1 publication-title: Science doi: 10.1126/science.1187659 contributor: fullname: Wu – volume: 458 year: 2009 ident: B60 article-title: Broad Diversity of Neutralizing Antibodies Isolated From Memory B Cells in HIV-Infected Individuals publication-title: Nature doi: 10.1038/nature07930 contributor: fullname: Scheid – volume: 12 start-page: e1005817 year: 2016 ident: B24 article-title: Antibody-Mediated Internalization of Infectious HIV-1 Virions Differs Among Antibody Isotypes and Subclasses publication-title: PloS Pathog doi: 10.1371/journal.ppat.1005817 contributor: fullname: Tay – volume: 80 year: 2006 ident: B7 article-title: Neutralizing Antibodies Do Not Mediate Suppression of Human Immunodeficiency Virus Type 1 in Elite Suppressors or Selection of Plasma Virus Variants in Patients on Highly Active Antiretroviral Therapy publication-title: J Virol doi: 10.1128/JVI.80.10.4758-4770.2006 contributor: fullname: Bailey – volume: 92 year: 2018 ident: B20 article-title: HIV-1 Envelope Glycoproteins From Diverse Clades Differentiate Antibody Responses and Durability Among Vaccinees publication-title: J Virol doi: 10.1128/JVI.01843-17 contributor: fullname: Yates – volume: 23 start-page: 897 year: 2009 ident: B6 article-title: Heterogeneous Neutralizing Antibody and Antibody-Dependent Cell Cytotoxicity Responses in HIV-1 Elite Controllers publication-title: Aids doi: 10.1097/QAD.0b013e328329f97d contributor: fullname: Lambotte – volume: 11 start-page: e1004658 year: 2015 ident: B48 article-title: Identification of Effective Subdominant Anti-HIV-1 CD8+ T Cells Within Entire Post-Infection and Post-Vaccination Immune Responses publication-title: PloS Pathog doi: 10.1371/journal.ppat.1004658 contributor: fullname: Hancock – volume: 9 start-page: 10165 year: 2019 ident: B47 article-title: HLA Class II-Restricted CD8+ T Cells in HIV-1 Virus Controllers publication-title: Sci Rep doi: 10.1038/s41598-019-46462-8 contributor: fullname: Nyanhete – volume: 375 start-page: 57 year: 2012 ident: B19 article-title: Development and Implementation of an International Proficiency Testing Program for a Neutralizing Antibody Assay for HIV-1 in TZM-Bl Cells publication-title: J Immunol Methods doi: 10.1016/j.jim.2011.09.007 contributor: fullname: Todd – volume: 15 start-page: 61 year: 2018 ident: B57 article-title: Development of Broadly Neutralizing Antibodies in HIV-1 Infected Elite Neutralizers publication-title: Retrovirology doi: 10.1186/s12977-018-0443-0 contributor: fullname: Landais – volume: 202 start-page: 595 year: 2010 ident: B41 article-title: Magnitude and Breadth of a Nonprotective Neutralizing Antibody Response in an Efficacy Trial of a Candidate HIV-1 Gp120 Vaccine publication-title: J Infect Dis doi: 10.1086/654816 contributor: fullname: Gilbert – volume: 25 year: 2004 ident: B33 article-title: UCSF Chimera–A Visualization System for Exploratory Research and Analysis publication-title: J Comput Chem doi: 10.1002/jcc.20084 contributor: fullname: Pettersen – volume: 1 start-page: 81 year: 2009 ident: B39 article-title: Simultaneous Evaluation of the Magnitude and Breadth of a Left and Right Censored Multivariate Response, With Application to HIV Vaccine Development publication-title: Stat Biopharm Res doi: 10.1198/sbr.2009.0008 contributor: fullname: Huang – volume: 179 year: 1999 ident: B5 article-title: A Longitudinal Study of Neutralizing Antibodies and Disease Progression in HIV-1-Infected Subjects publication-title: J Infect Dis doi: 10.1086/314773 contributor: fullname: Cecilia – volume: 22 year: 2016 ident: B9 article-title: Determinants of HIV-1 Broadly Neutralizing Antibody Induction publication-title: Nat Med doi: 10.1038/nm.4187 contributor: fullname: Rusert – volume: 84 start-page: 4998 year: 2010 ident: B49 article-title: Phenotypic and Functional Profile of HIV-Inhibitory CD8 T Cells Elicited by Natural Infection and Heterologous Prime/Boost Vaccination publication-title: J Virol doi: 10.1128/JVI.00138-10 contributor: fullname: Freel – volume: 57 start-page: 9 year: 2011 ident: B4 article-title: Correlation Between Circulating HIV-1 RNA and Broad HIV-1 Neutralizing Antibody Activity publication-title: J Acquir Immune Defic Syndr doi: 10.1097/QAI.0b013e3182100c1b contributor: fullname: Sajadi – volume: 32 year: 2016 ident: B42 article-title: The Neutralizing Antibody Response in an Individual With Triple HIV-1 Infection Remains Directed at the First Infecting Subtype publication-title: AIDS Res Hum Retroviruses doi: 10.1089/aid.2015.0324 contributor: fullname: Cornelissen – volume: 30 start-page: 984 year: 2020 ident: B59 article-title: Immunological Fingerprints of Controllers Developing Neutralizing HIV-1 Antibodies publication-title: Cell Rep doi: 10.1016/j.celrep.2019.12.087 contributor: fullname: Martin-Gayo – volume: 22 year: 1994 ident: B35 article-title: CLUSTAL W: Improving the Sensitivity of Progressive Multiple Sequence Alignment Through Sequence Weighting, Position-Specific Gap Penalties and Weight Matrix Choice publication-title: Nucleic Acids Res doi: 10.1093/nar/22.22.4673 contributor: fullname: Thompson – volume: 93 year: 2019 ident: B55 article-title: A Highly Unusual V1 Region of Env in an Elite Controller of HIV Infection publication-title: J Virol doi: 10.1128/JVI.00094-19 contributor: fullname: Silver – volume: 88 year: 2014 ident: B29 article-title: Capacity for Infectious HIV-1 Virion Capture Differs by Envelope Antibody Specificity publication-title: J Virol doi: 10.1128/JVI.03765-13 contributor: fullname: Liu – volume: 11 start-page: 520 year: 2020 ident: B27 article-title: Disruption of the HIV-1 Envelope Allosteric Network Blocks CD4-Induced Rearrangements publication-title: Nat Commun doi: 10.1038/s41467-019-14196-w contributor: fullname: Henderson – volume: 4 year: 1987 ident: B37 article-title: The Neighbor-Joining Method: A New Method for Reconstructing Phylogenetic Trees publication-title: Mol Biol Evol doi: 10.1093/oxfordjournals.molbev.a040454 contributor: fullname: Saitou – volume: 15 start-page: 70 year: 2018 ident: B56 article-title: The Expanding Array of HIV Broadly Neutralizing Antibodies publication-title: Retrovirology doi: 10.1186/s12977-018-0453-y contributor: fullname: McCoy – volume: 13 year: 2013 ident: B10 article-title: Unravelling the Mechanisms of Durable Control of HIV-1 publication-title: Nat Rev Immunol doi: 10.1038/nri3478 contributor: fullname: Walker – volume: 165 year: 2016 ident: B63 article-title: Maturation Pathway From Germline to Broad HIV-1 Neutralizer of a CD4-Mimic Antibody publication-title: Cell doi: 10.1016/j.cell.2016.02.022 contributor: fullname: Bonsignori – volume: 201 year: 2018 ident: B31 article-title: Qualified Biolayer Interferometry Avidity Measurements Distinguish the Heterogeneity of Antibody Interactions With Plasmodium Falciparum Circumsporozoite Protein Antigens publication-title: J Immunol doi: 10.4049/jimmunol.1800323 contributor: fullname: Dennison – volume: 93 year: 2019 ident: B26 article-title: Rare Detection of Antiviral Functions of Polyclonal IgA Isolated From Plasma and Breast Milk Compartments in Women Chronically Infected With HIV-1 publication-title: J Virol doi: 10.1128/JVI.02084-18 contributor: fullname: Tay – volume: 201 year: 2010 ident: B11 article-title: Cross-Reactive Neutralizing Humoral Immunity Does Not Protect From HIV Type 1 Disease Progression publication-title: J Infect Dis doi: 10.1086/651144 contributor: fullname: Euler – volume: 13 start-page: e1006148 year: 2017 ident: B32 article-title: Mapping Polyclonal HIV-1 Antibody Responses via Next-Generation Neutralization Fingerprinting publication-title: PloS Pathog doi: 10.1371/journal.ppat.1006148 contributor: fullname: Doria-Rose |
| SSID | ssj0000493335 |
| Score | 2.3499672 |
| Snippet | Broadly neutralizing antibodies (bNAbs), known to mediate immune control of HIV-1 infection, only develop in a small subset of HIV-1 infected individuals.... |
| SourceID | doaj pubmedcentral proquest crossref pubmed |
| SourceType | Open Website Open Access Repository Aggregation Database Index Database |
| StartPage | 670561 |
| SubjectTerms | Antibody Specificity antibody-dependent cellular phagocytosis (ADCP) Binding Sites, Antibody broadly neutralizing antibodies Broadly Neutralizing Antibodies - immunology CD4 Antigens - immunology CD4 Antigens - metabolism CD4 Lymphocyte Count CD4-binding site antibodies Epitope Mapping Epitopes - immunology Female Genes, env HIV Antibodies - immunology HIV Envelope Protein gp120 - immunology HIV Infections - immunology HIV-1 - immunology HIV-1 Virus Controllers HLA-B Antigens - immunology Humans Immune Evasion Immunoglobulin Fc Fragments - immunology Immunoglobulin Fragments - immunology Immunology Male Models, Molecular negative-stain electron microscopy neutralization fingerprinting assay Peptide Fragments - immunology Phagocytosis Protein Domains Recombinant Proteins - immunology Survivors Viral Load Viremia - immunology |
| SummonAdditionalLinks | – databaseName: DOAJ Directory of Open Access Journals dbid: DOA link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV1Lj9MwELbQSkhcEG_CS4PECcls4leSY7ewFA4rJNhqb5Yd2yKom6Dd5ND9G_xhxnFbtQiJC1cncSx_Y8_3xZMZQt7UuWNeMUtlbgMVwUtqG84obpeyqJyKkiNGW5ypxbn4fCEv9kp9xZiwlB44TdyxaFThg0RH44TgPre58cKH3LrK40abspcWck9M_Ui8l3Mu0zEmqrD6OLSXlyPqQVa8U2WkzQeOaMrX_zeS-Wes5J7zOb1H7m5YI8zSaO-TW757QG6nOpLrh-TXl361blaRVAPqauNWazjz4_QR4wZ9E8y6obW9W8OsSdUiYL5L1HzjHVhseC_gpJ3-cYGvyEPBdA6WnH7Enk237QF1NbQdGIgbjh-gD7D4tKQFLNur8RrmKfB9hZzyETk__fBtvqCbagu0EUoOlDfK27oy0hqmalVOuctEUdvgHHMqRCblrfTM1IirR0RlcBafKQQzoWT8MTnq-s4_JcBxYVtEp8TFL6IAZc4EyRtUk2VwucnI2-3U658pqYZGMRJx0hNOOuKkE04ZOYng7G6M-bCnBrQSvbES_S8rycjrLbQa1088FDGd78drjQqyijVuCpGRJwnq3au4nCQWz0h5YAQHYzm80rXfpxzdVYn2x6pn_2Pwz8mdOB8xiIbxF-RouBr9S6RCg301Wf1v8kQI7A priority: 102 providerName: Directory of Open Access Journals – databaseName: Scholars Portal Open Access Journals dbid: M48 link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwdV1bi9QwFA7rirIv4t16I4JPQtc2t7YPIrOj6yi4CDrDvpWkSbTSTXWmBbt_wz_sSS-DI-Nr2qRpvnOS72vScxB6nkWaGEFUyCNlQ2YND1VBSQjTJY9TLbzk8KctzsRiyT6c8_MDNKW3Ggdws1fa-XxSy3V1_Otn9xoc_pVXnLDevrTlxUULUo_ExyLxjPgKukoYZd7gP45s__tAhimlfNjb3F_zCF2nvOfVdGeh6uP57yOh_56l_GtxOr2JboysEs8GM7iFDoy7ja4NeSa7O-j3p7rqisqTbgy6W-qqw2em7T9yXMLahWeuKVWtOzwrhmwSeL4N5HxpNFZQ8Ibhk7L_BwZ_Bp6KpdN4RcN30LJ0Uwugu3HpsMR-QjINri1evF-FMV6V63aD58PB-Ao45120PH37Zb4Ix2wMYcEEb0JaCKOyVHIlichE0sc2Y3GmrNZEC-uZllHcEJkB7gYQ51YrqBMzIm1C6D106GpnHiBMwfGVEUkCkwPzApVoaTktQG0mVkcyQC-moc9_DEE3chArHrK8hyz3kOUDZAE68eBsb_TxsvuCev01H90vZ4WIjeVAVzRj1EQqkoYZGymdQj9SHqBnE7Q5-JffNJHO1O0mB4WZ-hw4MQvQ_QHq7aMmUwlQsmMEO33ZveLKb30M7zQBUyTpw_-2-Qgd-Zf0J2cIfYwOm3VrngD_adTT3qr_AAOpA58 priority: 102 providerName: Scholars Portal |
| Title | Polyclonal Broadly Neutralizing Antibody Activity Characterized by CD4 Binding Site and V3-Glycan Antibodies in a Subset of HIV-1 Virus Controllers |
| URI | https://www.ncbi.nlm.nih.gov/pubmed/35003053 https://www.proquest.com/docview/2618513314/abstract/ https://pubmed.ncbi.nlm.nih.gov/PMC8733328 https://doaj.org/article/4c61ef5241d443e0b0ae4ef0bd8e6785 |
| Volume | 12 |
| hasFullText | 1 |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1ba9swFBZtYaMvY_d5l6LBngZObN1sP6bZ2mzQUtga8mYkS9o8Ermk9kP6N_aHdyTHoRl72oswli9C35H0ffLxOQh9KBJNjCAq5omyMbOGx6qiJIbpkqe5Fl5yeG-LSzG7Zl8XfHGA-PAvTHDar1Q9csvVyNU_g2_lzaoaD35i46uLaZ5RSkk-PkSHcHRPov_qKS_U8v4LJgiwYmzr1aoDKUjSkcg8Yz5GDykP7JnuLUchav-_qObfHpP3lqCzx-jRljviSd_GJ-jAuKfoQZ9NcvMM_b5qlptq6ak1BnUt9XKDL00XtjLuYIXCE9fWqtEbPKn6nBF4ugvXfGc0VnDiE8OndfjTBX8DNoql03hO43N4snTDE0Bd49phif20Y1rcWDz7Mo9TPK_X3S2e9u7vS2CWz9H12efv01m8zbkQV0zwNqaVMKrIJVeSiEJkIYIZSwtltSZaWM-njOKGyALQNYArt1rBPSkj0maEvkBHrnHmFcIUhrcyIstgCmBehhItLacVaMrM6kRG6OPQ9eVNH1qjBEniISsDZKWHrOwhi9CpB2d3oY-KHU406x_l1jZKVonUWA6kRDNGTaISaZixidI5tCPnEXo_QFvCKPKfRqQzTXdbgo7MfaablEXoZQ_17lWDqUQo2zOCvbbs14DhhkjdW0N9_d93vkHHvhO8_wyhb9FRu-7MO2BBrToJuwdQni9SKC9YfhLGwR_qDAus |
| link.rule.ids | 230,315,733,786,790,870,891,2115,24346,27957,27958,53827,53829 |
| linkProvider | National Library of Medicine |
| linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1bb9MwFLbGELAXrgPK1Ug8IaVNfEvy2BVGB1s1ia3aW2THNgTaZOqSh_Zv8Ic5dppqnXiB1zh2nPjz8ffFx-cg9D4NNTGCqICHygbMGh6onJIAzCWPEi2c5HDeFhMxPmdfLvjFDuLdWRjvtJ-rol_O5v2y-OF9Ky_n-aDzExucnoySmFJKksEtdBvmK4mvifSfLemFct7uYYIESwe2mM8bEIMk6ovYceY9dJdyz5_p1oLk4_b_jWze9Jm8tggdPkDTrvut78mvflOrfr66Ednxn9_vIbq_pqV42BY_QjumfIzutIkql0_Q79NqtsxnjrVjEO5Sz5Z4Yhr_l2QFix8elnWhKr3Ew7xNR4FHm0jQK6OxggsfGT4o_CEa_A2ILpalxlMafIaWZdm1AMIdFyWW2Fk0U-PK4vHRNIjwtFg0V3jUetbPgLTuo_PDT2ejcbBO5xDkTPA6oLkwKk0kV5KIVMQ-OBqLUmW1JlpYR9WM4obIFIBjADLcagV1IkakjQl9inbLqjTPEaZgOZQRcQzWhTmFS7S0nOYgV2OrQ9lDH7oxzS7bqB0ZqB2HhcxjIXNYyFos9NCBG_XNjS7gtr9QLb5n62HJWC4iYznwHc0YNaEKpWHGhkon0I-E99C7DjMZTFC36yJLUzVXGUjUxCXRiVgPPWsxtHlUh8EeirfQtdWX7RLAjA8CvsbIi_-u-RbdG5-dHGfHR5OvL9Ge-yDOTYfQV2i3XjTmNZCtWr3xU-sPtiYq5g |
| linkToPdf | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3JbtswECXaFA1y6Z7GXVmgpwKyJS5ajo5T1-liGGhjBL0IpEi2amzJcKSD_Rv94Q4py7CDnnKVSIoUH4fviaMZhN4nviI6JNLjvjQeM5p7MqPEA3PJg1iFVnJYb4txOLpgny_55U6qL-e0n8m8W8zm3SL_7XwrF_Os1_qJ9SbfBnFEKSVxb6FM7y66B2uWJDtC_U9DfKEMb84xQYYlPZPP5zUIQhJ0w8jy5iN0SLnj0HRvU3Kx-_9HOG_6Te5sRMOH6Gc7hMb_5KpbV7KbrW9Ed7zVGB-hBxt6ivtNkcfoji6eoPtNwsrVU_R3Us5W2cyydwwCXqjZCo917b6WrGETxP2iymWpVrifNWkp8GAbEXqtFZZw4Yzh09z9TIO_A-HFolB4Sr1P0LIo2hZAwOO8wAJby6YrXBo8Op96AZ7my_oaDxoP-xmQ12foYvjxx2DkbdI6eBkLeeXRLNQyiQWXgoRJGLkgaSxIpFGKqNBYyqYl10QkACAN0OFGSagTMCJMROgxOijKQp8gTMGCSB1GEVgZZpUuUcJwmoFsjYzyRQd9aOc1XTTRO1JQPRYPqcNDavGQNnjooFM789uCNvC2u1Auf6WbqUlZFgbacOA9ijGqfekLzbTxpYqhHzHvoHctblJYqPb0RRS6rK9TkKqxTaYTsA563uBo-6gWhx0U7SFsry_7dwA3Lhj4Bicvbl3zLTqcnA3Tr-fjLy_RkX0f1luH0FfooFrW-jVwrkq-cavrH_u3LWY |
| 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=Polyclonal+Broadly+Neutralizing+Antibody+Activity+Characterized+by+CD4+Binding+Site+and+V3-Glycan+Antibodies+in+a+Subset+of+HIV-1+Virus+Controllers&rft.jtitle=Frontiers+in+immunology&rft.au=Nyanhete%2C+Tinashe+E&rft.au=Edwards%2C+Robert+J&rft.au=LaBranche%2C+Celia+C&rft.au=Mansouri%2C+Katayoun&rft.date=2021-12-23&rft.eissn=1664-3224&rft.volume=12&rft.spage=670561&rft_id=info:doi/10.3389%2Ffimmu.2021.670561&rft_id=info%3Apmid%2F35003053&rft.externalDocID=35003053 |
| thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1664-3224&client=summon |
| thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1664-3224&client=summon |
| thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1664-3224&client=summon |