Monoclonal antibodies to the V2 domain of MN-rgp120: fine mapping of epitopes and inhibition of α4β7 binding

Recombinant gp120 (MN-rgp120) was a major component of the AIDSVAX B/E vaccine used in the RV144 trial. This was the first clinical trial to show that vaccination could prevent HIV infection in humans. A recent RV144 correlates of protection study found that protection correlated with the presence o...

Full description

Saved in:
Bibliographic Details
Published inPloS one Vol. 7; no. 6; p. e39045
Main Authors Nakamura, Gerald R, Fonseca, Dora P A J, O'Rourke, Sara M, Vollrath, Aaron L, Berman, Phillip W
Format Journal Article
LanguageEnglish
Published United States Public Library of Science 13.06.2012
Public Library of Science (PLoS)
Subjects
Online AccessGet full text

Cover

Loading…
Abstract Recombinant gp120 (MN-rgp120) was a major component of the AIDSVAX B/E vaccine used in the RV144 trial. This was the first clinical trial to show that vaccination could prevent HIV infection in humans. A recent RV144 correlates of protection study found that protection correlated with the presence of antibodies to the V2 domain. It has been proposed that antibodies to the α4β7 binding site in the V2 domain might prevent HIV-1 infection by blocking the ability of virions to recognize α4β7 on activated T-cells. In this study we investigated the specificity of monoclonal antibodies (MAbs) to the V2 domain of MN-rgp120 and examined the possibility that these antibodies could inhibit the binding of MN-rgp120 to the α4β7 integrin. Nine MAbs to the V2 domain were isolated from mice immunized with recombinant envelope proteins. The ability of these MAbs to inhibit HIV infection, block the binding of gp120 to CD4, and block the binding of MN-rgp120 to the α4β7 integrin was measured. Mutational analysis showed that eight of the MAbs recognized two immunodominant clusters of amino acids (166-168 and 178-183) located at either end of the C strand within the four-strand anti-parallel sheet structure comprising the V1/V2 domain. These studies showed that the antigenic structure of the V2 domain is exceedingly complex and that MAbs isolated from mice immunized with MN-rgp120 exhibited a high level of strain specificity compared to MAbs to the V2 domain isolated from HIV-infected humans. We found that immunization with MN-rgp120 readily elicits antibodies to the V2 domain and some of these were able to block the binding of MN-rgp120 to the α4β7 integrin.
AbstractList Recombinant gp120 (MN-rgp120) was a major component of the AIDSVAX B/E vaccine used in the RV144 trial. This was the first clinical trial to show that vaccination could prevent HIV infection in humans. A recent RV144 correlates of protection study found that protection correlated with the presence of antibodies to the V2 domain. It has been proposed that antibodies to the α4β7 binding site in the V2 domain might prevent HIV-1 infection by blocking the ability of virions to recognize α4β7 on activated T-cells. In this study we investigated the specificity of monoclonal antibodies (MAbs) to the V2 domain of MN-rgp120 and examined the possibility that these antibodies could inhibit the binding of MN-rgp120 to the α4β7 integrin. Nine MAbs to the V2 domain were isolated from mice immunized with recombinant envelope proteins. The ability of these MAbs to inhibit HIV infection, block the binding of gp120 to CD4, and block the binding of MN-rgp120 to the α4β7 integrin was measured. Mutational analysis showed that eight of the MAbs recognized two immunodominant clusters of amino acids (166-168 and 178-183) located at either end of the C strand within the four-strand anti-parallel sheet structure comprising the V1/V2 domain. These studies showed that the antigenic structure of the V2 domain is exceedingly complex and that MAbs isolated from mice immunized with MN-rgp120 exhibited a high level of strain specificity compared to MAbs to the V2 domain isolated from HIV-infected humans. We found that immunization with MN-rgp120 readily elicits antibodies to the V2 domain and some of these were able to block the binding of MN-rgp120 to the α4β7 integrin.
Background Recombinant gp120 (MN-rgp120) was a major component of the AIDSVAX B/E vaccine used in the RV144 trial. This was the first clinical trial to show that vaccination could prevent HIV infection in humans. A recent RV144 correlates of protection study found that protection correlated with the presence of antibodies to the V2 domain. It has been proposed that antibodies to the α4β7 binding site in the V2 domain might prevent HIV-1 infection by blocking the ability of virions to recognize α4β7 on activated T-cells. In this study we investigated the specificity of monoclonal antibodies (MAbs) to the V2 domain of MN-rgp120 and examined the possibility that these antibodies could inhibit the binding of MN-rgp120 to the α4β7 integrin. Methodology/Principal Findings Nine MAbs to the V2 domain were isolated from mice immunized with recombinant envelope proteins. The ability of these MAbs to inhibit HIV infection, block the binding of gp120 to CD4, and block the binding of MN-rgp120 to the α4β7 integrin was measured. Mutational analysis showed that eight of the MAbs recognized two immunodominant clusters of amino acids (166–168 and 178–183) located at either end of the C strand within the four-strand anti-parallel sheet structure comprising the V1/V2 domain. Conclusions/Significance These studies showed that the antigenic structure of the V2 domain is exceedingly complex and that MAbs isolated from mice immunized with MN-rgp120 exhibited a high level of strain specificity compared to MAbs to the V2 domain isolated from HIV-infected humans. We found that immunization with MN-rgp120 readily elicits antibodies to the V2 domain and some of these were able to block the binding of MN-rgp120 to the α4β7 integrin.
BackgroundRecombinant gp120 (MN-rgp120) was a major component of the AIDSVAX B/E vaccine used in the RV144 trial. This was the first clinical trial to show that vaccination could prevent HIV infection in humans. A recent RV144 correlates of protection study found that protection correlated with the presence of antibodies to the V2 domain. It has been proposed that antibodies to the α4β7 binding site in the V2 domain might prevent HIV-1 infection by blocking the ability of virions to recognize α4β7 on activated T-cells. In this study we investigated the specificity of monoclonal antibodies (MAbs) to the V2 domain of MN-rgp120 and examined the possibility that these antibodies could inhibit the binding of MN-rgp120 to the α4β7 integrin.Methodology/principal findingsNine MAbs to the V2 domain were isolated from mice immunized with recombinant envelope proteins. The ability of these MAbs to inhibit HIV infection, block the binding of gp120 to CD4, and block the binding of MN-rgp120 to the α4β7 integrin was measured. Mutational analysis showed that eight of the MAbs recognized two immunodominant clusters of amino acids (166-168 and 178-183) located at either end of the C strand within the four-strand anti-parallel sheet structure comprising the V1/V2 domain.Conclusions/significanceThese studies showed that the antigenic structure of the V2 domain is exceedingly complex and that MAbs isolated from mice immunized with MN-rgp120 exhibited a high level of strain specificity compared to MAbs to the V2 domain isolated from HIV-infected humans. We found that immunization with MN-rgp120 readily elicits antibodies to the V2 domain and some of these were able to block the binding of MN-rgp120 to the α4β7 integrin.
Background Recombinant gp120 (MN-rgp120) was a major component of the AIDSVAX B/E vaccine used in the RV144 trial. This was the first clinical trial to show that vaccination could prevent HIV infection in humans. A recent RV144 correlates of protection study found that protection correlated with the presence of antibodies to the V2 domain. It has been proposed that antibodies to the α4β7 binding site in the V2 domain might prevent HIV-1 infection by blocking the ability of virions to recognize α4β7 on activated T-cells. In this study we investigated the specificity of monoclonal antibodies (MAbs) to the V2 domain of MN-rgp120 and examined the possibility that these antibodies could inhibit the binding of MN-rgp120 to the α4β7 integrin. Methodology/Principal Findings Nine MAbs to the V2 domain were isolated from mice immunized with recombinant envelope proteins. The ability of these MAbs to inhibit HIV infection, block the binding of gp120 to CD4, and block the binding of MN-rgp120 to the α4β7 integrin was measured. Mutational analysis showed that eight of the MAbs recognized two immunodominant clusters of amino acids (166–168 and 178–183) located at either end of the C strand within the four-strand anti-parallel sheet structure comprising the V1/V2 domain. Conclusions/Significance These studies showed that the antigenic structure of the V2 domain is exceedingly complex and that MAbs isolated from mice immunized with MN-rgp120 exhibited a high level of strain specificity compared to MAbs to the V2 domain isolated from HIV-infected humans. We found that immunization with MN-rgp120 readily elicits antibodies to the V2 domain and some of these were able to block the binding of MN-rgp120 to the α4β7 integrin.
Author Vollrath, Aaron L
O'Rourke, Sara M
Nakamura, Gerald R
Berman, Phillip W
Fonseca, Dora P A J
AuthorAffiliation University of California San Francisco, United States of America
1 Antibody Engineering Department, Genentech, Incorporated, South San Francisco, California, United States of America
2 Department of Biomolecular Engineering, University of California Santa Cruz, Santa Cruz, California, United States of America
AuthorAffiliation_xml – name: University of California San Francisco, United States of America
– name: 2 Department of Biomolecular Engineering, University of California Santa Cruz, Santa Cruz, California, United States of America
– name: 1 Antibody Engineering Department, Genentech, Incorporated, South San Francisco, California, United States of America
Author_xml – sequence: 1
  givenname: Gerald R
  surname: Nakamura
  fullname: Nakamura, Gerald R
  organization: Antibody Engineering Department, Genentech, Incorporated, South San Francisco, California, United States of America
– sequence: 2
  givenname: Dora P A J
  surname: Fonseca
  fullname: Fonseca, Dora P A J
– sequence: 3
  givenname: Sara M
  surname: O'Rourke
  fullname: O'Rourke, Sara M
– sequence: 4
  givenname: Aaron L
  surname: Vollrath
  fullname: Vollrath, Aaron L
– sequence: 5
  givenname: Phillip W
  surname: Berman
  fullname: Berman, Phillip W
BackLink https://www.ncbi.nlm.nih.gov/pubmed/22720026$$D View this record in MEDLINE/PubMed
BookMark eNp1kstuFDEQRS2UiDzgDxBYYt0Tv9ruZoEURTwiJWEDbC27XZ7xqMdu7B4kPgs-JN9ET6YTJYusbFXde6pUuifoIKYICL2hZEG5omfrtM3R9IthKi8I4S0R9Qt0TFvOKskIP3j0P0InpawJqXkj5Ut0xJhihDB5jOJ1iqnr00TCJo7BJheg4DHhcQX4J8MubUyIOHl8fVPl5UAZ-YB9iIA3ZhhCXO5aMIQxDZPPRIdDXAUbxpDuXLd_xe0_hW2IbhK_Qofe9AVez-8p-vH50_eLr9XVty-XF-dXVScErSvFPLRKGdtQkBakcV1tuXeNBe89EC67jltPoeWKUeqIY9Q6qmrh64Y4z0_Ruz136FPR86mKppzVhCmlyKS43CtcMms95LAx-Y9OJui7QspLbfIYuh607IT0jkkvDQjbuoYJSw1xwkrRMsYm1sd52tZuwHUQx2z6J9CnnRhWepl-a86VUKqZAO9nQE6_tlDGZ1YWe1WXUykZ_MMESvQuE_cuvcuEnjMx2d4-3u7BdB8C_h_5rrjE
CitedBy_id crossref_primary_10_1073_pnas_2011501117
crossref_primary_10_1128_JVI_01005_17
crossref_primary_10_1128_JVI_02325_16
crossref_primary_10_1074_jbc_M114_554089
crossref_primary_10_4161_hv_28462
crossref_primary_10_1371_journal_ppat_1007278
crossref_primary_10_1371_journal_pone_0053629
crossref_primary_10_1016_j_isci_2021_102047
crossref_primary_10_1128_JVI_03008_15
crossref_primary_10_1586_14760584_2014_951335
crossref_primary_10_1016_j_molimm_2016_07_003
crossref_primary_10_1371_journal_pone_0143895
crossref_primary_10_1371_journal_pone_0094002
crossref_primary_10_1016_j_vaccine_2016_04_027
crossref_primary_10_1097_COH_0b013e3283632c26
crossref_primary_10_1089_aid_2014_0034
crossref_primary_10_1016_j_vaccine_2014_07_026
crossref_primary_10_1371_journal_ppat_1011860
crossref_primary_10_1080_21645515_2020_1787070
crossref_primary_10_1128_JVI_03153_13
crossref_primary_10_1016_j_molimm_2014_06_025
crossref_primary_10_1016_j_jim_2013_12_007
crossref_primary_10_1016_j_virol_2015_10_010
crossref_primary_10_1126_scitranslmed_aau4711
crossref_primary_10_1128_JVI_01352_12
crossref_primary_10_1186_1471_2105_15_77
crossref_primary_10_1128_JVI_03296_13
crossref_primary_10_4049_jimmunol_2001010
crossref_primary_10_1016_j_virol_2019_01_011
crossref_primary_10_1016_j_jim_2018_11_015
crossref_primary_10_3390_vaccines7030082
crossref_primary_10_1128_CVI_00230_14
crossref_primary_10_3390_vaccines8040681
crossref_primary_10_1038_nm_3715
crossref_primary_10_1089_vim_2012_0046
Cites_doi 10.1128/JVI.01899-08
10.1006/viro.1999.0031
10.1001/jama.1994.03520060075035
10.1002/j.1460-2075.1990.tb08274.x
10.1086/428405
10.1128/JVI.66.2.848-856.1992
10.1128/JVI.67.8.4932-4944.1993
10.1126/science.1178746
10.1128/JVI.72.10.7840-7845.1998
10.1128/JVI.78.10.5205-5215.2004
10.1016/0042-6822(73)90341-3
10.1016/0092-8674(90)90802-L
10.1016/0042-6822(88)90568-5
10.1128/JVI.02658-10
10.1089/aid.1992.8.1875
10.1371/journal.ppat.1001028
10.4049/jimmunol.153.2.517
10.1073/pnas.82.2.488
10.1038/news.2011.541
10.1128/JVI.66.7.4464-4469.1992
10.1128/JVI.05045-11
10.1038/nri2801
10.4049/jimmunol.159.3.1497
10.4049/jimmunol.142.3.773
10.1128/JVI.00790-10
10.1128/JVI.68.12.8312-8320.1994
10.1093/infdis/jis367
10.1128/JVI.79.14.9069-9080.2005
10.1093/infdis/173.1.52
10.1128/JVI.69.4.2271-2278.1995
10.1128/JVI.79.8.5232-5237.2005
10.1093/molbev/msp254
10.4049/jimmunol.178.10.6596
10.1086/508748
10.1038/313450a0
10.1126/science.1118398
10.1056/NEJMoa1113425
10.1128/JVI.67.6.3656-3659.1993
10.1038/ni1566
10.1002/0471142735.im1211s64
10.1128/JVI.79.11.6909-6917.2005
10.1111/j.1749-6632.1975.tb29170.x
10.1038/nature10696
10.1086/428404
10.1128/JVI.02054-06
10.1073/pnas.0911796106
10.1016/S0021-9258(18)86956-3
10.1073/pnas.0802203105
10.1038/nature10373
10.1086/514055
10.1128/JVI.67.10.6179-6191.1993
10.1038/31405
10.1056/NEJMoa0908492
10.1111/j.1365-3083.1991.tb01601.x
10.1146/annurev.immunol.24.021605.090557
10.1128/JVI.69.1.222-230.1995
10.1128/JVI.70.7.4466-4473.1996
ContentType Journal Article
Copyright 2012 Nakamura et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.
Nakamura et al. 2012
Copyright_xml – notice: 2012 Nakamura et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.
– notice: Nakamura et al. 2012
DBID CGR
CUY
CVF
ECM
EIF
NPM
AAYXX
CITATION
3V.
7QG
7QL
7QO
7RV
7SN
7SS
7T5
7TG
7TM
7U9
7X2
7X7
7XB
88E
8AO
8C1
8FD
8FE
8FG
8FH
8FI
8FJ
8FK
ABJCF
ABUWG
AFKRA
ARAPS
ATCPS
AZQEC
BBNVY
BENPR
BGLVJ
BHPHI
C1K
CCPQU
D1I
DWQXO
FR3
FYUFA
GHDGH
GNUQQ
H94
HCIFZ
K9.
KB.
KB0
KL.
L6V
LK8
M0K
M0S
M1P
M7N
M7P
M7S
NAPCQ
P5Z
P62
P64
PATMY
PDBOC
PIMPY
PQEST
PQQKQ
PQUKI
PRINS
PTHSS
PYCSY
RC3
5PM
DOA
DOI 10.1371/journal.pone.0039045
DatabaseName Medline
MEDLINE
MEDLINE (Ovid)
MEDLINE
MEDLINE
PubMed
CrossRef
ProQuest Central (Corporate)
Animal Behavior Abstracts
Bacteriology Abstracts (Microbiology B)
Biotechnology Research Abstracts
ProQuest Nursing & Allied Health Database
Ecology Abstracts
Entomology Abstracts (Full archive)
Immunology Abstracts
Meteorological & Geoastrophysical Abstracts
Nucleic Acids Abstracts
Virology and AIDS Abstracts
Agricultural Science Collection
Health & Medical Collection
ProQuest Central (purchase pre-March 2016)
Medical Database (Alumni Edition)
ProQuest Pharma Collection
ProQuest Public Health Database
Technology Research Database
ProQuest SciTech Collection
ProQuest Technology Collection
ProQuest Natural Science Collection
Hospital Premium Collection
Hospital Premium Collection (Alumni Edition)
ProQuest Central (Alumni) (purchase pre-March 2016)
Materials Science & Engineering Collection
ProQuest Central (Alumni)
ProQuest Central
Advanced Technologies & Aerospace Collection
Agricultural & Environmental Science Collection
ProQuest Central Essentials
Biological Science Collection
ProQuest Central
Technology Collection
Natural Science Collection
Environmental Sciences and Pollution Management
ProQuest One Community College
ProQuest Materials Science Collection
ProQuest Central Korea
Engineering Research Database
Health Research Premium Collection
Health Research Premium Collection (Alumni)
ProQuest Central Student
AIDS and Cancer Research Abstracts
SciTech Premium Collection
ProQuest Health & Medical Complete (Alumni)
https://resources.nclive.org/materials
Nursing & Allied Health Database (Alumni Edition)
Meteorological & Geoastrophysical Abstracts - Academic
ProQuest Engineering Collection
Biological Sciences
Agriculture Science Database
Health & Medical Collection (Alumni Edition)
PML(ProQuest Medical Library)
Algology Mycology and Protozoology Abstracts (Microbiology C)
Biological Science Database
Engineering Database
Nursing & Allied Health Premium
Advanced Technologies & Aerospace Database
ProQuest Advanced Technologies & Aerospace Collection
Biotechnology and BioEngineering Abstracts
Environmental Science Database
Materials Science Collection
Publicly Available Content Database
ProQuest One Academic Eastern Edition (DO NOT USE)
ProQuest One Academic
ProQuest One Academic UKI Edition
ProQuest Central China
Engineering Collection
Environmental Science Collection
Genetics Abstracts
PubMed Central (Full Participant titles)
Directory of Open Access Journals
DatabaseTitle MEDLINE
Medline Complete
MEDLINE with Full Text
PubMed
MEDLINE (Ovid)
CrossRef
Agricultural Science Database
Publicly Available Content Database
ProQuest Central Student
ProQuest Advanced Technologies & Aerospace Collection
ProQuest Central Essentials
Nucleic Acids Abstracts
SciTech Premium Collection
ProQuest Central China
Environmental Sciences and Pollution Management
Health Research Premium Collection
Meteorological & Geoastrophysical Abstracts
Natural Science Collection
Biological Science Collection
ProQuest Medical Library (Alumni)
Engineering Collection
Advanced Technologies & Aerospace Collection
Engineering Database
Virology and AIDS Abstracts
ProQuest Biological Science Collection
ProQuest One Academic Eastern Edition
Agricultural Science Collection
ProQuest Hospital Collection
ProQuest Technology Collection
Health Research Premium Collection (Alumni)
Biological Science Database
Ecology Abstracts
ProQuest Hospital Collection (Alumni)
Biotechnology and BioEngineering Abstracts
Environmental Science Collection
Entomology Abstracts
Nursing & Allied Health Premium
ProQuest Health & Medical Complete
ProQuest One Academic UKI Edition
Environmental Science Database
ProQuest Nursing & Allied Health Source (Alumni)
Engineering Research Database
ProQuest One Academic
Meteorological & Geoastrophysical Abstracts - Academic
Technology Collection
Technology Research Database
Materials Science Collection
ProQuest Health & Medical Complete (Alumni)
ProQuest Central (Alumni Edition)
ProQuest One Community College
ProQuest Natural Science Collection
ProQuest Pharma Collection
ProQuest Central
Genetics Abstracts
ProQuest Engineering Collection
Biotechnology Research Abstracts
Health and Medicine Complete (Alumni Edition)
ProQuest Central Korea
Bacteriology Abstracts (Microbiology B)
Algology Mycology and Protozoology Abstracts (Microbiology C)
Agricultural & Environmental Science Collection
AIDS and Cancer Research Abstracts
Materials Science Database
ProQuest Materials Science Collection
ProQuest Public Health
ProQuest Nursing & Allied Health Source
ProQuest SciTech Collection
Advanced Technologies & Aerospace Database
ProQuest Medical Library
Animal Behavior Abstracts
Materials Science & Engineering Collection
Immunology Abstracts
ProQuest Central (Alumni)
DatabaseTitleList MEDLINE
Agricultural Science Database


Database_xml – sequence: 1
  dbid: DOA
  name: 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
– sequence: 4
  dbid: 8FG
  name: ProQuest Technology Collection
  url: https://search.proquest.com/technologycollection1
  sourceTypes: Aggregation Database
DeliveryMethod fulltext_linktorsrc
Discipline Sciences (General)
Medicine
Biology
DocumentTitleAlternate Monoclonal Antibodies to the MN-rgp120 V2 Domain
EISSN 1932-6203
Editor Nixon, Douglas F.
Editor_xml – sequence: 1
  givenname: Douglas F.
  surname: Nixon
  fullname: Nixon, Douglas F.
ExternalDocumentID 1325027770
oai_doaj_org_article_6c46fd26f6ae4b9d824b1a0d4b649222
2940467831
10_1371_journal_pone_0039045
22720026
Genre Journal Article
GeographicLocations United States--US
North America
California
GeographicLocations_xml – name: North America
– name: United States--US
– name: California
GroupedDBID ---
123
29O
2WC
3V.
53G
5VS
7RV
7X2
7X7
7XC
88E
8AO
8C1
8CJ
8FE
8FG
8FH
8FI
8FJ
A8Z
AAFWJ
ABDBF
ABIVO
ABJCF
ABUWG
ACGFO
ACIHN
ACIWK
ACPRK
ADBBV
ADRAZ
AEAQA
AENEX
AFKRA
AFRAH
AHMBA
ALIPV
ALMA_UNASSIGNED_HOLDINGS
AOIJS
APEBS
ARAPS
ATCPS
BAWUL
BBNVY
BBORY
BCNDV
BENPR
BGLVJ
BHPHI
BKEYQ
BPHCQ
BVXVI
BWKFM
CCPQU
CGR
CS3
CUY
CVF
D1I
D1J
D1K
DIK
DU5
E3Z
EAP
EAS
EBD
ECM
EIF
EMOBN
ESTFP
ESX
EX3
F5P
FPL
FYUFA
GROUPED_DOAJ
GX1
HCIFZ
HH5
HMCUK
HYE
IAO
IEA
IHR
IHW
INH
INR
IOV
IPNFZ
IPY
ISE
ISR
ITC
K6-
KB.
KQ8
L6V
LK5
LK8
M0K
M1P
M48
M7P
M7R
M7S
M~E
NAPCQ
NPM
O5R
O5S
OK1
P2P
P62
PATMY
PDBOC
PIMPY
PQQKQ
PROAC
PSQYO
PTHSS
PV9
PYCSY
RIG
RNS
RPM
RZL
SV3
TR2
UKHRP
WOQ
WOW
~02
~KM
AAYXX
CITATION
7QG
7QL
7QO
7SN
7SS
7T5
7TG
7TM
7U9
7XB
8FD
8FK
AZQEC
C1K
DWQXO
FR3
GNUQQ
H94
K9.
KL.
M7N
P64
PQEST
PQUKI
PRINS
RC3
5PM
AFPKN
ACUHS
-
02
AAPBV
ABPTK
ADACO
BBAFP
KM
ID FETCH-LOGICAL-c4415-72fe977ab81e6be6adc5b3fd8befffe036cc3bf1e937211d0d21bd1754f580df3
IEDL.DBID RPM
ISSN 1932-6203
IngestDate Fri Nov 26 17:12:28 EST 2021
Tue Dec 17 15:18:45 EST 2024
Tue Sep 17 21:25:41 EDT 2024
Thu Oct 10 16:44:18 EDT 2024
Fri Nov 22 00:08:57 EST 2024
Sat Nov 02 12:22:18 EDT 2024
IsDoiOpenAccess true
IsOpenAccess true
IsPeerReviewed true
IsScholarly true
Issue 6
Language English
License This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
Creative Commons Attribution License
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c4415-72fe977ab81e6be6adc5b3fd8befffe036cc3bf1e937211d0d21bd1754f580df3
Notes Conceived and designed the experiments: GRN DF SMO PWB. Performed the experiments: GRN DF SMO ALV. Analyzed the data: GRN DF ALV SMO PWB. Wrote the paper: GRN PWB.
OpenAccessLink https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3374778/
PMID 22720026
PQID 1325027770
PQPubID 1436336
ParticipantIDs plos_journals_1325027770
doaj_primary_oai_doaj_org_article_6c46fd26f6ae4b9d824b1a0d4b649222
pubmedcentral_primary_oai_pubmedcentral_nih_gov_3374778
proquest_journals_1325027770
crossref_primary_10_1371_journal_pone_0039045
pubmed_primary_22720026
PublicationCentury 2000
PublicationDate 2012-06-13
PublicationDateYYYYMMDD 2012-06-13
PublicationDate_xml – month: 06
  year: 2012
  text: 2012-06-13
  day: 13
PublicationDecade 2010
PublicationPlace United States
PublicationPlace_xml – name: United States
– name: San Francisco
– name: San Francisco, USA
PublicationTitle PloS one
PublicationTitleAlternate PLoS One
PublicationYear 2012
Publisher Public Library of Science
Public Library of Science (PLoS)
Publisher_xml – sequence: 0
  name: Public Library of Science (PLoS)
– name: Public Library of Science
References WJ Honnen (ref47) 2007; 81
BF Haynes (ref11) 2012; 366
M Tidswell (ref56) 1997; 159
Z Wu (ref45) 1995; 69
SM O'Rourke (ref37) 2010; 84
LM Walker (ref49) 2011
A Pinter (ref51) 2005; 79
S Rerks-Ngarm (ref7) 2009; 361
NM Flynn (ref8) 2005; 191
DN Forthal (ref13) 2007; 178
PW Berman (ref5) 1998; 14
SD Gowda (ref24) 1989; 142
LM Walker (ref20) 2010; 6
A Pinter (ref18) 2004; 78
D Montefiori (ref10) 2004
L Stamatatos (ref17) 1998; 72
S Vijh-Warrier (ref46) 1996; 70
PW Berman (ref59) 1997; 176
MA Muesing (ref53) 1985; 313
MK Gorny (ref32) 2005; 79
M Stevenson (ref25) 1990; 9
FL Graham (ref58) 1973; 52
C Shotton (ref44) 1995; 69
C Gurgo (ref52) 1988; 164
LM Walker (ref22) 2009; 326
PW Berman (ref3) 1996; 173
P Pitisuttithum (ref9) 2006; 194
C Cicala (ref15) 2009; 106
GR Nakamura (ref28) 1993; 67
JS McLellan (ref34) 2011; 480
PK Nakane (ref55) 1975; 254
CC Huang (ref39) 2005; 310
GR Nakamura (ref27) 1992; 8
JP Moore (ref42) 1993; 67
M Perez-Losada (ref60) 2010; 27
PW Berman (ref1) 1992; 66
RB Belshe (ref2) 1994; 272
BF Keele (ref29) 2008; 105
R Pantophlet (ref48) 2006; 24
M Bonsignori (ref35) 2011; 85
MK Gorny (ref43) 1994; 68
S Zolla-Pazner (ref36) 2012
DP Francis (ref4) 1998; 14
PD Kwong (ref38) 1998; 393
J Arthos (ref23) 2008; 9
DG Stupack (ref30) 1991; 34
S Zolla-Pazner (ref33) 2010; 10
CJ Saunders (ref19) 2005; 79
DJ Erle (ref31) 1994; 153
JA Zack (ref26) 1990; 61
MS Fung (ref40) 1992; 66
CK Leonard (ref54) 1990; 265
DC Montefiori (ref12) 2012
E Callaway (ref16) 2011
TA Kunkel (ref57) 1985; 82
SK Lai (ref14) 2009; 83
PL Moore (ref21) 2011; 85
PB Gilbert (ref50) 2005; 191
JA McKeating (ref41) 1993; 67
PW Berman (ref6) 1999; 265
References_xml – volume: 83
  start-page: 11196
  year: 2009
  ident: ref14
  article-title: Human immunodeficiency virus type 1 is trapped by acidic but not by neutralized human cervicovaginal mucus.
  publication-title: J Virol
  doi: 10.1128/JVI.01899-08
  contributor:
    fullname: SK Lai
– volume: 265
  start-page: 1
  year: 1999
  ident: ref6
  article-title: Development of bivalent (B/E) vaccines able to neutralize CCR5-dependent viruses from the United States and Thailand.
  publication-title: Virology
  doi: 10.1006/viro.1999.0031
  contributor:
    fullname: PW Berman
– volume: 272
  start-page: 475
  year: 1994
  ident: ref2
  article-title: Neutralizing antibodies to HIV-1 in seronegative volunteers immunized with recombinant gp120 from the MN strain of HIV-1. NIAID AIDS Vaccine Clinical Trials Network.
  publication-title: Jama
  doi: 10.1001/jama.1994.03520060075035
  contributor:
    fullname: RB Belshe
– volume: 9
  start-page: 1551
  year: 1990
  ident: ref25
  article-title: HIV-1 replication is controlled at the level of T cell activation and proviral integration.
  publication-title: Embo J
  doi: 10.1002/j.1460-2075.1990.tb08274.x
  contributor:
    fullname: M Stevenson
– volume: 191
  start-page: 666
  year: 2005
  ident: ref50
  article-title: Correlation between immunologic responses to a recombinant glycoprotein 120 vaccine and incidence of HIV-1 infection in a phase 3 HIV-1 preventive vaccine trial.
  publication-title: J Infect Dis
  doi: 10.1086/428405
  contributor:
    fullname: PB Gilbert
– volume: 66
  start-page: 848
  year: 1992
  ident: ref40
  article-title: Identification and characterization of a neutralization site within the second variable region of human immunodeficiency virus type 1 gp120.
  publication-title: J Virol
  doi: 10.1128/JVI.66.2.848-856.1992
  contributor:
    fullname: MS Fung
– volume: 67
  start-page: 4932
  year: 1993
  ident: ref41
  article-title: Characterization of neutralizing monoclonal antibodies to linear and conformation-dependent epitopes within the first and second variable domains of human immunodeficiency virus type 1 gp120.
  publication-title: J Virol
  doi: 10.1128/JVI.67.8.4932-4944.1993
  contributor:
    fullname: JA McKeating
– volume: 326
  start-page: 285
  year: 2009
  ident: ref22
  article-title: Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target.
  publication-title: Science
  doi: 10.1126/science.1178746
  contributor:
    fullname: LM Walker
– volume: 72
  start-page: 7840
  year: 1998
  ident: ref17
  article-title: An envelope modification that renders a primary, neutralization-resistant clade B human immunodeficiency virus type 1 isolate highly susceptible to neutralization by sera from other clades.
  publication-title: J Virol
  doi: 10.1128/JVI.72.10.7840-7845.1998
  contributor:
    fullname: L Stamatatos
– volume: 78
  start-page: 5205
  year: 2004
  ident: ref18
  article-title: The V1/V2 domain of gp120 is a global regulator of the sensitivity of primary human immunodeficiency virus type 1 isolates to neutralization by antibodies commonly induced upon infection.
  publication-title: J Virol
  doi: 10.1128/JVI.78.10.5205-5215.2004
  contributor:
    fullname: A Pinter
– volume: 52
  start-page: 456
  year: 1973
  ident: ref58
  article-title: A new technique for the assay of infectivity of human adenovirus 5 DNA.
  publication-title: Virology
  doi: 10.1016/0042-6822(73)90341-3
  contributor:
    fullname: FL Graham
– volume: 61
  start-page: 213
  year: 1990
  ident: ref26
  article-title: HIV-1 entry into quiescent primary lymphocytes: molecular analysis reveals a labile, latent viral structure.
  publication-title: Cell
  doi: 10.1016/0092-8674(90)90802-L
  contributor:
    fullname: JA Zack
– volume: 164
  start-page: 531
  year: 1988
  ident: ref52
  article-title: Envelope sequences of two new United States HIV-1 isolates.
  publication-title: Virology
  doi: 10.1016/0042-6822(88)90568-5
  contributor:
    fullname: C Gurgo
– volume: 14
  start-page: S325
  year: 1998
  ident: ref4
  article-title: Advancing AIDSVAX to phase 3. Safety, immunogenicity, and plans for phase 3.
  publication-title: AIDS Res Hum Retroviruses
  contributor:
    fullname: DP Francis
– volume: 85
  start-page: 3128
  year: 2011
  ident: ref21
  article-title: Potent and Broad Neutralization of HIV-1 Subtype C by Plasma Antibodies Targeting a Quaternary Epitope Including Residues in the V2 Loop.
  publication-title: J Virol
  doi: 10.1128/JVI.02658-10
  contributor:
    fullname: PL Moore
– volume: 8
  start-page: 1875
  year: 1992
  ident: ref27
  article-title: Monoclonal antibodies to the extracellular domain of HIV-1IIIB gp160 that neutralize infectivity, block binding to CD4, and react with diverse isolates.
  publication-title: AIDS Res Hum Retroviruses
  doi: 10.1089/aid.1992.8.1875
  contributor:
    fullname: GR Nakamura
– volume: 6
  start-page: e1001028
  year: 2010
  ident: ref20
  article-title: A limited number of antibody specificities mediate broad and potent serum neutralization in selected HIV-1 infected individuals.
  publication-title: PLoS Pathog
  doi: 10.1371/journal.ppat.1001028
  contributor:
    fullname: LM Walker
– volume: 153
  start-page: 517
  year: 1994
  ident: ref31
  article-title: Expression and function of the MAdCAM-1 receptor, integrin alpha 4 beta 7, on human leukocytes.
  publication-title: J Immunol
  doi: 10.4049/jimmunol.153.2.517
  contributor:
    fullname: DJ Erle
– volume: 82
  start-page: 488
  year: 1985
  ident: ref57
  article-title: Rapid and efficient site-specific mutagenesis without phenotypic selection.
  publication-title: Proc Natl Acad Sci U S A
  doi: 10.1073/pnas.82.2.488
  contributor:
    fullname: TA Kunkel
– year: 2011
  ident: ref16
  article-title: Clues emerge to explain first successful HIV vaccine trial.
  doi: 10.1038/news.2011.541
  contributor:
    fullname: E Callaway
– volume: 66
  start-page: 4464
  year: 1992
  ident: ref1
  article-title: Neutralization of multiple laboratory and clinical isolates of human immunodeficiency virus type 1 (HIV-1) by antisera raised against gp120 from the MN isolate of HIV-1.
  publication-title: J Virol
  doi: 10.1128/JVI.66.7.4464-4469.1992
  contributor:
    fullname: PW Berman
– volume: 85
  start-page: 9998
  year: 2011
  ident: ref35
  article-title: Analysis of a Clonal Lineage of HIV-1 Envelope V2/V3 Conformational Epitope-Specific Broadly Neutralizing Antibodies and Their Inferred Unmutated Common Ancestors.
  publication-title: J Virol
  doi: 10.1128/JVI.05045-11
  contributor:
    fullname: M Bonsignori
– volume: 10
  start-page: 527
  year: 2010
  ident: ref33
  article-title: Structure-function relationships of HIV-1 envelope sequence-variable regions refocus vaccine design.
  publication-title: Nat Rev Immunol
  doi: 10.1038/nri2801
  contributor:
    fullname: S Zolla-Pazner
– volume: 159
  start-page: 1497
  year: 1997
  ident: ref56
  article-title: Structure-function analysis of the integrin beta 7 subunit: identification of domains involved in adhesion to MAdCAM-1.
  publication-title: J Immunol
  doi: 10.4049/jimmunol.159.3.1497
  contributor:
    fullname: M Tidswell
– volume: 142
  start-page: 773
  year: 1989
  ident: ref24
  article-title: Evidence that T cell activation is required for HIV-1 entry in CD4+ lymphocytes.
  publication-title: J Immunol
  doi: 10.4049/jimmunol.142.3.773
  contributor:
    fullname: SD Gowda
– volume: 84
  start-page: 11200
  year: 2010
  ident: ref37
  article-title: Mutation at a single position in the V2 domain of the HIV-1 envelope protein confers neutralization sensitivity to a highly neutralization-resistant virus.
  publication-title: J Virol
  doi: 10.1128/JVI.00790-10
  contributor:
    fullname: SM O'Rourke
– volume: 68
  start-page: 8312
  year: 1994
  ident: ref43
  article-title: Human anti-V2 monoclonal antibody that neutralizes primary but not laboratory isolates of human immunodeficiency virus type 1.
  publication-title: J Virol
  doi: 10.1128/JVI.68.12.8312-8320.1994
  contributor:
    fullname: MK Gorny
– year: 2012
  ident: ref12
  article-title: Magnitude and Breadth of the Neutralizing Antibody Response in the RV144 and VAX003 HIV-1 Vaccine Efficacy Trials.
  doi: 10.1093/infdis/jis367
  contributor:
    fullname: DC Montefiori
– volume: 79
  start-page: 9069
  year: 2005
  ident: ref19
  article-title: The V1, V2, and V3 regions of the human immunodeficiency virus type 1 envelope differentially affect the viral phenotype in an isolate-dependent manner.
  publication-title: J Virol
  doi: 10.1128/JVI.79.14.9069-9080.2005
  contributor:
    fullname: CJ Saunders
– volume: 173
  start-page: 52
  year: 1996
  ident: ref3
  article-title: Protection of MN-rgp120-immunized chimpanzees from heterologous infection with a primary isolate of human immunodeficiency virus type 1.
  publication-title: J Infect Dis
  doi: 10.1093/infdis/173.1.52
  contributor:
    fullname: PW Berman
– volume: 69
  start-page: 2271
  year: 1995
  ident: ref45
  article-title: Characterization of neutralization epitopes in the V2 region of human immunodeficiency virus type 1 gp120: role of glycosylation in the correct folding of the V1/V2 domain.
  publication-title: J Virol
  doi: 10.1128/JVI.69.4.2271-2278.1995
  contributor:
    fullname: Z Wu
– volume: 79
  start-page: 5232
  year: 2005
  ident: ref32
  article-title: Identification of a new quaternary neutralizing epitope on human immunodeficiency virus type 1 virus particles.
  publication-title: J Virol
  doi: 10.1128/JVI.79.8.5232-5237.2005
  contributor:
    fullname: MK Gorny
– volume: 27
  start-page: 417
  year: 2010
  ident: ref60
  article-title: Phylodynamics of HIV-1 from a phase-III AIDS vaccine trial in North America.
  publication-title: Mol Biol Evol
  doi: 10.1093/molbev/msp254
  contributor:
    fullname: M Perez-Losada
– volume: 178
  start-page: 6596
  year: 2007
  ident: ref13
  article-title: Recombinant gp120 vaccine-induced antibodies inhibit clinical strains of HIV-1 in the presence of Fc receptor-bearing effector cells and correlate inversely with HIV infection rate.
  publication-title: J Immunol
  doi: 10.4049/jimmunol.178.10.6596
  contributor:
    fullname: DN Forthal
– volume: 194
  start-page: 1661
  year: 2006
  ident: ref9
  article-title: Randomized, double-blind, placebo-controlled efficacy trial of a bivalent recombinant glycoprotein 120 HIV-1 vaccine among injection drug users in Bangkok, Thailand.
  publication-title: J Infect Dis
  doi: 10.1086/508748
  contributor:
    fullname: P Pitisuttithum
– volume: 313
  start-page: 450
  year: 1985
  ident: ref53
  article-title: Nucleic acid structure and expression of the human AIDS/lymphadenopathy retrovirus.
  publication-title: Nature
  doi: 10.1038/313450a0
  contributor:
    fullname: MA Muesing
– volume: 310
  start-page: 1025
  year: 2005
  ident: ref39
  article-title: Structure of a V3-containing HIV-1 gp120 core.
  publication-title: Science
  doi: 10.1126/science.1118398
  contributor:
    fullname: CC Huang
– volume: 366
  start-page: 1275
  year: 2012
  ident: ref11
  article-title: Immune-correlates analysis of an HIV-1 vaccine efficacy trial.
  publication-title: N Engl J Med
  doi: 10.1056/NEJMoa1113425
  contributor:
    fullname: BF Haynes
– volume: 67
  start-page: 3656
  year: 1993
  ident: ref42
  article-title: A monoclonal antibody to the CDR-3 region of CD4 inhibits soluble CD4 binding to virions of human immunodeficiency virus type 1.
  publication-title: J Virol
  doi: 10.1128/JVI.67.6.3656-3659.1993
  contributor:
    fullname: JP Moore
– volume: 9
  start-page: 301
  year: 2008
  ident: ref23
  article-title: HIV-1 envelope protein binds to and signals through integrin alpha4beta7, the gut mucosal homing receptor for peripheral T cells.
  publication-title: Nat Immunol
  doi: 10.1038/ni1566
  contributor:
    fullname: J Arthos
– year: 2004
  ident: ref10
  article-title: Evaluating neutralizing antibodies against HIV, SIV and SHIV in luciferase reporter gene assays.
  doi: 10.1002/0471142735.im1211s64
  contributor:
    fullname: D Montefiori
– volume: 79
  start-page: 6909
  year: 2005
  ident: ref51
  article-title: The C108g epitope in the V2 domain of gp120 functions as a potent neutralization target when introduced into envelope proteins derived from human immunodeficiency virus type 1 primary isolates.
  publication-title: J Virol
  doi: 10.1128/JVI.79.11.6909-6917.2005
  contributor:
    fullname: A Pinter
– year: 2012
  ident: ref36
  article-title: Analysis of the V2 Antibody Response Induced in Vaccinees Participating in the ALVAC/AIDSVAX HIV-1 Clinical Vaccine Trial.
  contributor:
    fullname: S Zolla-Pazner
– volume: 254
  start-page: 203
  year: 1975
  ident: ref55
  article-title: Recent progress in the peroxidase-labeled antibody method.
  publication-title: Ann N Y Acad Sci
  doi: 10.1111/j.1749-6632.1975.tb29170.x
  contributor:
    fullname: PK Nakane
– volume: 480
  start-page: 336
  year: 2011
  ident: ref34
  article-title: Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9.
  publication-title: Nature
  doi: 10.1038/nature10696
  contributor:
    fullname: JS McLellan
– volume: 191
  start-page: 654
  year: 2005
  ident: ref8
  article-title: Placebo-controlled phase 3 trial of a recombinant glycoprotein 120 vaccine to prevent HIV-1 infection.
  publication-title: J Infect Dis
  doi: 10.1086/428404
  contributor:
    fullname: NM Flynn
– volume: 81
  start-page: 1424
  year: 2007
  ident: ref47
  article-title: Type-specific epitopes targeted by monoclonal antibodies with exceptionally potent neutralizing activities for selected strains of human immunodeficiency virus type 1 map to a common region of the V2 domain of gp120 and differ only at single positions from the clade B consensus sequence.
  publication-title: J Virol
  doi: 10.1128/JVI.02054-06
  contributor:
    fullname: WJ Honnen
– volume: 106
  start-page: 20877
  year: 2009
  ident: ref15
  article-title: The integrin alpha4beta7 forms a complex with cell-surface CD4 and defines a T-cell subset that is highly susceptible to infection by HIV-1.
  publication-title: Proc Natl Acad Sci U S A
  doi: 10.1073/pnas.0911796106
  contributor:
    fullname: C Cicala
– volume: 265
  start-page: 10373
  year: 1990
  ident: ref54
  article-title: Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells.
  publication-title: J Biol Chem
  doi: 10.1016/S0021-9258(18)86956-3
  contributor:
    fullname: CK Leonard
– volume: 105
  start-page: 7552
  year: 2008
  ident: ref29
  article-title: Identification and characterization of transmitted and early founder virus envelopes in primary HIV-1 infection.
  publication-title: Proc Natl Acad Sci U S A
  doi: 10.1073/pnas.0802203105
  contributor:
    fullname: BF Keele
– volume: 14
  start-page: S277
  year: 1998
  ident: ref5
  article-title: Development of bivalent rgp120 vaccines to prevent HIV type 1 infection.
  publication-title: AIDS Res Hum Retroviruses
  contributor:
    fullname: PW Berman
– year: 2011
  ident: ref49
  article-title: Broad neutralization coverage of HIV by multiple highly potent antibodies.
  doi: 10.1038/nature10373
  contributor:
    fullname: LM Walker
– volume: 176
  start-page: 384
  year: 1997
  ident: ref59
  article-title: Genetic and immunologic characterization of viruses infecting MN-rgp120-vaccinated volunteers.
  publication-title: J Infect Dis
  doi: 10.1086/514055
  contributor:
    fullname: PW Berman
– volume: 67
  start-page: 6179
  year: 1993
  ident: ref28
  article-title: Strain specificity and binding affinity requirements of neutralizing monoclonal antibodies to the C4 domain of gp120 from human immunodeficiency virus type 1.
  publication-title: J Virol
  doi: 10.1128/JVI.67.10.6179-6191.1993
  contributor:
    fullname: GR Nakamura
– volume: 393
  start-page: 648
  year: 1998
  ident: ref38
  article-title: Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody.
  publication-title: Nature
  doi: 10.1038/31405
  contributor:
    fullname: PD Kwong
– volume: 361
  start-page: 2209
  year: 2009
  ident: ref7
  article-title: Vaccination with ALVAC and AIDSVAX to prevent HIV-1 infection in Thailand.
  publication-title: N Engl J Med
  doi: 10.1056/NEJMoa0908492
  contributor:
    fullname: S Rerks-Ngarm
– volume: 34
  start-page: 761
  year: 1991
  ident: ref30
  article-title: B lymphocyte fibronectin receptors: expression and utilization.
  publication-title: Scand J Immunol
  doi: 10.1111/j.1365-3083.1991.tb01601.x
  contributor:
    fullname: DG Stupack
– volume: 24
  start-page: 739
  year: 2006
  ident: ref48
  article-title: GP120: target for neutralizing HIV-1 antibodies.
  publication-title: Annu Rev Immunol
  doi: 10.1146/annurev.immunol.24.021605.090557
  contributor:
    fullname: R Pantophlet
– volume: 69
  start-page: 222
  year: 1995
  ident: ref44
  article-title: Identification and characterization of monoclonal antibodies specific for polymorphic antigenic determinants within the V2 region of the human immunodeficiency virus type 1 envelope glycoprotein.
  publication-title: J Virol
  doi: 10.1128/JVI.69.1.222-230.1995
  contributor:
    fullname: C Shotton
– volume: 70
  start-page: 4466
  year: 1996
  ident: ref46
  article-title: Synergistic neutralization of human immunodeficiency virus type 1 by a chimpanzee monoclonal antibody against the V2 domain of gp120 in combination with monoclonal antibodies against the V3 loop and the CD4-binding site.
  publication-title: J Virol
  doi: 10.1128/JVI.70.7.4466-4473.1996
  contributor:
    fullname: S Vijh-Warrier
SSID ssj0053866
Score 2.294844
Snippet Recombinant gp120 (MN-rgp120) was a major component of the AIDSVAX B/E vaccine used in the RV144 trial. This was the first clinical trial to show that...
Background Recombinant gp120 (MN-rgp120) was a major component of the AIDSVAX B/E vaccine used in the RV144 trial. This was the first clinical trial to show...
BackgroundRecombinant gp120 (MN-rgp120) was a major component of the AIDSVAX B/E vaccine used in the RV144 trial. This was the first clinical trial to show...
Background Recombinant gp120 (MN-rgp120) was a major component of the AIDSVAX B/E vaccine used in the RV144 trial. This was the first clinical trial to show...
SourceID plos
doaj
pubmedcentral
proquest
crossref
pubmed
SourceType Open Website
Open Access Repository
Aggregation Database
Index Database
StartPage e39045
SubjectTerms Acquired immune deficiency syndrome
AIDS
Amino acids
Antibodies, Monoclonal - immunology
Antibody Specificity
Antigens
Binding sites
Biology
Blocking
CD4 antigen
Correlation analysis
Epitope Mapping
Glycoprotein gp120
HIV
HIV Envelope Protein gp120 - chemistry
HIV Envelope Protein gp120 - immunology
Human immunodeficiency virus
Humans
Immunization
Infections
Integrins - immunology
Integrins - metabolism
Lymphocytes T
Medicine
Mice
Monoclonal antibodies
Mutagenesis, Site-Directed
Neutralization Tests
Protein Binding
Proteins
Vaccination
Vaccines
Virions
SummonAdditionalLinks – databaseName: Directory of Open Access Journals
  dbid: DOA
  link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV3NTtwwELYqTr1Uhf6QllY-9NAeDLbj2E5vUIFQpXIqFbfIztgQCZKI3T5Y-yA8E2Mni3YRUi-9ZhLZmRl7vpFnPhPyCWqLMFg4ZnRVMQwBlrnWAKshSO60ss7naoszfXquvl9UF2tXfaWasIkeeFLcgW6VjiB11C4oX4OVygvHQXmtagxuefflcpVMTXswrmKt50a50oiD2S7749CH_dSOylP70logynz9id_0elg8hTUfl0yuxaCTl-TFDB7p4TTpbfIs9Dtke16eC_p55pD-8or0uFaH9jrBbIq66_yQqgXpcqAI-OgvSWG4cV1Ph0h_nLHby1FI_pVGhJz0xiXKhsskCiOu9xG_cz3Qrr_qfC7wSqK7P-rur6G-y10xr8n5yfHPb6dsvlqBtSmBYkbGgMjPeSuC9kE7aCtfRrA-xBgDhrW2LX0UAdELpojAQQoPCDVUrCyHWL4hWz0qc5dQi4BAA2o0YKQTtfdGCAMt95UDxEp1QdhKz804MWg0-RjNYOYx6a1JdmlmuxTkKBnj4d3Ef50foFc0s1c0__KKguwmU64GWOBwiPWkMYYXZG9l3qfFbydLP0xApqNqTFULYjZ8YGOGm5K-u8pM3WWJ2Zqx7_7HL70nzxGsyVSmJso9srW8_R0-ICBa-o_Z9-8BjwwLLQ
  priority: 102
  providerName: Directory of Open Access Journals
– databaseName: ProQuest Technology Collection
  dbid: 8FG
  link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfV3NbtQwELagXLggyl8DBfnAAQ5uYyexEy6IQpeC1J4o6i2yY3sbqY3D7vJg8CB9Jma8TumiimvGka0Zj-cbz48JeW2bGmAw10zJqmJgAmqmO2VZY53ItSxrbWK2xYk8Oi2_nlVn6cJtmdIqpzMxHtQ2dHhHvg9eU4XxRpW_H38wfDUKo6vpCY275B4XMBtWis8-Tycx6LKUqVyuUHw_SWdvDIPbw6LUHIuYbpij2LUfu5xehOVtiPPfxMkblmj2kDxIEJJ-WMt8m9xxwyOynZR0Sd-kTtJvH5MBNDZ0FyEOH1a9CZgzSFeBAuyj3wX9FC51P9Dg6fEJW8xHLvJ3dAbAkx5rbNwwR9LhCFo_wn96sPTLcN6bmOaFpKtf5dVvRQ_6WBvzhJzODr99PGLpgQXWoRvFlPAO8J82NXfSOKltV5nC29o4770D49Z1hfHcAYYBR9HmVnBjAXCUvqpz64unZGsAZu4QWgMskBY46sDe8cYYxbmyXW4qbQExNRlhE5_bcd1Ho43BNAX-x5pvLcqlTXLJyAEK43osdsGOH8Ji3ialamVXSm-F9FK70jS2FqXhOrelkWUDwCcjOyjKaYJl-3cTZWR3Eu_t5GdrSV8vQGDAGhzWjKiNPbCxwk3K0J_Hft1FAT6bqp__f8oX5D6AMYFpaLzYJVurxU_3EgDPyryKu_oPKAMBsA
  priority: 102
  providerName: ProQuest
– databaseName: Scholars Portal Journals: Open Access
  dbid: M48
  link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwlZ3NbtQwEICtUi5cEOWvgYJ84AAHr2LHsROkClHoqiBtTyzqLbJjextpG4fdRYLHah-kz9SxN1mxaDlwje04mvFkvpHHY4TemLIADKaKSJHnBFxAQVQtDSmNZakSvFA6Zluci7Mp_3qRX-yh4c7WXoDLnaFduE9qupiPfv34_QEM_jje2iDpMGjU-daOwmFTwJR76D4D3xiSvCZ8s68A1h13LwO1EMHSrD9M96-3bDmrWNM_1ECd--UuHv07rfIPPzV-hB72gIk_rlfEAdqz7WN00JvwEr_t60y_e4JasGdfz33s3q4a7UNGIV55DFCIvzP82V-ppsXe4ck5Wcw6ytL3eAxYiicqlHWYhabTDv4JHYxTrcFf2stGxySw0HR7zW9vJD5p4smZp2g6Pv326Yz01y-QOgRZRDJngQ6VLqgV2gpl6lxnzhTaOucsuL66zrSjFggHwkiTGka1ARzhLi9S47JnaL8FYR4iXAA0CAMSteANaam1pFSaOtW5MsBTZYLIIOeqW1fZqOJWm4ToZC23Kuil6vWSoJOgjE3fUCM7PvCLWdWbXCVqLpxhwglluS5NwbimKjVcC14CFiXoMKhymGAJ0wEPMillmqCjQb27m5-vNb35ABa2syGcTZDcWgNbX7jd0jaXsZp3lkFEJ4sX_ymCl-gBsBsLWWs0O0L7q8VP-wr4aKVfxyV_B6g1D6Y
  priority: 102
  providerName: Scholars Portal
Title Monoclonal antibodies to the V2 domain of MN-rgp120: fine mapping of epitopes and inhibition of α4β7 binding
URI https://www.ncbi.nlm.nih.gov/pubmed/22720026
https://www.proquest.com/docview/1325027770
https://pubmed.ncbi.nlm.nih.gov/PMC3374778
https://doaj.org/article/6c46fd26f6ae4b9d824b1a0d4b649222
http://dx.doi.org/10.1371/journal.pone.0039045
Volume 7
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3NjtMwELZ2F4G4ILb8bGCpfOAAh7RxfmyHGy0tC1KqFWJRb5Ed291IbRK15cBjwYPsMzF2ktUW7YmLD3HsWJ4Zzzfx-DNCb1XKAQYT4TOaJD64AO6Lgik_VToMBI25kC7bYkEvruKvy2R5hJL-LIxL2i9kOarWm1FVXrvcymZTjPs8sfFlNo0iAMGMj4_RMbjfPkRvl18wYEq7M3IRI-NOJKOmrvTInkQFDGMZgO3-o6NUuOOOHGu_ZTld17v7EOe_iZN3PNH8KXrSQUj8sR3qKTrS1QA9bC-V_DVAj7Juu3yATjvL3eF3Hb30-2eoAjOui3Xt-qj2paxtIiHe1xiwIP4R4k_1RpQVrg3OFv521ZAw-IDn0CHOhGVzWNmqWQNLQQPtRKXwl-q6lC73y1bd_I5v_jA8Kd2Bmefoaj77Pr3wu1sX_MLGVj4LjQZQKCQnmkpNhSoSGRnFpTbGaPB4RRFJQzQAG4geVaBCIhWgkNgkPFAmeoFOKpjsM4Q5YAWqYMY1OEGSSskIYaoIZCIUwKjUQ34_-XnTkmvkboeNQVDSTmZu5ZZ3cvPQxEro9l1Lje0e1NtV3ilITouYGhVSQ4WOZap4GEsiAhVLGqeAhjx0ZuXbf2AHnwMYGDLGAg-d9zK_v_plK_7bAfRa5CF2oBgHIzysAZ12JN6dDr_675av0WMAb6FNWyPROTrZb3_qNwCQ9nIIZrFkUPIpseX88xA9mMwWl9-G7pcDlFnMh85s_gJeyxbn
link.rule.ids 230,314,727,780,784,864,885,2102,2221,12056,12223,12765,21388,24318,27924,27925,31719,33266,33373,33744,43310,43579,43600,43805,53791,53793,73745,74014,74035,74302
linkProvider National Library of Medicine
linkToHtml http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfV1LbxMxELagHOCCKK9uH-ADBzi4Xe_D9nJBbWmUQpNTi3pb2Ws7Xamst0n6w-CH9DcxdpzQoIrrjle2PDOebzwPI_RBVwJgMJWEs7IkYAIEkQ3XpNImSyUrhFQh22LMhhfFt8vyMl64zWJa5fJMDAe1do2_Iz8Ar6n08UaefulviH81ykdX4xMaj9ETMPvcS7U4XqV4gC4zFsvlck4PInf2e9eZfV-UmvoipnvmKHTt911Or93sIcT5b-LkPUs0eIGeRwiJDxc830SPTPcSbUYlneGPsZP0p1eoA411zbULw7t5q5zPGcRzhwH24R8Z_up-yrbDzuLRmEwnPc3Sz3gAwBOPpG_cMPGkkx60vof_ZKfxaXfVqpDm5Ul3v4q73xwftaE25jW6GJycHw9JfGCBNN6NIjyzBvCfVIIapgyTuilVbrVQxlprwLg1Ta4sNYBhwFHUqc6o0gA4CluKVNv8DdroYDO3EBYAC5iGHTVg72ilFKeU6yZVpdSAmKoEkeU-1_2ij0Ydgmkc_I_FvtWeL3XkS4KOPDNWY30X7PDBTSd1VKqaNQWzOmOWSVOoSousUFSmulCsqAD4JGjLs3I5waz-K0QJ2l2y92Hy2wWnVwvIfMAaHNYE8TUZWFvhOqVrr0K_7jwHn42L7f9P-R49HZ6Pzuqz0_H3HfQMgFnmU9Jovos25tNbswfgZ67eBQn_AypWBG8
linkToPdf http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfV1Lb9QwELagSIgLorwaKOADBzikG-dhO1wQfaxaoCsOFPUW2bG9jVTisLv8MPgh_U3MeL1LF1VcM4lszXg838TfjAl5bWoJMJipVPCqSiEEyFS1wqS1sXmmeCmVDmyLCT8-Kz-eV-eR_zSPtMrVnhg2auNb_Ec-gqypwvNGkY1cpEV8ORy_H36keIMUnrTG6zRukzt4yxz20ZcHa7oH-DXnsXSuEGwULbU3-N7uYYFqhgVN10JT6OCPHU8v_fwm9PkvifJaVBo_IPcjnKQflvbfJrds_5BsR4ed0zexq_TbR6QH7_XtpQ-v94tOe-QP0oWnAAHpt5we-u-q66l39HSSzqYDy7N3dAwglJ4qbOIwRdHRADvAAN-p3tCT_qLTgfKFoqtf5dVvQfe7UCfzmJyNj74eHKfxsoW0xZQqFbmzgAWVlsxybbkybaULZ6S2zjkLga5tC-2YBTwDSaPJTM60AfBRukpmxhVPyFYPytwhVAJE4AY0aiH2sVprwZgwbaYrZQA91QlJV3puhmVPjSYcrAnIRZZ6a9AuTbRLQvbRGOt3sSN2eOBn0yY6WMPbkjuTc8eVLXVtZF5qpjJTal7WAIISsoOmXA0wb_4uqITsrsx7s_jp0tLrCeR4eA3Ja0LExhrYmOGmpO8uQu_uooD8Tchn_x_yFbkLi7v5fDL59JzcA4yWIzuNFbtkazH7aV8ADlrol2GB_wES0QiU
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=Monoclonal+Antibodies+to+the+V2+Domain+of+MN-rgp120%3A+Fine+Mapping+of+Epitopes+and+Inhibition+of+%CE%B14%CE%B27+Binding&rft.jtitle=PloS+one&rft.au=Nakamura%2C+Gerald+R.&rft.au=Fonseca%2C+Dora+P.+A.+J.&rft.au=O%27Rourke%2C+Sara+M.&rft.au=Vollrath%2C+Aaron+L.&rft.date=2012-06-13&rft.issn=1932-6203&rft.eissn=1932-6203&rft.volume=7&rft.issue=6&rft.spage=e39045&rft_id=info:doi/10.1371%2Fjournal.pone.0039045&rft.externalDBID=n%2Fa&rft.externalDocID=10_1371_journal_pone_0039045
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1932-6203&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1932-6203&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1932-6203&client=summon