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1. Full Text Viral Escape from HIV-1 Neutralizing Antibodies Drives Increased Plasma Neutralization Breadth through Sequential Recognition of Multiple Epitopes and Immunotypes
by Wibmer, Constantinos Kurt and Bhiman, Jinal N and Gray, Elin S and Tumba, Nancy and Abdool Karim, Salim S and Williamson, Carolyn and Morris, Lynn and Moore, Penny L
PLoS Pathogens, ISSN 1553-7366, 10/2013, Volume 9, Issue 10, pp. e1003738 - e1003738
Identifying the targets of broadly neutralizing antibodies to HIV-1 and understanding how these antibodies develop remain important goals in the quest to... 
B-CELL RESPONSES | BROAD NEUTRALIZATION | CD4 BINDING-SITE | GP120 ENVELOPE GLYCOPROTEIN | MICROBIOLOGY | SUBTYPE-C INFECTION | HUMAN-IMMUNODEFICIENCY-VIRUS | CONFORMATIONAL EPITOPE | VIROLOGY | CD4-BINDING SITE | HIV-1-INFECTED INDIVIDUALS | HUMAN MONOCLONAL-ANTIBODIES | PARASITOLOGY | HIV Antibodies - blood | HIV Infections - blood | Antibody Specificity | CD4 Antigens - immunology | HIV-1 - metabolism | CD4 Antigens - blood | Humans | Epitopes - blood | Epitopes - immunology | HIV Infections - immunology | Antibodies, Neutralizing - immunology | HIV-1 - immunology | Immune Evasion | HIV Antibodies - immunology | Female | Antibodies, Neutralizing - blood | Cohort Studies | Host-parasite relationships | Physiological aspects | Research | HIV antibodies | Health aspects | Blood plasma | Index Medicus | Plasma | AIDS | Immunology | Vaccines | Acquired immune deficiency syndrome
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2. Full Text The Neutralization Breadth of HIV-1 Develops Incrementally over Four Years and Is Associated with CD4+ T Cell Decline and High Viral Load during Acute Infection
by Elin S. Gray and Maphuti C. Madiga and Tandile Hermanus and Penny L. Moore and Constantinos Kurt Wibmer and Nancy L. Tumba and Lise Werner and Koleka Mlisana and Sengeziwe Sibeko and Carolyn Williamson and Salim S. Abdool Karim and Lynn Morris and and the CAPRISA002 Study Team and CAPRISA 002 Acute Infection Study Team and CAPRISA002 Study Team and and the CAPRISA002 Study Team
Journal of Virology, ISSN 0022-538X, 05/2011, Volume 85, Issue 10, pp. 4828 - 4840
Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley... 
TARGET | VIROLOGY | PROTECTION | VARIANTS | HUMORAL IMMUNITY | SUBTYPE-C INFECTION | MACAQUES | HUMAN-IMMUNODEFICIENCY-VIRUS | HUMAN MONOCLONAL-ANTIBODIES | TYPE-1 INFECTION | DISEASE PROGRESSION | HIV Antibodies - blood | Epitope Mapping | HIV Infections - virology | Humans | Viral Load | CD4-Positive T-Lymphocytes - immunology | Cross Reactions | Epitopes - immunology | HIV Infections - immunology | HIV-1 - immunology | Time Factors | Female | CD4-Positive T-Lymphocytes - virology | Antibodies, Neutralizing - blood | Index Medicus | Pathogenesis and Immunity
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3. Full Text Developmental pathway for potent V1V2-directed HIV-neutralizing antibodies
by Doria-Rose, Nicole A and Schramm, Chaim A and Gorman, Jason and Moore, Penny L and Bhiman, Jinal N and Dekosky, Brandon J and Ernandes, Michael J and Georgiev, Ivelin S and Kim, Helen J and Pancera, Marie and Staupe, Ryan P and Altae-Tran, Han R and Bailer, Robert T and Crooks, Ema T and Cupo, Albert and z, Aliaksan and Garrett, Nigel J and Hoi, Kam H and Kong, Rui and Louder, Mark K and Longo, Nancy S and McKee, Krisha and Nonyane, Molati and O'Dell, Sijy and Roark, Ryan S and Rudicell, Rebecca S and Schmidt, Stephen D and Sheward, Daniel J and Soto, Cinque and Wibmer, Constantinos Kurt and Yang, Yongping and Zhang, Zhenhai and Mullikin, James C and Binley, James M and Sanders, Rogier W and Wilson, Ian A and Moore, John P and Ward, Anew B and Georgiou, George and Williamson, Carolyn and Abdool Karim, Salim S and Morris, Lynn and Kwong, Peter D and Shapiro, Lawrence and Mascola, John R and Becker, Jesse and Benjamin, Betty and Blakesley, Robert and Bouffard, Gerry and Brooks, Shelise and Coleman, Holly and Dekhtyar, Mila and Gregory, Michael and Guan, Xiaobin and Gupta, Jyoti and Han, Joel and Hargrove, April and Ho, Shi-ling and Johnson, Taccara and Legaspi, Richelle and Lovett, Sean and Maduro, Quino and Masiello, Cathy and Maskeri, Baishali and McDowell, Jenny and Montemayor, Casana and Mullikin, James and Park, Morgan and Riebow, Nancy and Schandler, Karen and Schmidt, Brian and Sison, Christina and Stantripop, Mal and Thomas, James and Thomas, Pam and Vemulapalli, Meg and Young, Alice and NISC Comparative Sequencing and NISC Comparative Sequencing Program
Nature, ISSN 0028-0836, 2014, Volume 509, Issue 7498, pp. 55 - 62
Antibodies capable of neutralizing HIV-1 often target variable regions 1 and 2 (V1V2) of the HIV-1 envelope, but the mechanism of their elicitation has been... 
B-CELLS | MAXIMUM-LIKELIHOOD | STRUCTURAL BASIS | HIV-1-NEUTRALIZING ANTIBODIES | MULTIDISCIPLINARY SCIENCES | IMMUNODEFICIENCY-VIRUS TYPE-1 | VACCINE EFFICACY | INFECTION | BROAD | HUMAN MONOCLONAL-ANTIBODIES | ENVELOPE TRIMER | Complementarity Determining Regions - genetics | Epitope Mapping | Epitopes, B-Lymphocyte - chemistry | Humans | AIDS Vaccines - immunology | Molecular Sequence Data | Antibody Affinity - immunology | Neutralization Tests | Epitopes, B-Lymphocyte - immunology | HIV Antibodies - isolation & purification | HIV Infections - immunology | Antibodies, Neutralizing - immunology | HIV Antibodies - immunology | HIV Envelope Protein gp160 - chemistry | Complementarity Determining Regions - chemistry | HIV-1 - chemistry | Binding Sites - immunology | B-Lymphocytes - metabolism | Protein Structure, Tertiary | Amino Acid Sequence | CD4 Antigens - immunology | B-Lymphocytes - cytology | Models, Molecular | Antibody Affinity - genetics | Antibodies, Neutralizing - genetics | HIV Antibodies - chemistry | AIDS Vaccines - chemistry | Antibodies, Neutralizing - isolation & purification | Cell Lineage | HIV-1 - immunology | B-Lymphocytes - immunology | Antibodies, Neutralizing - chemistry | Complementarity Determining Regions - immunology | HIV Envelope Protein gp160 - immunology | HIV Antibodies - genetics | Somatic Hypermutation, Immunoglobulin - genetics | CD4 Antigens - metabolism | Evolution, Molecular | Viral antibodies | Antigen-antibody reactions | AIDS vaccines | AIDS (Disease) | Antibodies | Physiological aspects | Research | AIDS research | Cell culture | Genes | Human immunodeficiency virus--HIV | Phylogenetics | Amino acids | Infections | Genomes | Mutation | Index Medicus
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4. Full Text Common helical V1V2 conformations of HIV-1 Envelope expose the α4β7 binding site on intact virions
by Wibmer, Constantinos Kurt and Richardson, Simone I and Yolitz, Jason and Cicala, Claudia and Arthos, James and Moore, Penny L and Morris, Lynn and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Nature Communications, ISSN 2041-1723, 12/2018, Volume 9, Issue 1, pp. 4489 - 14
The α4β7 integrin is a non-essential HIV-1 adhesion receptor, bound by the gp120 V1V2 domain, facilitating rapid viral dissemination into gut-associated... 
HIV Antibodies - metabolism | HIV-1 - metabolism | Humans | Integrins - chemistry | Receptors, HIV - chemistry | Protein Binding - immunology | Virion - metabolism | HIV Envelope Protein gp120 - metabolism | Integrins - metabolism | HIV Envelope Protein gp120 - immunology | HIV Infections - immunology | HIV-1 - immunology | Receptors, HIV - antagonists & inhibitors | HIV Antibodies - immunology | Receptors, HIV - metabolism | Protein Conformation | Epitopes - chemistry | Antibodies, Monoclonal - metabolism | HIV Envelope Protein gp120 - chemistry | Binding Sites | Antibodies, Monoclonal - immunology | Integrins - antagonists & inhibitors | Immunoglobulins | Peptides | Pathogenesis | Blocking antibodies | Antibodies | Trimers | Vaccines | Lymphoid tissue | Gut-associated lymphoid tissues | Virions | Human immunodeficiency virus--HIV | Monoclonal antibodies | Binding sites | Glycoprotein gp120 | Conformation | Index Medicus
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5. Full Text Polyclonal B Cell Responses to Conserved Neutralization Epitopes in a Subset of HIV-1-Infected Individuals
by Georgia D. Tomaras and James M. Binley and Elin S. Gray and Emma T. Crooks and Keiko Osawa and Penny L. Moore and Nancy Tumba and Tommy Tong and Xiaoying Shen and Nicole L. Yates and Julie Decker and Constantinos Kurt Wibmer and Feng Gao and S. Munir Alam and Philippa Easterbrook and Salim Abdool Karim and Gift Kamanga and John A. Crump and Myron Cohen and George M. Shaw and John R. Mascola and Barton F. Haynes and David C. Montefiori and Lynn Morris
Journal of Virology, ISSN 0022-538X, 11/2011, Volume 85, Issue 21, pp. 11502 - 11519
Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley... 
PROXIMAL EXTERNAL REGION | ENV CLONES | VIROLOGY | VACCINE DESIGN | HIV-INFECTED INDIVIDUALS | CORECEPTOR BINDING-SITE | IMMUNODEFICIENCY-VIRUS TYPE-1 | ENVELOPE GLYCOPROTEIN | SUBTYPE-C INFECTION | HUMAN MONOCLONAL-ANTIBODIES | VIRAL ENVELOPE | HIV Antibodies - blood | HIV Envelope Protein gp120 - immunology | HIV Infections - immunology | HIV-1 - immunology | B-Lymphocytes - immunology | HIV Envelope Protein gp41 - immunology | Humans | Epitopes, B-Lymphocyte - immunology | Antibodies, Neutralizing - blood | Index Medicus | Pathogenesis and Immunity
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6. Full Text V2-Directed Vaccine-like Antibodies from HIV-1 Infection Identify an Additional K169-Binding Light Chain Motif with Broad ADCC Activity
by van Eeden, Charmaine and Wibmer, Constantinos Kurt and Scheepers, Cathrine and Richardson, Simone I and Nonyane, Molati and Lambson, Bronwen and Mkhize, Nonhlanhla N and Vijayakumar, Balakrishnan and Sheng, Zizhang and Stanfield-Oakley, Sherry and Bhiman, Jinal N and Bekker, Valerie and Hermanus, Tandile and Mabvakure, Batsirai and Ismail, Arshad and Moody, M. Anthony and Wiehe, Kevin and Garrett, Nigel and Karim, Salim Abdool and Dirr, Heini and Fernandes, Manuel A and Sayed, Yasien and Shapiro, Lawrence and Ferrari, Guido and Haynes, Barton F and Moore, Penny L and Morris, Lynn
Cell Reports, ISSN 2211-1247, 12/2018, Volume 25, Issue 11, pp. 3123 - 3135.e6
Antibodies that bind residue K169 in the V2 region of the HIV-1 envelope correlated with reduced risk of infection in the RV144 vaccine trial but were... 
antibody evolution | V2 antibodies | RV144 vaccine response | HIV | ED motif | CH58 | K169 | CAP228 | V2 structure | ADCC | NEUTRALIZING ANTIBODIES | EPITOPE | RECOGNITION | EFFICACY | IMMUNE PRESSURE | ALPHABETA | ENVELOPE V2 REGION | IMMUNODEFICIENCY-VIRUS TYPE-1 | GP120 | HUMAN MONOCLONAL-ANTIBODIES | CELL BIOLOGY
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7. Full Text Structure and Recognition of a Novel HIV-1 gp120-gp41 Interface Antibody that Caused MPER Exposure through Viral Escape
by Wibmer, Constantinos Kurt and Gorman, Jason and Ozorowski, Gabriel and Bhiman, Jinal N and Sheward, Daniel J and Elliott, Debra H and Rouelle, Julie and Smira, Ashley and Joyce, M. Gordon and Ndabambi, Nonkululeko and Druz, Aliaksandr and Asokan, Mangai and Burton, Dennis R and Connors, Mark and Abdool Karim, Salim S and Mascola, John R and Robinson, James E and Ward, Andrew B and Williamson, Carolyn and Kwong, Peter D and Morris, Lynn and Moore, Penny L and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
PLoS Pathogens, ISSN 1553-7366, 01/2017, Volume 13, Issue 1, pp. e1006074 - e1006074
A comprehensive understanding of the regions on HIV-1 envelope trimers targeted by broadly neutralizing antibodies may contribute to rational design of an... 
ENVELOPE GLYCOPROTEIN TRIMERS | SITE | MUCOSAL SHIV CHALLENGE | B-CELL RESPONSES | NEUTRALIZING ANTIBODIES | BROAD NEUTRALIZATION | MICROBIOLOGY | CONFORMATIONAL EPITOPE | VIROLOGY | GLYCOSYLATION PROFILES | IMMUNODEFICIENCY-VIRUS TYPE-1 | HUMAN MONOCLONAL-ANTIBODIES | PARASITOLOGY | Prevention | AIDS vaccines | Monoclonal antibodies | Research | HIV infection | Health aspects | Risk factors | Pediatrics | Health sciences | Manycompanies | Immunoglobulins | Laboratories | Colleges & universities | Vaccines | Virology | Infectious diseases | Acquired immune deficiency syndrome--AIDS | Mutagenesis | Collaboration | Human immunodeficiency virus--HIV | Mutation | Research centers | Index Medicus | BASIC BIOLOGICAL SCIENCES | AIDS | Acquired immune deficiency syndrome | HIV | Human immunodeficiency virus
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8. Full Text New member of the V1V2-directed CAP256-VRC26 lineage that shows increased breadth and exceptional potency
by Doria-Rose, Nicole A and Bhiman, Jinal N and Roark, Ryan S and Schramm, Chaim A and Gorman, Jason and Chuang, Gwo-Yu and Pancera, Marie and Cale, Evan M and Ernandes, Michael J and Louder, Mark K and Asokan, Mangaiarkarasi and Bailer, Robert T and Druz, Aliaksandr and Fraschilla, Isabella R and Garrett, Nigel J and Jarosinski, Marissa and Lynch, Rebecca M and McKee, Krisha and O'Dell, Sijy and Pegu, Amarendra and Schmidt, Stephen D and Staupe, Ryan P and Sutton, Matthew S and Wang, Keyun and Wibmer, Constantinos Kurt and Haynes, Barton F and Abdool-Karim, Salim and Shapiro, Lawrence and Kwong, Peter D and Moore, Penny L and Morris, Lynn and Mascola, John R and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Journal of Virology, ISSN 0022-538X, 2016, Volume 90, Issue 1, pp. 76 - 91
The epitopes defined by HIV-1 broadly neutralizing antibodies (bNAbs) are valuable templates for vaccine design, and studies of the immunological development... 
VACCINE DEVELOPMENT | V1/V2 DOMAIN | VIRUS | VIROLOGY | RECOGNITION | BROADLY NEUTRALIZING ANTIBODIES | HIV-1 ENVELOPE TRIMER | SEQUENCE | HUMAN B-CELLS | INFECTION | HUMAN MONOCLONAL-ANTIBODIES | Epitope Mapping | HIV Infections - virology | Humans | Molecular Sequence Data | Antibodies, Neutralizing - genetics | HIV Antibodies - isolation & purification | Sequence Analysis, DNA | Antibodies, Neutralizing - isolation & purification | Cross Reactions | HIV Envelope Protein gp120 - immunology | HIV Infections - immunology | Antibodies, Neutralizing - immunology | HIV-1 - immunology | HIV Antibodies - immunology | Inhibitory Concentration 50 | Female | HIV Antibodies - genetics | Index Medicus
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9. Full Text Antibody Specificities Associated with Neutralization Breadth in Plasma from Human Immunodeficiency Virus Type 1 Subtype C-Infected Blood Donors
by Elin S. Gray and Natasha Taylor and Diane Wycuff and Penny L. Moore and Georgia D. Tomaras and Constantinos Kurt Wibmer and Adrian Puren and Allan DeCamp and Peter B. Gilbert and Blake Wood and David C. Montefiori and James M. Binley and George M. Shaw and Barton F. Haynes and John R. Mascola and Lynn Morris
Journal of Virology, ISSN 0022-538X, 09/2009, Volume 83, Issue 17, pp. 8925 - 8937
Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley... 
HIV VACCINE DESIGN | RESPONSES | PROXIMAL EXTERNAL REGION | ENV CLONES | EPITOPE | VIROLOGY | ANTICARDIOLIPIN ANTIBODIES | CORECEPTOR BINDING-SITE | ENVELOPE | HUMAN MONOCLONAL-ANTIBODY | GP120 | Cross Reactions | HIV Antibodies - blood | Antibody Specificity | Blood Donors | Epitope Mapping | HIV-1 - immunology | Humans | Neutralization Tests | Antibodies, Anticardiolipin - blood | Index Medicus | Pathogenesis and Immunity
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10. Full Text Select gp120 V2 domain specific antibodies derived from HIV and SIV infection and vaccination inhibit gp120 binding to α4β7
by Lertjuthaporn, Sakaorat and Cicala, Claudia and Van Ryk, Donald and Liu, Matthew and Yolitz, Jason and Wei, Danlan and Nawaz, Fatima and Doyle, Allison and Horowitch, Brooke and Park, Chung and Lu, Shan and Lou, Yang and Wang, Shixia and Pan, Ruimin and Jiang, Xunqing and Villinger, Francois and Byrareddy, Siddappa N and Santangelo, Philip J and Morris, Lynn and Wibmer, Constantinos Kurt and Biris, Kristin and Mason, Rosemarie D and Gorman, Jason and Hiatt, Joseph and Martinelli, Elena and Roederer, Mario and Fujikawa, Dai and Gorini, Giacomo and Franchini, Genoveffa and Arakelyan, Anush and Ansari, Aftab A and Pattanapanyasat, Kovit and Kong, Xiang-Peng and Fauci, Anthony S and Arthos, James
PLoS Pathogens, ISSN 1553-7366, 08/2018, Volume 14, Issue 8, pp. e1007278 - e1007278
The GI tract is preferentially targeted during acute/early HIV-1 infection. Consequent damage to the gut plays a central role in HIV pathogenesis. The basis... 
Sieve analysis | Health sciences | Residues | Inflammatory bowel diseases | Peptides | Laboratories | Pathogenesis | Vaccination | Antibodies | Amino acids | Antagonists | Infections | Biochemistry | Vaccines | Tissues | Seeding | Cell surface | Mimicry | Cell adhesion & migration | Homing | Cell growth | Immunology |