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1. Full Text Recombinant HIV envelope trimer selects for quaternary-dependent antibodies targeting the trimer apex
by Devin Sok and Marit J. van Gils and Matthias Pauthner and Jean-Philippe Julien and Karen L. Saye-Francisco and Jessica Hsueh and Bryan Briney and Jeong Hyun Lee and Khoa M. Le and Peter S. Lee and Yuanzi Hua and Michael S. Seaman and John P. Moore and Andrew B. Ward and Ian A. Wilson and Rogier W. Sanders and Dennis R. Burton
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 12/2014, Volume 111, Issue 49, pp. 17624 - 17629
Broadly neutralizing antibodies (bnAbs) targeting the trimer apex of HIV envelope are favored candidates for vaccine design and immunotherapy because of their... 
Antigens | Germ cells | HIV | B lymphocytes | Neutralizing antibodies | Vaccination | Antibodies | Trimers | Epitopes | HIV 1 | BG505 SOSIP | B cell | Vaccine | Broadly neutralizing antibodies | MULTIDISCIPLINARY SCIENCES | HUMAN-IMMUNODEFICIENCY-VIRUS | broadly neutralizing antibodies | B-CELLS | vaccine | CONFORMATIONAL EPITOPE | ENV TRIMERS | BINDING-SITE | CD4 BINDING | HUMAN MONOCLONAL-ANTIBODIES | TYPE-1 | N-GLYCAN RECOGNITION | Amino Acid Sequence | Humans | Molecular Conformation | Models, Molecular | Molecular Sequence Data | Neutralization Tests | Peptide Library | Phylogeny | Protein Folding | Cross Reactions | Genetic Variation | HIV Envelope Protein gp120 - immunology | Sequence Homology, Amino Acid | HIV Infections - immunology | Antibodies, Neutralizing - immunology | B-Lymphocytes - immunology | HIV Antibodies - immunology | Recombinant Proteins - immunology | Base Sequence | Inhibitory Concentration 50 | Immunologic Memory | Leukocytes, Mononuclear - cytology | Epitopes - chemistry | Genetic research | Protein research | Genetic aspects | Research | HIV antibodies | Genetic recombination | Vaccines | Human immunodeficiency virus--HIV | Immunotherapy | Cells | Biological Sciences
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2. Full Text Abstracts of the HIV Research for Prevention Meeting, HIVR4P, 17-20 October, 2016, Chicago, USA
by Sullivan, Patrick and Yuan, Maoli and Coleman, John and Destefano, Joanne and Zhang, Xinsheng and Yates, Nicole and Barouch, Dan and Ackerman, Margaret and Decamp, Allan and Alter, Galit and Tomaras, Georgia and Tomaras, Georgia and Montefiori, David and Montefiori, David and Rasmussen, Beth and Morrow, Gavin and Koff, Wayne and Kashuba, Angela and Kashuba, Angela and Mascola, John and Picker, Louis and Kent, Stephen and Selhorst, Philippe and Masson, Lindi and Ngandu, Nobubelo and Rademeyer, Cecilia and Karim, Quarraisha Abdool and Kijak, Gustavo and Barouch, Dan and Rasheed, Ata Ur and Havenar-Daughton, Colin and Pham, Matthew and Kovalenkov, Yevgeniy and Gumber, Sanjeev and Johnson, Matthew and Wrammert, Jens and Villinger, Francois and Haynes, Barton and Haynes, Barton and Fox, Christopher and Reed, Steve and Vasilakos, John and Tomai, Mark and Crotty, Shane and Ahmed, Rafi and Pulendran, Bali and Fukazawa, Yoshinori and Lifson, Jeffrey and Lifson, Jeffrey and Moore, Penny and Chatora, Kumbirai and Skorochod, Elisabeth and Madidi, Ngonidzashe and Gomez, Anabel and Ncube, Getrude and Sundaram, Maaya and Kretschmer, Steve and Pauthner, Matthias and Briney, Bryan and Lee, Jeong Hyun and Saye-Francisco, Karen and Hsueh, Jessica and Ramos, Alejandra and Le, Khoa and Jones, Meaghan and Jardine, Joseph and Bastidas, Raiza and Sarkar, Anita and Liang, Chi-Hui and Wilson, Ian and Ward, Andrew and Zhu, Jiang and Poignard, Pascal and Burton, Dennis and Krebs, Shelly and Law, Wiliam and Gift, Syna and Chenine, Agnes and Rolland, Morgane and Moody, M. Anthony and Jarosinski, Marissa and Georgiev, Ivelin and Chuang, Gwo-Yu and Chuang, Gwo-Yu and Asokan, Mangaiarkarasi and Bailer, Robert T and Cale, Evan M and Louder, Mark and Kwong, Peter D and Polonis, Victoria and Tovanabutra, Sodsai and Robb, Merlin and Mascola, John R and Wibmer, Constantinos Kurt and Wibmer, Constantinos Kurt and Madzorera, Vimbai S and Doria-Rose, Nicole A and Morris, Lynn and Moore, Penny L and Anthony, Colin and ...
AIDS Research and Human Retroviruses, ISSN 0889-2229, 10/2016, Volume 32, Issue S1, pp. 1 - 409
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3. Full Text Rapid elicitation of broadly neutralizing antibodies to HIV by immunization in cows
by Sok, Devin and Le, Khoa M and Vadnais, Melissa and Saye-Francisco, Karen L and Jardine, Joseph G and Torres, Jonathan L and Berndsen, Zachary T and Kong, Leopold and Stanfield, Robyn and Ruiz, Jennifer and Ramos, Alejandra and Liang, Chi-Hui and Chen, Patricia L and Criscitiello, Michael F and Mwangi, Waithaka and Wilson, Ian A and Ward, Andrew B and Smider, Vaughn V and Burton, Dennis R
Nature, ISSN 0028-0836, 08/2017, Volume 548, Issue 7665, pp. 108 - 111
No immunogen to date has reliably elicited broadly neutralizing antibodies to HIV in humans or animal models. Advances in the design of immunogens that... 
HEAVY-CHAINS | LONG CDR3S | SYSTEM | POTENT | MULTIDISCIPLINARY SCIENCES | ENVELOPE | V-H FAMILY | GENERATION | DIVERSITY | DISCOVERY | BOVINE IGM ANTIBODIES | Antibodies, Neutralizing - isolation & purification | Amino Acid Sequence | Antibodies, Neutralizing - immunology | Immunization | Animals | Antibodies, Neutralizing - biosynthesis | Antibodies, Neutralizing - chemistry | Humans | HEK293 Cells | HIV - immunology | HIV Envelope Protein gp160 - immunology | Cattle - immunology | Immunogenetics | HIV antibodies | Cows | Vaccination of animals | Genetic aspects | Research | Methods | Immunological research | Animal models | Immunoglobulins | Glycoprotein | Antibodies | Amino acids | Vaccines | Epitopes | Cattle | Neutralizing | Human immunodeficiency virus--HIV | Monoclonal antibodies | Neutralization
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4. Full Text A Prominent Site of Antibody Vulnerability on HIV Envelope Incorporates a Motif Associated with CCR5 Binding and Its Camouflaging Glycans
by Sok, Devin and Pauthner, Matthias and Briney, Bryan and Lee, Jeong Hyun and Saye-Francisco, Karen L and Hsueh, Jessica and Ramos, Alejandra and Le, Khoa M and Jones, Meaghan and Jardine, Joseph G and Bastidas, Raiza and Sarkar, Anita and Liang, Chi-Hui and Shivatare, Sachin S and Wu, Chung-Yi and Schief, William R and Wong, Chi-Huey and Wilson, Ian A and Ward, Andrew B and Zhu, Jiang and Poignard, Pascal and Burton, Dennis R
Immunity, ISSN 1074-7613, 07/2016, Volume 45, Issue 1, pp. 31 - 45
The dense patch of high-mannose-type glycans surrounding the N332 glycan on the HIV envelope glycoprotein (Env) is targeted by multiple broadly neutralizing... 
POTENT | HEPATITIS-C VIRUS | BROADLY NEUTRALIZING ANTIBODIES | CRYSTAL-STRUCTURE | VACCINE DESIGN | IMMUNODEFICIENCY-VIRUS TYPE-1 | IMMUNOLOGY | HUMAN MONOCLONAL-ANTIBODIES | CRYO-EM STRUCTURE | DEPENDENT EPITOPE | GP41-GP120 INTERFACE | Epitope Mapping | Binding Sites, Antibody - immunology | Peptide Fragments - metabolism | Epitopes - metabolism | Humans | Polysaccharides - immunology | HIV Envelope Protein gp120 - metabolism | Amino Acid Motifs | Polysaccharides - metabolism | HIV Envelope Protein gp120 - immunology | HIV Infections - immunology | Antibodies, Neutralizing - immunology | HIV-1 - immunology | Receptors, CCR5 - metabolism | Genetic Engineering | HIV Antibodies - immunology | Immunity, Humoral | HEK293 Cells | Protein Binding | Immunologic Memory | CD4 Antigens - metabolism | Viral antibodies | International relief | Antigens | Polysaccharides | AIDS vaccines | Peptides | Antibodies | HIV (Viruses) | Sugars | Monosaccharides | Immunoglobulins | Immunology | Acquired immune deficiency syndrome--AIDS | Human immunodeficiency virus--HIV | Influenza | Viruses | Vaccines | Experiments | Binding sites | Manuscripts | Life Sciences | Biomolecules | Biochemistry, Molecular Biology
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5. Full Text Minimally Mutated HIV-1 Broadly Neutralizing Antibodies to Guide Reductionist Vaccine Design
by Jardine, Joseph G and Sok, Devin and Julien, Jean-Philippe and Briney, Bryan and Sarkar, Anita and Liang, Chi-Hui and Scherer, Erin A and Henry Dunand, Carole J and Adachi, Yumiko and Diwanji, Devan and Hsueh, Jessica and Jones, Meaghan and Kalyuzhniy, Oleksandr and Kubitz, Michael and Spencer, Skye and Pauthner, Matthias and Saye-Francisco, Karen L and Sesterhenn, Fabian and Wilson, Patrick C and Galloway, Denise M and Stanfield, Robyn L and Wilson, Ian A and Burton, Dennis R and Schief, William R and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
PLoS Pathogens, ISSN 1553-7366, 08/2016, Volume 12, Issue 8, p. e1005815
An optimal HIV vaccine should induce broadly neutralizing antibodies (bnAbs) that neutralize diverse viral strains and subtypes. However, potent bnAbs develop... 
SITE | POTENT NEUTRALIZATION | CRYSTAL-STRUCTURE | MICROBIOLOGY | ENVELOPE PROTEIN | IMMUNOGEN DESIGN | MATURATION | EVOLUTION | VIROLOGY | STRUCTURAL BASIS | HUMAN MONOCLONAL-ANTIBODIES | LINEAGE | PARASITOLOGY | Amino Acid Sequence | Humans | AIDS Vaccines - immunology | Models, Molecular | Antibodies, Neutralizing - genetics | HIV Infections - immunology | Antibodies, Neutralizing - immunology | HIV-1 - immunology | High-Throughput Screening Assays | HIV Antibodies - immunology | Drug Design | HIV Antibodies - genetics | Mutation | Antigen-antibody reactions | AIDS vaccines | HIV antibodies | Gene mutations | Innovations | Genetic aspects | Health aspects | Immunoglobulins | Acquired immune deficiency syndrome--AIDS | Mutagenesis | Funding | Human immunodeficiency virus--HIV | Data collection | Viruses | Vaccines | Acquired immune deficiency syndrome | HIV | AIDS | Human immunodeficiency virus
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6. Full Text Structural Evolution of Glycan Recognition by a Family of Potent HIV Antibodies
by Garces, Fernando and Sok, Devin and Kong, Leopold and McBride, Ryan and Kim, Helen J and Saye-Francisco, Karen F and Julien, Jean-Philippe and Hua, Yuanzi and Cupo, Albert and Moore, John P and Paulson, James C and Ward, Andrew B and Burton, Dennis R and Wilson, Ian A
Cell, ISSN 0092-8674, 09/2014, Volume 159, Issue 1, pp. 69 - 79
The HIV envelope glycoprotein (Env) is densely covered with self-glycans that should help shield it from recognition by the human immune system. Here, we... 
COMPLEX | DOMAIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | BROAD | DEGLYCOSYLATION | GLYCOSYLATION | GP120 | CLONES | CELL BIOLOGY | HIV Antibodies - metabolism | Amino Acid Sequence | AIDS Vaccines - immunology | Antibodies, Neutralizing - metabolism | Models, Molecular | Molecular Sequence Data | HIV Antibodies - chemistry | AIDS Vaccines - chemistry | HIV Envelope Protein gp120 - immunology | HIV-1 - immunology | Sequence Alignment | HIV-1 - chemistry | Antibodies, Neutralizing - chemistry | HIV Envelope Protein gp120 - chemistry | Proteins | International relief | Polysaccharides | AIDS vaccines | HIV antibodies | HIV (Viruses) | Antigens | Research institutes | Molecular biology | Index Medicus
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7. Full Text Tailored Immunogens Direct Affinity Maturation toward HIV Neutralizing Antibodies
by Briney, Bryan and Sok, Devin and Jardine, Joseph G and Kulp, Daniel W and Skog, Patrick and Menis, Sergey and Jacak, Ronald and Kalyuzhniy, Oleksandr and de Val, Natalia and Sesterhenn, Fabian and Le, Khoa M and Ramos, Alejandra and Jones, Meaghan and Saye-Francisco, Karen L and Blane, Tanya R and Spencer, Skye and Georgeson, Erik and Hu, Xiaozhen and Ozorowski, Gabriel and Adachi, Yumiko and Kubitz, Michael and Sarkar, Anita and Wilson, Ian A and Ward, Andrew B and Nemazee, David and Burton, Dennis R and Schief, William R
Cell, ISSN 0092-8674, 09/2016, Volume 166, Issue 6, pp. 1459 - 1470.e11
Induction of broadly neutralizing antibodies (bnAbs) is a primary goal of HIV vaccine development. VRC01-class bnAbs are important vaccine leads because their... 
B-CELLS | DESIGN | CD4-BINDING SITE | STRUCTURAL BASIS | POTENCY | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | BROAD | CLADE | GENERATION | MONOCLONAL-ANTIBODIES | CELL BIOLOGY | HIV Antibodies - blood | Amino Acid Sequence | Humans | Male | Mice, Transgenic | Antibodies, Neutralizing - genetics | Vaccines, Synthetic - immunology | Antigens, Viral - immunology | Antibodies, Neutralizing - immunology | HIV-1 - immunology | Sequence Alignment | Animals | B-Lymphocytes - immunology | HIV Antibodies - immunology | Adult | Female | Mice | HIV Antibodies - genetics | Mutation | Vaccines, Synthetic - administration & dosage | Viral antibodies | Antigens | AIDS vaccines | Analysis | Antibodies | Genetic engineering | B cells | Research institutes | HIV (Viruses)
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8. Full Text Lipid interactions and angle of approach to the HIV-1 viral membrane of broadly neutralizing antibody 10E8: Insights for vaccine and therapeutic design
by Irimia, Adriana and Serra, Andreia M and Sarkar, Anita and Jacak, Ronald and Kalyuzhniy, Oleksandr and Sok, Devin and Saye-Francisco, Karen L and Schiffner, Torben and Tingle, Ryan and Kubitz, Michael and Adachi, Yumiko and Stanfield, Robyn L and Deller, Marc C and Burton, Dennis R and Schief, William R and Wilson, Ian A and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
PLoS Pathogens, ISSN 1553-7366, 02/2017, Volume 13, Issue 2, pp. e1006212 - e1006212
Among broadly neutralizing antibodies to HIV, 10E8 exhibits greater neutralizing breadth than most. Consequently, this antibody is the focus of... 
2F5 | GP41 | MICROBIOLOGY | ANTI-HIV-1 ANTIBODIES | PROXIMAL EXTERNAL REGION | EPITOPE | VIROLOGY | STRUCTURAL BASIS | ENVELOPE | IMMUNODEFICIENCY-VIRUS TYPE-1 | MONOCLONAL-ANTIBODIES | CRYO-EM STRUCTURE | PARASITOLOGY | Surface Plasmon Resonance | Antibodies, Neutralizing - immunology | HIV-1 - immunology | HIV Antibodies - immunology | Antibodies, Blocking - chemistry | HIV Envelope Protein gp41 - immunology | X-Ray Diffraction | Antibodies, Neutralizing - chemistry | Humans | Antibodies, Blocking - immunology | Protein Conformation | HIV Antibodies - chemistry | Membrane lipids | Viral envelopes | HIV antibodies | Properties | Analysis | Protein-protein interactions | Immunology | Acquired immune deficiency syndrome--AIDS | Human immunodeficiency virus--HIV | Collaboration | Data collection | Glycerol | Lipids | Biology | Vaccines | Pharmaceutical industry | Research centers | Index Medicus | AIDS | Acquired immune deficiency syndrome | HIV | Human immunodeficiency virus
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9. Full Text Promiscuous glycan site recognition by antibodies to the high-mannose patch of gp120 broadens neutralization of HIV
by Sok, Devin and Doores, Katie J and Briney, Bryan and Le, Khoa M and Saye-Francisco, Karen L and Ramos, Alejandra and Kulp, Daniel W and Julien, Jean-Philippe and Menis, Sergey and Wickramasinghe, Lalinda and Seaman, Michael S and Schief, William R and Wilson, Ian A and Poignard, Pascal and Burton, Dennis R
Science Translational Medicine, ISSN 1946-6234, 05/2014, Volume 6, Issue 236, pp. 236ra63 - 236ra63
Broadly neutralizing monoclonal antibodies (bnmAbs) that target the high- mannose patch centered around the glycan at position 332 on HIV Env are promising... 
MEDICINE, RESEARCH & EXPERIMENTAL | POTENT | DESIGN | VIRUS | EPITOPE | CD4 BINDING | GLYCOPROTEIN GP120 | MONOCLONAL-ANTIBODIES | CLUSTER | DOMAIN EXCHANGE | OCCUPANCY | CELL BIOLOGY | Enzyme-Linked Immunosorbent Assay | HIV Seropositivity | Humans | Immunoglobulin G - chemistry | Molecular Sequence Data | Neutralization Tests | Glycosylation | HIV Antibodies - chemistry | HIV Envelope Protein gp120 - immunology | HIV Infections - immunology | HIV-1 - immunology | Time Factors | Antibodies, Neutralizing - chemistry | Inhibitory Concentration 50 | Polysaccharides - chemistry | Epitopes - chemistry | HIV Envelope Protein gp120 - chemistry | Binding Sites | Antibodies, Monoclonal - chemistry | Mannose - chemistry
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10. Full Text Sequential Immunization Elicits Broadly Neutralizing Anti-HIV-1 Antibodies in Ig Knockin Mice
by Escolano, Amelia and Steichen, Jon M and Dosenovic, Pia and Kulp, Daniel W and Golijanin, Jovana and Sok, Devin and Freund, Natalia T and Gitlin, Alexander D and Oliveira, Thiago and Araki, Tatsuya and Lowe, Sarina and Chen, Spencer T and Heinemann, Jennifer and Yao, Kai-Hui and Georgeson, Erik and Saye-Francisco, Karen L and Gazumyan, Anna and Adachi, Yumiko and Kubitz, Michael and Burton, Dennis R and Schief, William R and Nussenzweig, Michel C
Cell, ISSN 0092-8674, 09/2016, Volume 166, Issue 6, pp. 1445 - 1458.e12
A vaccine that elicits broadly neutralizing antibodies (bNAbs) against HIV-1 is likely to be protective, but this has not been achieved. To explore... 
B-CELLS | VACCINE DEVELOPMENT | RESPONSES | CHIMERIC VIRUS | IN-VITRO | PROTECTION | AFFINITY MATURATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | HIV-1 ENVELOPE GLYCOPROTEIN | IMMUNOGEN DESIGN | LINEAGE | CELL BIOLOGY | Amino Acid Sequence | Immunization | Antigens, Viral - administration & dosage | AIDS Vaccines - immunology | Antigens, Viral - genetics | Immunoglobulins - genetics | DNA Primers - chemistry | Gene Knock-In Techniques | Epitopes - immunology | Antigens, Viral - immunology | HIV Infections - immunology | Antibodies, Neutralizing - immunology | HIV-1 - immunology | Sequence Alignment | Animals | B-Lymphocytes - immunology | HIV Antibodies - immunology | Cloning, Molecular | Mice | Mutation | International relief | Polysaccharides | AIDS vaccines | B cells | HIV (Viruses) | Enzyme-linked immunosorbent assay | Antigenic determinants
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