B
Baoshan Zhang
Researcher at National Institutes of Health
Publications - 121
Citations - 15823
Baoshan Zhang is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Epitope & Antibody. The author has an hindex of 45, co-authored 121 publications receiving 11448 citations. Previous affiliations of Baoshan Zhang include Vaccine Research Center.
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Journal ArticleDOI
Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7.
Pengfei Wang,Manoj S. Nair,Lihong Liu,Sho Iketani,Sho Iketani,Yang Luo,Yicheng Guo,Maple Wang,Jian Yu,Baoshan Zhang,Peter D. Kwong,Peter D. Kwong,Barney S. Graham,John R. Mascola,Jennifer Y Chang,Jennifer Y Chang,Michael T. Yin,Michael T. Yin,Magdalena E. Sobieszczyk,Magdalena E. Sobieszczyk,Christos A. Kyratsous,Lawrence Shapiro,Lawrence Shapiro,Zizhang Sheng,Yaoxing Huang,David D. Ho,David D. Ho +26 more
TL;DR: In this paper, the authors show that B.1.7 is refractory to neutralization by most monoclonal antibodies against the N-terminal domain of the spike protein and is relatively resistant to a few monoclanal antibody against the receptor-binding domain.
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Co-evolution of a broadly neutralizing HIV-1 antibody and founder virus
Hua-Xin Liao,Rebecca M. Lynch,Tongqing Zhou,Feng Gao,Feng Gao,S. Munir Alam,S. Munir Alam,Scott D. Boyd,Andrew Fire,Krishna M. Roskin,Chaim A. Schramm,Zhenhai Zhang,Jiang Zhu,Lawrence Shapiro,Lawrence Shapiro,Nisc Comparative Sequencing Program,James C. Mullikin,Sandrasegaram Gnanakaran,Peter T. Hraber,Kevin Wiehe,Kevin Wiehe,Garnett Kelsoe,Garnett Kelsoe,Guang Yang,Guang Yang,Shi-Mao Xia,Shi-Mao Xia,David C. Montefiori,David C. Montefiori,Robert Parks,Robert Parks,Krissey E. Lloyd,Krissey E. Lloyd,Richard M. Scearce,Richard M. Scearce,Kelly A. Soderberg,Kelly A. Soderberg,Myron S. Cohen,Gift Kamanga,Mark K. Louder,Lillian Tran,Yue Chen,Yue Chen,Fangping Cai,Fangping Cai,Sheri Chen,Sheri Chen,Stephanie Moquin,Xiulian Du,M. Gordon Joyce,Sanjay Srivatsan,Baoshan Zhang,Anqi Zheng,George M. Shaw,Beatrice H. Hahn,Thomas B. Kepler,Bette T. Korber,Peter D. Kwong,John R. Mascola,Barton F. Haynes,Barton F. Haynes +60 more
TL;DR: The isolation, evolution and structure of a broadly neutralizing antibody from an African donor followed from the time of infection and its co-crystal structure revealed a new loop-based mechanism of CD4-binding-site recognition.
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Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9
Jason S. McLellan,Marie Pancera,Chris Carrico,Jason Gorman,Jean-Philippe Julien,Reza Khayat,Robert K. Louder,Robert Pejchal,Mallika Sastry,Kaifan Dai,Sijy O'Dell,Nikita Patel,Syed Shahzad-ul-Hussan,Yongping Yang,Baoshan Zhang,Tongqing Zhou,Jiang Zhu,Jeffrey C. Boyington,Gwo-Yu Chuang,Devan Diwanji,Ivelin S. Georgiev,Young Do Kwon,Doyung Lee,Mark K. Louder,Stephanie Moquin,Stephen D. Schmidt,Zhi Yong Yang,Mattia Bonsignori,John A. Crump,John A. Crump,Saidi Kapiga,Noel E. Sam,Barton F. Haynes,Dennis R. Burton,Dennis R. Burton,Wayne C. Koff,Laura M. Walker,Sanjay Phogat,Richard T. Wyatt,Jared Orwenyo,Lai-Xi Wang,James Arthos,Carole A. Bewley,John R. Mascola,Gary J. Nabel,William R. Schief,William R. Schief,Andrew B. Ward,Ian A. Wilson,Peter D. Kwong +49 more
TL;DR: The structure of V1/V2 in complex with PG9 is reported, identifying a paradigm of antibody recognition for highly glycosylated antigens, which—with PG9—involves a site of vulnerability comprising just two glycans and a strand.
Journal ArticleDOI
Broad and potent neutralization of HIV-1 by a gp41-specific human antibody
Jinghe Huang,Gilad Ofek,Leo B. Laub,Mark K. Louder,Nicole A. Doria-Rose,Nancy S. Longo,Hiromi Imamichi,Robert T. Bailer,Bimal K. Chakrabarti,Shailendra Kumar Sharma,S. Munir Alam,Tao Wang,Yongping Yang,Baoshan Zhang,Stephen A. Migueles,Richard T. Wyatt,Barton F. Haynes,Peter D. Kwong,John R. Mascola,Mark Connors +19 more
TL;DR: The structure of 10E8 in complex with the complete MPER revealed a site of vulnerability comprising a narrow stretch of highly conserved gp41-hydrophobic residues and a critical arginine or lysine just before the transmembrane region, suggesting the importance of these residues for neutralization.
Journal ArticleDOI
Structure-Based Design of a Fusion Glycoprotein Vaccine for Respiratory Syncytial Virus
Jason S. McLellan,Man Chen,M. Gordon Joyce,Mallika Sastry,Guillaume Stewart-Jones,Yongping Yang,Baoshan Zhang,Lei Chen,Sanjay Srivatsan,Anqi Zheng,Tongqing Zhou,Kevin W. Graepel,Azad Kumar,Syed M. Moin,Jeffrey C. Boyington,Gwo-Yu Chuang,Cinque Soto,Ulrich Baxa,Arjen Q. Bakker,Hergen Spits,Tim Beaumont,Zizheng Zheng,Ningshao Xia,Sung Youl Ko,John Paul Todd,Srinivas S. Rao,Barney S. Graham,Peter D. Kwong +27 more
TL;DR: A viral antigen is sought that provides greater protection than currently available vaccines and focused on antigenic site Ø, a metastable site specific to the prefusion state of the RSV fusion (F) glycoprotein, as this site is targeted by extremely potent RSV-neutralizing antibodies.