J
Jinghe Huang
Researcher at Fudan University
Publications - 56
Citations - 5329
Jinghe Huang is an academic researcher from Fudan University. The author has contributed to research in topics: Antibody & Medicine. The author has an hindex of 25, co-authored 46 publications receiving 4516 citations. Previous affiliations of Jinghe Huang include Harvard University & Ragon Institute of MGH, MIT and Harvard.
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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 and immune recognition of trimeric pre-fusion HIV-1 Env
Marie Pancera,Tongqing Zhou,Aliaksandr Druz,Ivelin S. Georgiev,Cinque Soto,Jason Gorman,Jinghe Huang,Priyamvada Acharya,Gwo-Yu Chuang,Gilad Ofek,Guillaume Stewart-Jones,Jonathan Stuckey,Robert T. Bailer,M. Gordon Joyce,Mark K. Louder,Nancy Tumba,Yongping Yang,Baoshan Zhang,Myron S. Cohen,Barton F. Haynes,John R. Mascola,Lynn Morris,James B. Munro,Scott C. Blanchard,Walther Mothes,Mark Connors,Peter D. Kwong +26 more
TL;DR: The structure at 3.5 Å resolution for an HIV-1 Env trimer captured in a mature closed state by antibodies PGT122 and 35O22 is reported, revealing the pre-fusion conformation of gp41, rearrangements needed for fusion activation, and defines parameters of immune evasion and immune recognition.
Posted ContentDOI
Neutralizing antibody responses to SARS-CoV-2 in a COVID-19 recovered patient cohort and their implications
Fan Wu,Aojie Wang,Liu Mei,Qimin Wang,Jun Chen,Shuai Xia,Yun Ling,Yuling Zhang,Jingna Xun,Lu Lu,Shibo Jiang,Hongzhou Lu,Yumei Wen,Jinghe Huang +13 more
TL;DR: The correlation of NAb titers with age, lymphocyte counts, and blood CRP levels suggested that the interplay between virus and host immune response in coronavirus infections should be further explored for the development of effective vaccine against SARS-CoV-2 virus.
Journal ArticleDOI
Broad and potent HIV-1 neutralization by a human antibody that binds the gp41–gp120 interface
Jinghe Huang,Byong H. Kang,Marie Pancera,Jeong Hyun Lee,Tommy Tong,Yu Feng,Hiromi Imamichi,Ivelin S. Georgiev,Gwo-Yu Chuang,Aliaksandr Druz,Nicole A. Doria-Rose,Leo B. Laub,Kwinten Sliepen,Marit J. van Gils,Alba Torrents de la Peña,Ronald Derking,Per Johan Klasse,Stephen A. Migueles,Robert T. Bailer,Munir Alam,Pavel Pugach,Barton F. Haynes,Richard T. Wyatt,Rogier W. Sanders,James M. Binley,Andrew B. Ward,John R. Mascola,Peter D. Kwong,Mark Connors +28 more
TL;DR: A broad and extremely potent HIV-specific monoclonal antibody, termed 35O22, which binds a novel HIV-1 envelope glycoprotein (Env) epitope, which represents a novel site of vulnerability on HIV Env, which serum analysis indicates to be commonly elicited by natural infection.
Journal ArticleDOI
Identification of a CD4-Binding-Site Antibody to HIV that Evolved Near-Pan Neutralization Breadth.
Jinghe Huang,Byong H. Kang,Elise Ishida,Tongqing Zhou,Trevor Griesman,Zizhang Sheng,Fan Wu,Nicole A. Doria-Rose,Baoshan Zhang,Krisha McKee,Sijy O'Dell,Gwo-Yu Chuang,Aliaksandr Druz,Ivelin S. Georgiev,Chaim A. Schramm,Anqi Zheng,M. Gordon Joyce,Mangaiarkarasi Asokan,Amy Ransier,Sam Darko,Stephen A. Migueles,Robert T. Bailer,Mark K. Louder,S. Munir Alam,Robert Parks,Garnett Kelsoe,Tarra Von Holle,Barton F. Haynes,Daniel C. Douek,Vanessa M. Hirsch,Michael S. Seaman,Lawrence Shapiro,Lawrence Shapiro,John R. Mascola,Peter D. Kwong,Mark Connors +35 more
TL;DR: A CD4-binding site (CD4bs) antibody, named N6, is reported that potently neutralized 98% of HIV-1 isolates, including 16 of 20 that were resistant to other members of its class.