L
Lingshu Wang
Researcher at Vaccine Research Center
Publications - 11
Citations - 1682
Lingshu Wang is an academic researcher from Vaccine Research Center. The author has contributed to research in topics: Antibody & Coronavirus. The author has an hindex of 9, co-authored 11 publications receiving 1111 citations. Previous affiliations of Lingshu Wang include National Institutes of Health.
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Journal ArticleDOI
Immunogenicity and structures of a rationally designed prefusion MERS-CoV spike antigen
Jesper Pallesen,Nianshuang Wang,Kizzmekia S. Corbett,Daniel Wrapp,Robert N. Kirchdoerfer,Hannah L. Turner,Christopher A. Cottrell,Michelle M. Becker,Lingshu Wang,Wei Shi,Wing-Pui Kong,Erica L. Andres,Arminja N. Kettenbach,Mark R. Denison,Mark R. Denison,James D. Chappell,Barney S. Graham,Andrew B. Ward,Jason S. McLellan +18 more
TL;DR: An engineering strategy for stabilization of soluble S proteins in the prefusion conformation is described, which results in greatly increased expression, conformational homogeneity, and elicitation of potent antibody responses, and an engineered immunogen is able to elicit high neutralizing antibody titers against MERS-CoV.
Journal ArticleDOI
Induction of HIV Neutralizing Antibody Lineages in Mice with Diverse Precursor Repertoires.
Ming Tian,Ming Tian,Cheng Cheng,Xuejun Chen,Hongying Duan,Hwei-Ling Cheng,Hwei-Ling Cheng,Mai Dao,Mai Dao,Zizhang Sheng,Michael T. Kimble,Michael T. Kimble,Lingshu Wang,Sherry Lin,Sherry Lin,Stephen D. Schmidt,Zhou Du,Zhou Du,M. Gordon Joyce,Yiwei Chen,Yiwei Chen,Brandon J. DeKosky,Yimin Chen,Yimin Chen,Erica Normandin,Elizabeth Cantor,Elizabeth Cantor,Rita E. Chen,Nicole A. Doria-Rose,Yi Zhang,Wei Shi,Wing-Pui Kong,Misook Choe,Amy R. Henry,Farida Laboune,Ivelin S. Georgiev,Pei-Yi Huang,Pei-Yi Huang,Suvi Jain,Suvi Jain,Andrew T. McGuire,Eric Georgeson,Sergey Menis,Daniel C. Douek,William R. Schief,William R. Schief,William R. Schief,Leonidas Stamatatos,Peter D. Kwong,Lawrence Shapiro,Lawrence Shapiro,Barton F. Haynes,John R. Mascola,Frederick W. Alt,Frederick W. Alt +54 more
TL;DR: A mouse vaccination model is described that allows a germline human IGHV1-2(∗)02 segment to undergo normal V(D)J recombination and leads to the generation of peripheral B cells that express a highly diverse repertoire of VRC01-related receptors.
Posted ContentDOI
LY-CoV1404 (bebtelovimab) potently neutralizes SARS-CoV-2 variants
Kathryn Westendorf,Stefanie Žentelis,Denisa Foster,Peter Edward Vaillancourt,Wiggin M,Erica Lovett,van der Lee R,Jorg Hendle,A. Pustilnik,Sauder Jm,Lucas Kraft,Yuri Hwang,Robert W. Siegel,Chen J,Beverly A. Heinz,Richard E. Higgs,Kalleward N,Kevin R. Jepson,Rodrigo Goya,Maia A. Smith,David Collins,Davide Pellacani,Ping Xiang,de Puyraimond,Marketa Ricicova,Devorkin L,Pritchard C,O’Neill A,Dalal K,Panwar P,Dhupar H,Garces Fa,Courtney A. Cohen,John M. Dye,Kathleen E. Huie,Catherine V. Badger,Darwyn Kobasa,Darwyn Kobasa,Jonathan Audet,Jonathan Audet,Freitas Jj,Saleema Hassanali,Ina Hughes,Munoz L,Palma Hc,Bharathi Ramamurthy,Cross Rw,Cross Rw,Geisbert Tw,Geisbert Tw,Menacherry,Kumari G. Lokugamage,Borisevich,Lanz I,Lisa Anderson,Sipahimalani P,Kizzmekia S. Corbett,Lingshu Wang,Eun Sung Yang,Yanzhao Zhang,Wei Shi,Barney S. Graham,Mascola,Fernandez Tl,Carl L. Hansen,Ester Falconer,Bryan Edward Jones,Bryan C. Barnhart +67 more
TL;DR: The LY-CoV1404 (also known as bebtelovimab) is a highly potent, neutralizing, SARS CoV-2 spike glycoprotein receptor binding domain (RBD)-specific antibody identified from a convalescent COVID-19 patient sample, obtained approximately 60 days after symptom onset as mentioned in this paper.
Journal ArticleDOI
Trypsin treatment unlocks barrier for zoonotic bat coronavirus infection
Vineet D. Menachery,Vineet D. Menachery,Kenneth H. Dinnon,Boyd Yount,Eileen T. McAnarney,Eileen T. McAnarney,Lisa E. Gralinski,Andrew E. Hale,Rachel L. Graham,Trevor Scobey,Simon J. Anthony,Lingshu Wang,Barney S. Graham,Scott H. Randell,W. Ian Lipkin,Ralph S. Baric +15 more
TL;DR: Overcoming host restriction of two Middle East respiratory syndrome (MERS)-like bat CoVs using exogenous protease treatment demonstrates that proteolytic cleavage is the primary barrier to infection for a subset of zoonotic coronaviruses.
Journal ArticleDOI
Junctional and allele-specific residues are critical for MERS-CoV neutralization by an exceptionally potent germline-like antibody
Tianlei Ying,Ponraj Prabakaran,Lanying Du,Wei Shi,Yang Feng,Yanping Wang,Lingshu Wang,Wei Li,Wei Li,Shibo Jiang,Shibo Jiang,Dimiter S. Dimitrov,Tongqing Zhou +12 more
TL;DR: It is shown that m336, an exceptionally potent human anti-MERS-CoV antibody, is almost germline with only one somatic mutation in the heavy chain, revealing that its IGHV1-69-derived heavy chain provides more than 85% binding surface and that its epitope almost completely overlaps with the receptor-binding site.