M
Matthew D. Gray
Researcher at Fred Hutchinson Cancer Research Center
Publications - 16
Citations - 1231
Matthew D. Gray is an academic researcher from Fred Hutchinson Cancer Research Center. The author has contributed to research in topics: Antibody & Epitope. The author has an hindex of 9, co-authored 16 publications receiving 946 citations.
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Journal ArticleDOI
Structural repertoire of HIV-1-neutralizing antibodies targeting the CD4 supersite in 14 donors
Tongqing Zhou,Rebecca M. Lynch,Lei Chen,Priyamvada Acharya,Xueling Wu,Nicole A. Doria-Rose,M. Gordon Joyce,Daniel Lingwood,Cinque Soto,Robert T. Bailer,Michael J. Ernandes,Rui Kong,Nancy S. Longo,Mark K. Louder,Krisha McKee,Sijy O'Dell,Stephen D. Schmidt,Lillian Tran,Zhongjia Yang,Aliaksandr Druz,Timothy S. Luongo,Stephanie Moquin,Sanjay Srivatsan,Yongping Yang,Baoshan Zhang,Anqi Zheng,Marie Pancera,Tatsiana Kirys,Ivelin S. Georgiev,Tatyana Gindin,Hung-Pin Peng,An-Suei Yang,James C. Mullikin,Matthew D. Gray,Leonidas Stamatatos,Dennis R. Burton,Dennis R. Burton,Wayne C. Koff,Myron S. Cohen,Barton F. Haynes,Joseph P. Casazza,Mark Connors,Davide Corti,Antonio Lanzavecchia,Quentin J. Sattentau,Robin A. Weiss,Anthony P. West,Pamela J. Bjorkman,Johannes F. Scheid,Michel C. Nussenzweig,Michel C. Nussenzweig,Lawrence Shapiro,Lawrence Shapiro,John R. Mascola,Peter D. Kwong +54 more
TL;DR: The repertoire for effective recognition of the CD4 supersite thus comprises antibodies with distinct paratopes arrayed about two optimal geometric orientations, one achieved by CDR H3 ontogenies and the other achieved by VH-gene-restricted ontogeny.
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Immunization for HIV-1 Broadly Neutralizing Antibodies in Human Ig Knockin Mice
Pia Dosenovic,Lotta von Boehmer,Amelia Escolano,Joseph G. Jardine,Natalia T. Freund,Alexander D. Gitlin,Andrew T. McGuire,Daniel W. Kulp,Thiago Y. Oliveira,Louise Scharf,John Pietzsch,Matthew D. Gray,Albert Cupo,Marit J. van Gils,Kai Hui Yao,Cassie Liu,Anna Gazumyan,Anna Gazumyan,Michael S. Seaman,Pamela J. Bjorkman,Pamela J. Bjorkman,Rogier W. Sanders,Rogier W. Sanders,John P. Moore,Leonidas Stamatatos,Leonidas Stamatatos,William R. Schief,Michel C. Nussenzweig,Michel C. Nussenzweig +28 more
TL;DR: It is suggested that vaccination to elicit anti-HIV-1 antibodies will require immunization with a succession of related immunogens, specifically designed to activate B cells bearing germline antibodies.
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Transcriptional Programming of Normal and Inflamed Human Epidermis at Single-Cell Resolution.
Jeffrey B. Cheng,Andrew J. Sedgewick,Alex I Finnegan,Paymann Harirchian,Jerry Lee,Sunjong Kwon,Marlys S. Fassett,Justin Golovato,Matthew D. Gray,Ruby Ghadially,Wilson Liao,Bethany E. Perez White,Theodora M. Mauro,Thaddeus W. Mully,Esther A. Kim,Hani Sbitany,Isaac M. Neuhaus,Roy C. Grekin,Siegrid S. Yu,Joe W. Gray,Elizabeth Purdom,Ralf Paus,Ralf Paus,Charles J. Vaske,Stephen C. Benz,Jun S. Song,Raymond J. Cho +26 more
TL;DR: This compendium of RNA profiles provides a critical step toward elucidating epidermal diseases of development, differentiation, and inflammation.
Journal ArticleDOI
Specifically modified Env immunogens activate B-cell precursors of broadly neutralizing HIV-1 antibodies in transgenic mice
Andrew T. McGuire,Matthew D. Gray,Pia Dosenovic,Alexander D. Gitlin,Natalia T. Freund,John Petersen,Colin Correnti,William A. Johnsen,Robert Kegel,Andrew B. Stuart,Jolene Glenn,Michael S. Seaman,William R. Schief,Roland K. Strong,Michel C. Nussenzweig,Leonidas Stamatatos,Leonidas Stamatatos +16 more
TL;DR: It is shown that an optimized Env immunogen can engage multiple glVRC01-class antibodies and activate naive B cells expressing the human germline heavy chain of 3BNC60, paired with endogenous mouse light chains in vivo.
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An Antibody Targeting the Fusion Machinery Neutralizes Dual-Tropic Infection and Defines a Site of Vulnerability on Epstein-Barr Virus.
Joost Snijder,Michael S. Ortego,Connor Weidle,Andrew B. Stuart,Matthew D. Gray,M. Juliana McElrath,M. Juliana McElrath,Marie Pancera,David Veesler,David Veesler,Andrew T. McGuire,Andrew T. McGuire +11 more
TL;DR: Structural analysis of the antibody‐gH/gL glycoprotein complex reveals a key site of EBV vulnerability that may pave the way for a next‐generation EBV vaccine.