Structural basis for Epstein–Barr virus host cell tropism mediated by gp42 and gHgL entry glycoproteins

Karthik Sathiyamoorthy; Yao Xiong Hu; Britta S. Möhl; Jia Chen; Richard Longnecker; Theodore S. Jardetzky

doi:10.1038/ncomms13557

Nature Communications (Dec 2016)

Structural basis for Epstein–Barr virus host cell tropism mediated by gp42 and gHgL entry glycoproteins

Karthik Sathiyamoorthy,
Yao Xiong Hu,
Britta S. Möhl,
Jia Chen,
Richard Longnecker,
Theodore S. Jardetzky

Affiliations

Karthik Sathiyamoorthy: Department of Structural Biology, Stanford University School of Medicine
Yao Xiong Hu: Department of Structural Biology, Stanford University School of Medicine
Britta S. Möhl: Department of Microbiology and Immunology, Feinberg School of Medicine, Northwestern University
Jia Chen: Department of Microbiology and Immunology, Feinberg School of Medicine, Northwestern University
Richard Longnecker: Department of Microbiology and Immunology, Feinberg School of Medicine, Northwestern University
Theodore S. Jardetzky: Department of Structural Biology, Stanford University School of Medicine

DOI: https://doi.org/10.1038/ncomms13557
Journal volume & issue: Vol. 7, no. 1
pp. 1 – 14

Abstract

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The entry of herpesviruses (such as Epstein-Barr virus) into host cells is mediated by a multitude of glycoproteins. Here, the authors show the structure of a viral glycoprotein complex, gHgL/gp42, bound to an anti-gHgL antibody, clarifying determinants of EBV host cell tropism.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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