Epstein-Barr virus infection mechanisms

被引：20

作者：

Chesnokova, Liudmila S.

Hutt-Fletcher, Lindsey M. ^{[1
,2
]}

机构：

[1] Louisiana State Univ, Hlth Sci Ctr, Ctr Mol Tumor Virol, Dept Microbiol & Immunol, Shreveport, LA 71130 USA

[2] Louisiana State Univ, Hlth Sci Ctr, Feist Weiller Canc Ctr, Shreveport, LA 71130 USA

来源：

CHINESE JOURNAL OF CANCER | 2014年 / 33卷 / 11期

关键词：

Glycoproteins; complement receptor type 2; HLA class II; integrins; entry; ORAL EPITHELIAL-CELLS; B-CELLS; HERPESVIRUS ENTRY; CONFORMATIONAL-CHANGE; GLYCOPROTEINS GHGL; CRYSTAL-STRUCTURE; MEMBRANE-FUSION; BINDING; GH/GL; COMPLEX;

D O I：

10.5732/cjc.014.10168

中图分类号：

R73 [肿瘤学];

学科分类号：

100214 ;

摘要：

Epstein-Barr virus (EBV) infection occurs by distinct mechanisms across different cell types. EBV infection of B cells in vitro minimally requires 5 viral glycoproteins and 2 cellular proteins. By contrast, infection of epithelial cells requires a minimum of 3 viral glycoproteins, which are capable of interacting with one or more of 3 different cellular proteins. The full complement of proteins involved in entry into all cell types capable of being infected in vivo is unknown. This review discusses the events that occur when the virus is delivered into the cytoplasm of a cell, the players known to be involved in these events, and the ways in which these players are thought to function.

引用

页码：545 / 548

页数：4

共 37 条

[1] Hydrophobic residues that form putative fusion loops of Epstein-Barr virus glycoprotein B are critical for fusion activity [J].

Backovic, Marija ;

Jardetzky, Theodore S. ;

Longnecker, Richard .

JOURNAL OF VIROLOGY, 2007, 81 (17) :9596-9600

[2] Structure of a core fragment of glycoprotein H from pseudorabies virus in complex with antibody [J].

Backovic, Marija ;

DuBois, Rebecca M. ;

Cockburn, Joseph J. ;

Sharff, Andrew J. ;

Vaney, Marie-Christine ;

Granzow, Harald ;

Klupp, Barbara G. ;

Bricogne, Gerard ;

Mettenleiter, Thomas C. ;

Rey, Felix A. .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2010, 107 (52) :22635-22640

[3] Structure of a trimeric variant of the Epstein-Barr virus glycoprotein B [J].

Backovic, Marija ;

Longnecker, Richard ;

Jardetzky, Theodore S. .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2009, 106 (08) :2880-2885

[4] Epstein-Barr virus recombinant lacking expression of glycoprotein gp150 infects B cells normally but is enhanced for infection of epithelial cells [J].

Borza, CM ;

Hutt-Fletcher, LM .

JOURNAL OF VIROLOGY, 1998, 72 (09) :7577-7582

[5] Use of gHgL for attachment of Epstein-Barr virus to epithelial cells compromises infection [J].

Borza, CM ;

Morgan, AJ ;

Turk, SM ;

Hutt-Fletcher, LM .

JOURNAL OF VIROLOGY, 2004, 78 (10) :5007-5014

[6] Alternate replication in B cells and epithelial cells switches tropism of Epstein-Barr virus [J].

Borza, CM ;

Hutt-Fletcher, LM .

NATURE MEDICINE, 2002, 8 (06) :594-599

[7] The Large Groove Found in the gH/gL Structure Is an Important Functional Domain for Epstein-Barr Virus Fusion [J].

Chen, Jia ;

Jardetzky, Theodore S. ;

Longnecker, Richard .

JOURNAL OF VIROLOGY, 2013, 87 (07) :3620-3627

[8] The KGD Motif of Epstein-Barr Virus gH/gL Is Bifunctional, Orchestrating Infection of B Cells and Epithelial Cells [J].

Chen, Jia ;

Rowe, Cynthia L. ;

Jardetzky, Theodore S. ;

Longnecker, Richard .

MBIO, 2012, 3 (01) :1-9

[9] Epstein-Barr Virus Glycoprotein gB and gHgL Can Mediate Fusion and Entry in trans, and Heat Can Act as a Partial Surrogate for gHgL and Trigger a Conformational Change in gB [J].

Chesnokova, Liudmila S. ;

Ahuja, Munish K. ;

Hutt-Fletcher, Lindsey M. .

JOURNAL OF VIROLOGY, 2014, 88 (21) :12193-12201

[10] Fusion of Epstein-Barr Virus with Epithelial Cells Can Be Triggered by αvβ5 in Addition to αvβ6 and αvβ8, and Integrin Binding Triggers a Conformational Change in Glycoproteins gHgL [J].

Chesnokova, Liudmila S. ;

Hutt-Fletcher, Lindsey M. .

JOURNAL OF VIROLOGY, 2011, 85 (24) :13214-13223

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