Document Detail

Epstein-Barr virus infection of polarized epithelial cells via the basolateral surface by memory B cell-mediated transfer infection.
MedLine Citation:
PMID:  21573183     Owner:  NLM     Status:  MEDLINE    
Epstein Barr virus (EBV) exhibits a distinct tropism for both B cells and epithelial cells. The virus persists as a latent infection of memory B cells in healthy individuals, but a role for infection of normal epithelial is also likely. Infection of B cells is initiated by the interaction of the major EBV glycoprotein gp350 with CD21 on the B cell surface. Fusion is triggered by the interaction of the EBV glycoprotein, gp42 with HLA class II, and is thereafter mediated by the core fusion complex, gH/gL/gp42. In contrast, direct infection of CD21-negative epithelial cells is inefficient, but efficient infection can be achieved by a process called transfer infection. In this study, we characterise the molecular interactions involved in the three stages of transfer infection of epithelial cells: (i) CD21-mediated co-capping of EBV and integrins on B cells, and activation of the adhesion molecules, (ii) conjugate formation between EBV-loaded B cells and epithelial cells via the capped adhesion molecules, and (iii) interaction of EBV glycoproteins with epithelial cells, with subsequent fusion and uptake of virions. Infection of epithelial cells required the EBV gH and gL glycoproteins, but not gp42. Using an in vitro model of normal polarized epithelia, we demonstrated that polarization of the EBV receptor(s) and adhesion molecules restricted transfer infection to the basolateral surface. Furthermore, the adhesions between EBV-loaded B cells and the basolateral surface of epithelial cells included CD11b on the B cell interacting with heparan sulphate moieties of CD44v3 and LEEP-CAM on epithelial cells. Consequently, transfer infection was efficiently mediated via CD11b-positive memory B cells but not by CD11b-negative naïve B cells. Together, these findings have important implications for understanding the mechanisms of EBV infection of normal and pre-malignant epithelial cells in vivo.
Claire Shannon-Lowe; Martin Rowe
Related Documents :
18025553 - Cell immobilization and xylitol production using sugarcane bagasse as raw material.
1367053 - Serum-free medium for fermentor cultures of hybridomas.
447503 - Disseminated endocrine cells of the gastrointestinal tract and their possible influence...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2011-05-05
Journal Detail:
Title:  PLoS pathogens     Volume:  7     ISSN:  1553-7374     ISO Abbreviation:  PLoS Pathog.     Publication Date:  2011 May 
Date Detail:
Created Date:  2011-05-16     Completed Date:  2011-09-08     Revised Date:  2013-06-28    
Medline Journal Info:
Nlm Unique ID:  101238921     Medline TA:  PLoS Pathog     Country:  United States    
Other Details:
Languages:  eng     Pagination:  e1001338     Citation Subset:  IM    
Cancer Research UK Birmingham Cancer Centre, School of Cancer Sciences, College of Medical and Dental Sciences, The University of Birmingham, Birmingham, United Kingdom.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
B-Lymphocytes / cytology*,  virology*
Cell Adhesion
Cell Adhesion Molecules / immunology
Cell Line
Cell Polarity
Epithelial Cells / cytology,  immunology,  virology*
Epstein-Barr Virus Infections / immunology*
Herpesvirus 4, Human / metabolism*,  pathogenicity
Receptors, Complement 3d / immunology,  metabolism
Viral Matrix Proteins / genetics,  metabolism
Virion / metabolism
Virus Internalization*
Grant Support
//Cancer Research UK
Reg. No./Substance:
0/Cell Adhesion Molecules; 0/EBV-associated membrane antigen, Epstein-Barr virus; 0/Receptors, Complement 3d; 0/Viral Matrix Proteins

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Interleukin-13 promotes susceptibility to chlamydial infection of the respiratory and genital tracts...
Next Document:  A functional nuclear epidermal growth factor receptor, SRC and Stat3 heteromeric complex in pancreat...