Two Epstein-Barr Virus Glycoprotein Complexes

2001 ◽  
pp. 51-64 ◽  
Author(s):  
L. M. Hutt-Fletcher ◽  
C. M. Lake
Keyword(s):  
Epstein Barr Virus ◽  
Virus Glycoprotein ◽  
Barr Virus ◽  
Epstein Barr

scholarly journals Epstein–Barr virus glycoprotein gM can interact with the cellular protein p32 and knockdown of p32 impairs virus

Virology ◽  
2016 ◽  
Vol 489 ◽  
pp. 223-232 ◽  
Author(s):  
Harish Changotra ◽  
Susan M. Turk ◽  
Antonio Artigues ◽  
Nagendra Thakur ◽  
Mindy Gore ◽  
...  
Keyword(s):  
Epstein Barr Virus ◽  
Cellular Protein ◽  
Virus Glycoprotein ◽  
Barr Virus ◽  
Epstein Barr

scholarly journals Epstein-Barr virus glycoprotein homologous to herpes simplex virus gB.

1987 ◽  
Vol 61 (2) ◽  
pp. 499-508 ◽  
Author(s):  
M Gong ◽  
T Ooka ◽  
T Matsuo ◽  
E Kieff
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Epstein Barr Virus ◽  
Virus Glycoprotein ◽  
Barr Virus ◽  
Epstein Barr ◽  
Simplex Virus

scholarly journals Molecular Basis of the Interaction between Complement Receptor Type 2 (CR2/CD21) and Epstein-Barr Virus Glycoprotein gp350

2008 ◽  
Vol 82 (22) ◽  
pp. 11217-11227 ◽  
Author(s):  
Kendra A. Young ◽  
Andrew P. Herbert ◽  
Paul N. Barlow ◽  
V. Michael Holers ◽  
Jonathan P. Hannan
Keyword(s):  
Epstein Barr Virus ◽  
Receptor Type ◽  
Complement Receptor ◽  
Wild Type ◽  
Virus Glycoprotein ◽  
Complement Receptor Type ◽  
Barr Virus ◽  
Epstein Barr ◽  
Mutant Forms

ABSTRACT The binding of the Epstein-Barr virus glycoprotein gp350 by complement receptor type 2 (CR2) is critical for viral attachment to B lymphocytes. We set out to test hypotheses regarding the molecular nature of this interaction by developing an enzyme-linked immunosorbent assay (ELISA) for the efficient analysis of the gp350-CR2 interaction by utilizing wild-type and mutant forms of recombinant gp350 and also of the CR2 N-terminal domains SCR1 and SCR2 (designated CR2 SCR1-2). To delineate the CR2-binding site on gp350, we generated 17 gp350 single-site substitutions targeting an area of gp350 that has been broadly implicated in the binding of both CR2 and the major inhibitory anti-gp350 monoclonal antibody (MAb) 72A1. These site-directed mutations identified a novel negatively charged CR2-binding surface described by residues Glu-21, Asp-22, Glu-155, Asp-208, Glu-210, and Asp-296. We also identified gp350 amino acid residues involved in non-charge-dependent interactions with CR2, including Tyr-151, Ile-160, and Trp-162. These data were supported by experiments in which phycoerythrin-conjugated wild-type and mutant forms of gp350 were incubated with CR2-expressing K562 cells and binding was assessed by flow cytometry. The ELISA was further utilized to identify several positively charged residues (Arg-13, Arg-28, Arg-36, Lys-41, Lys-57, Lys-67, Arg-83, and Arg-89) within SCR1-2 of CR2 that are involved in the binding interaction with gp350. These experiments allowed a comparison of those CR2 residues that are important for binding gp350 to those that define the epitope for an effective inhibitory anti-CR2 MAb, 171 (Asn-11, Arg-13, Ser-32, Thr-34, Arg-36, and Tyr-64). The mutagenesis data were used to calculate a model of the CR2-gp350 complex using the soft-docking program HADDOCK.

Salivary and serum IgA antibodies to the epstein-barr virus glycoprotein gp340: incidence and potential for virus neutralization

2007 ◽  
Vol 48 (1) ◽  
pp. 45-50 ◽  
Author(s):  
Q. Y. Yao ◽  
M. Rowe ◽  
A. J. Morgan ◽  
C. K. Sam ◽  
U. Prasad ◽  
...  
Keyword(s):  
Epstein Barr Virus ◽  
Virus Neutralization ◽  
Virus Glycoprotein ◽  
Barr Virus ◽  
Serum Iga ◽  
Iga Antibodies ◽  
Epstein Barr
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