EBV-positive human sera contain antibodies against the EBV BMRF-2 protein.
We previously showed that the EBV glycoprotein BMRF-2 contains a functional integrin-binding Arg-Gly-Asp (RGD) domain that plays an important role in viral infection and cell-to-cell spread of progeny virions in oral epithelial cells. In this study, we found that EBV-seropositive human sera contain antibodies against BMRF-2. The inhibitory effect of EBV-positive sera on EBV infection of oral epithelial cells was substantially reduced by pre-incubation of serum samples with the BMRF-2 RGD peptide, suggesting that anti-BMRF-2 human antibodies possess neutralizing activity. EBV-specific sera reacted strongly with the BMRF-2 extracellular domain (170-213 aa) containing the RGD motif, whereas they reacted only weakly or not at all with a mutated form of the BMRF-2 extracellular domain containing AAA instead of RGD. These data indicate that RGD motif of BMRF-2 is part of an immunodominant antigenic determinant within the extracellular domain of BMRF-2 that may contribute to EBV neutralization during EBV reactivation.
Xiao
Jianqiao
J
Department of Medicine, University of California, San Francisco, CA 94143-0654, USA.
Palefsky
Joel M
JM
Herrera
Rossana
R
Sunshine
Carl
C
Tugizov
Sharof M
SM
D000914:Antibodies, Viral / Q000097:blood* / Q000276:immunology*; D000956:Antigens, Viral / Q000276:immunology*; D004847:Epithelial Cells / Q000821:virology; D020031:Epstein-Barr Virus Infections / Q000276:immunology*; D006801:Humans; D008562:Membrane Glycoproteins / Q000276:immunology*; D009500:Neutralization Tests; D014764:Viral Proteins / Q000276:immunology*
D000914:Antibodies, Viral; D000956:Antigens, Viral; C109482:BMRF-2 protein, Human herpesvirus 4; D008562:Membrane Glycoproteins; D014764:Viral Proteins
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