Journal
VIROLOGY
Volume 393, Issue 1, Pages 151-159Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2009.07.025
Keywords
Epstein-Barr virus; BMRF-2; Protein; Humoral immune response; Antigenicity; Immunodominant epitope
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Funding
- National Institute of Health [R01 DE14894, R21 DE016009]
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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. (C) 2009 Elsevier Inc. All rights reserved.
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