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Virology. 2011 Jul 5;415(2):122-31. doi: 10.1016/j.virol.2011.04.003. Epub 2011 May 8.

Investigation of the function of the putative self-association site of Epstein-Barr virus (EBV) glycoprotein 42 (gp42).

Author information

1
Department of Microbiology and Immunology, The Feinberg School of Medicine, Northwestern University, Chicago, IL 60611, USA. c-rowe@northwestern.edu

Abstract

The Epstein-Barr virus (EBV) glycoprotein 42 (gp42) is a type II membrane protein essential for entry into B cells but inhibits entry into epithelial cells. X-ray crystallography suggests that gp42 may form dimers when bound to human leukocyte antigen (HLA) class II receptor (Mullen et al., 2002) or multimerize when not bound to HLA class II (Kirschner et al., 2009). We investigated this self-association of gp42 using several different approaches. We generated soluble mutants of gp42 containing mutations within the self-association site and found that these mutants have a defect in fusion. The gp42 mutants bound to gH/gL and HLA class II, but were unable to bind wild-type gp42 or a cleavage mutant of gp42. Using purified gp42, gH/gL, and HLA, we found these proteins associate 1:1:1 by gel filtration suggesting that gp42 dimerization or multimerization does not occur or is a transient event undetectable by our methods.

PMID:
21550622
PMCID:
PMC3107886
DOI:
10.1016/j.virol.2011.04.003
[Indexed for MEDLINE]
Free PMC Article

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