کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
3424847 1227250 2011 10 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Investigation of the function of the putative self-association site of Epstein–Barr virus (EBV) glycoprotein 42 (gp42)
موضوعات مرتبط
علوم زیستی و بیوفناوری ایمنی شناسی و میکروب شناسی ویروس شناسی
پیش نمایش صفحه اول مقاله
Investigation of the function of the putative self-association site of Epstein–Barr virus (EBV) glycoprotein 42 (gp42)
چکیده انگلیسی

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.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Virology - Volume 415, Issue 2, 5 July 2011, Pages 122–131
نویسندگان
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