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Vaccinia virus L1 binds to cell surfaces and blocks virus entry independently of glycosaminoglycans

Authors :
Foo, Chwan Hong
Lou, Huan
Whitbeck, J. Charles
Ponce-de-León, Manuel
Atanasiu, Doina
Eisenberg, Roselyn J.
Cohen, Gary H.
Source :
Virology. Mar2009, Vol. 385 Issue 2, p368-382. 15p.
Publication Year :
2009

Abstract

Abstract: L1 and A28 are vaccinia virus (VACV) envelope proteins which are essential for cellular entry. However, their specific roles during entry are unknown. We tested whether one or both of these proteins might serve as receptor binding proteins (RBP). We found that a soluble, truncated form of L1, but not A28, bound to cell surfaces independently of glycosaminoglycans (GAGs). Hence, VACV A28 is not likely to be a RBP and functions after attachment during entry. Importantly, soluble L1 inhibited both binding and entry of VACV in GAG-deficient cells, suggesting that soluble L1 blocks entry at the binding step by competing with the virions for non-GAG receptors on cells. In contrast, soluble A27, a VACV protein which attaches to GAGs but is non-essential for virus entry, inhibited binding and entry of VACV in a GAG-dependent manner. To our knowledge, this is the first report of a VACV envelope protein that blocks virus binding and entry independently of GAGs. [Copyright &y& Elsevier]

Details

Language :
English
ISSN :
00426822
Volume :
385
Issue :
2
Database :
Academic Search Index
Journal :
Virology
Publication Type :
Academic Journal
Accession number :
36681762
Full Text :
https://doi.org/10.1016/j.virol.2008.12.019