期刊
VIROLOGY
卷 385, 期 2, 页码 368-382出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2008.12.019
关键词
Poxvirus; Vaccinia; Entry; Attachment; L1; A28; Receptor-binding
类别
资金
- National Institutes of Health [R21-Al-53404, A148487]
- NIAID Mid-Atlantic Regional Center of Excellence [U54 A1057168]
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 nonessential 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. (c) 2008 Elsevier Inc. All rights reserved.
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