期刊
VIROLOGY
卷 344, 期 1, 页码 17-24出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2005.09.016
关键词
herpes simplex virus; HSV; entry; cell fusion; receptors; HVEM; nectin-1; gD
类别
资金
- NCI NIH HHS [R01 CA021776] Funding Source: Medline
- NIAID NIH HHS [R37 AI036293, U19 AI031494, T32 AI07476] Funding Source: Medline
- NIAMS NIH HHS [T32 AR07593] Funding Source: Medline
One of the herpes simplex virus envelope glycoproteins, designated gD, is the principal determinant of cell recognition for viral entry. Other viral glycoproteins, gB, gH and gL, cooperate with gD to mediate the membrane fusion that is required for viral entry and cell fusion. Membrane fusion is triggered by the binding of gD to one of its receptors. These receptors belong to three different classes of cell surface molecules. This review summarizes recent findings on the structure and function of gD. The results presented indicate that gD may assume more than one conformation, one in the absence of receptor, another when gD is bound to the herpesvirus entry mediator, a member of the TNF receptor family, and a third when gD is bound to nectin-1, a cell adhesion molecule in the immunoglobulin superfamily. Finally, information and ideas are presented about a membrane-proximal region of gD that is required for membrane fusion, but not for receptor binding, and that may have a role in activating the fusogenic activity of gB, gH and gL. (c) 2005 Elsevier Inc. All rights reserved.
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