2002
DOI: 10.1128/jvi.76.21.10894-10904.2002
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Structure-Based Analysis of the Herpes Simplex Virus Glycoprotein D Binding Site Present on Herpesvirus Entry Mediator HveA (HVEM)

Abstract: Binding of herpes simplex virus (HSV) envelope glycoprotein D (gD) to a cell surface receptor is an essential step of virus entry. We recently determined the crystal structure of gD bound to one receptor, HveA. HveA is a member of the tumor necrosis factor receptor family and contains four characteristic cysteine-rich domains (CRDs). The first two CRDs of HveA are necessary and sufficient for gD binding. The structure of the gD-HveA complex reveals that 17 amino acids in HveA CRD1 and 4 amino acids in HveA CRD… Show more

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Cited by 97 publications
(113 citation statements)
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“…These results are in agreement with crystal structure data pinpointing the binding site for HveA and demonstrate that HveA binding to the N-terminus of gD results in a conformational change that may be responsible for inducing virus envelope fusion with the cell surface. 59,60 Together, these studies suggest that HveA is recognized by a folded part of gD that can be affected by mutations spanning a substantial portion of the molecule.…”
Section: Virus Attachment and Entrymentioning
confidence: 89%
“…These results are in agreement with crystal structure data pinpointing the binding site for HveA and demonstrate that HveA binding to the N-terminus of gD results in a conformational change that may be responsible for inducing virus envelope fusion with the cell surface. 59,60 Together, these studies suggest that HveA is recognized by a folded part of gD that can be affected by mutations spanning a substantial portion of the molecule.…”
Section: Virus Attachment and Entrymentioning
confidence: 89%
“…At least some of the interactions of gD with its receptors have been mapped to the N terminus of gD, whereas the fusogenic determinant maps in the C-terminal portion of the ectodomain (residues 260-310). These residues (260-310) become actively engaged in membrane fusion after the interaction of the N-terminal domain with one of its cognate receptors (6)(7)(8)(10)(11)(12)(13)(14). gD also blocks apoptosis resulting from endocytosis of virus particles lacking gD.…”
mentioning
confidence: 99%
“…The four essential glycoproteins required for HSV entry are required and are also sufficient to induce fusion of cells that express a gD receptor (9). The gD-binding site on HVEM maps mainly to the N-terminal cysteine-rich domain 1, with a hot spot at Y23 (10,11). For nectin1, the N-terminal V domain, in particular its CCЈCЉ ridge (amino acids 64-104) is sufficient to mediate HSV entry (12)(13)(14)(15).…”
mentioning
confidence: 99%