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• W2068366518 endingPage "8140" @default.
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• W2068366518 abstract "Herpes simplex virus (HSV) entry into cells requires the binding of glycoprotein D (gD) to one of several cell surface receptors. The crystal structure of gD bound to one of these receptors, HveA/HVEM, reveals that the core of gD comprises an immunoglobulin fold flanked by a long C-terminal extension and an N-terminal hairpin loop. HveA is a member of the tumor necrosis factor receptor family and contains four cysteine-rich domains (CRDs) characteristic of this family. Fourteen amino acids within the gD N-terminal loop comprise the entire binding site for HveA. To determine the contribution of each gD contact residue to virus entry, we constructed gD molecules mutated in these amino acids. We determined the abilities of the gD mutants to bind receptors, facilitate virus entry, and mediate cell-cell fusion. Seven of the gD mutants exhibited wild-type levels of receptor binding and gD function. Results from the other seven gD mutants revealed three critical regions at the gD-HveA interface. (i) Several gD residues that participate in an intermolecular beta-sheet with HveA were found to be crucial for HveA binding and entry into HveA-expressing cells. (ii) Two gD residues that contact HveA-Y23 contributed to HveA binding but were not required for mediating entry into cells. HveA-Y23 fits into a crevice on the surface of gD and was previously shown to be essential for gD binding. (iii) CRD2 was previously shown to contribute to gD binding, and this study shows that one gD residue that contacts CRD2 contributes to HveA binding. None of the gD mutations prevented interaction with nectin-1, another gD receptor. However, when cotransfected with the other glycoproteins required for fusion, two gD mutants gained the ability to mediate fusion of cells expressing nectin-2, a gD receptor that interacts with several laboratory-derived gD mutants but not with wild-type gD. Thus, results from this panel of gD mutants as well as those of previous studies (A. Carfi, S. H. Willis, J. C. Whitbeck, C. Krummenacher, G. H. Cohen, R. J. Eisenberg, and D. C. Wiley, Mol. Cell 8:169-179, 2001, and S. A. Connolly, D. J. Landsburg, A. Carfi, D. C. Wiley, R. J. Eisenberg, and G. H. Cohen, J. Virol. 76:10894-10904, 2002) provide a detailed picture of the gD-HveA interface and the contacts required for functional interaction. The results demonstrate that of the 35 gD and HveA contact residues that comprise the gD-HveA interface, only a handful are critical for complex formation." @default.
• W2068366518 created "2016-06-24" @default.
• W2068366518 creator A5009243601 @default.
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• W2068366518 date "2003-07-15" @default.
• W2068366518 modified "2023-10-02" @default.
• W2068366518 title "Structure-Based Mutagenesis of Herpes Simplex Virus Glycoprotein D Defines Three Critical Regions at the gD-HveA/HVEM Binding Interface" @default.
• W2068366518 cites W1495740018 @default.
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• W2068366518 cites W1529453182 @default.
• W2068366518 cites W1542886234 @default.
• W2068366518 cites W1551760256 @default.
• W2068366518 cites W1552115305 @default.
• W2068366518 cites W1625079248 @default.
• W2068366518 cites W1695142101 @default.
• W2068366518 cites W1754237182 @default.
• W2068366518 cites W1844703465 @default.
• W2068366518 cites W1847479747 @default.
• W2068366518 cites W1851936098 @default.
• W2068366518 cites W1894845554 @default.
• W2068366518 cites W1919588248 @default.
• W2068366518 cites W1964638291 @default.
• W2068366518 cites W1976876715 @default.
• W2068366518 cites W1978117087 @default.
• W2068366518 cites W1978771262 @default.
• W2068366518 cites W1982277550 @default.
• W2068366518 cites W1984624532 @default.
• W2068366518 cites W1985090349 @default.
• W2068366518 cites W1988570956 @default.
• W2068366518 cites W1992512657 @default.
• W2068366518 cites W1995181927 @default.
• W2068366518 cites W1995459626 @default.
• W2068366518 cites W1997221411 @default.
• W2068366518 cites W1998185093 @default.
• W2068366518 cites W2008358775 @default.
• W2068366518 cites W2008486572 @default.
• W2068366518 cites W2015642465 @default.
• W2068366518 cites W2018961679 @default.
• W2068366518 cites W2022058386 @default.
• W2068366518 cites W2023653272 @default.
• W2068366518 cites W2025609599 @default.
• W2068366518 cites W2026370952 @default.
• W2068366518 cites W2027657241 @default.
• W2068366518 cites W2028807141 @default.
• W2068366518 cites W2042107416 @default.
• W2068366518 cites W2043074722 @default.
• W2068366518 cites W2044228301 @default.
• W2068366518 cites W2051710717 @default.
• W2068366518 cites W2054498103 @default.
• W2068366518 cites W2058527555 @default.
• W2068366518 cites W2084090660 @default.
• W2068366518 cites W2095038585 @default.
• W2068366518 cites W2096555292 @default.
• W2068366518 cites W2099806165 @default.
• W2068366518 cites W2100058611 @default.
• W2068366518 cites W2105258399 @default.
• W2068366518 cites W2109956845 @default.
• W2068366518 cites W2111646121 @default.
• W2068366518 cites W2120919816 @default.
• W2068366518 cites W2131243228 @default.
• W2068366518 cites W2140450674 @default.
• W2068366518 cites W2146341052 @default.
• W2068366518 cites W2148173142 @default.
• W2068366518 cites W2149818029 @default.
• W2068366518 cites W2161964161 @default.
• W2068366518 cites W2163314722 @default.
• W2068366518 cites W2163504590 @default.
• W2068366518 cites W2165910525 @default.
• W2068366518 cites W2165962324 @default.
• W2068366518 cites W2166413214 @default.
• W2068366518 cites W2168890635 @default.
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• W2068366518 doi "https://doi.org/10.1128/jvi.77.14.8127-8140.2003" @default.
• W2068366518 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/161942" @default.
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• W2068366518 hasPublicationYear "2003" @default.
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