Single amino acid substitutions in gD of herpes simplex virus 1 confer resistance to gD-mediated interference and cause cell-type-dependent alterations in infectivity.
about
Structural features of nectin-2 (HveB) required for herpes simplex virus entryCellular localization of nectin-1 and glycoprotein D during herpes simplex virus infectionDifferences in the N termini of herpes simplex virus type 1 and 2 gDs that influence functional interactions with the human entry receptor Nectin-2 and an entry receptor expressed in Chinese hamster ovary cellsMutations in the N-terminal domains of nectin-1 and nectin-2 reveal differences in requirements for entry of various alphaherpesviruses and for nectin-nectin interactions.The ectodomain of a novel member of the immunoglobulin subfamily related to the poliovirus receptor has the attributes of a bona fide receptor for herpes simplex virus types 1 and 2 in human cellsNectin2alpha (PRR2alpha or HveB) and nectin2delta are low-efficiency mediators for entry of herpes simplex virus mutants carrying the Leu25Pro substitution in glycoprotein DStructure-based analysis of the herpes simplex virus glycoprotein D binding site present on herpesvirus entry mediator HveA (HVEM).The V domain of herpesvirus Ig-like receptor (HIgR) contains a major functional region in herpes simplex virus-1 entry into cells and interacts physically with the viral glycoprotein DRoles for endocytosis and low pH in herpes simplex virus entry into HeLa and Chinese hamster ovary cellsStriking similarity of murine nectin-1alpha to human nectin-1alpha (HveC) in sequence and activity as a glycoprotein D receptor for alphaherpesvirus entry.Three-dimensional structure of herpes simplex virus type 1 glycoprotein D at 2.4-nanometer resolutionGlycoprotein D actively induces rapid internalization of two nectin-1 isoforms during herpes simplex virus entryMonoclonal antibodies to distinct sites on herpes simplex virus (HSV) glycoprotein D block HSV binding to HVEMHerpes simplex virus glycoprotein D can bind to poliovirus receptor-related protein 1 or herpesvirus entry mediator, two structurally unrelated mediators of virus entry.HveA (herpesvirus entry mediator A), a coreceptor for herpes simplex virus entry, also participates in virus-induced cell fusion.The first immunoglobulin-like domain of HveC is sufficient to bind herpes simplex virus gD with full affinity, while the third domain is involved in oligomerization of HveC.Herpes simplex virus with highly reduced gD levels can efficiently enter and spread between human keratinocytes.The pro-fusion domain of herpes simplex virus glycoprotein D (gD) interacts with the gD N terminus and is displaced by soluble forms of viral receptors.Anti-heparan sulfate peptides that block herpes simplex virus infection in vivo.Herpes simplex virus type 1 glycoprotein e is required for axonal localization of capsid, tegument, and membrane glycoproteins.Herpes simplex virus glycoprotein D interferes with binding of herpesvirus entry mediator to its ligands through downregulation and direct competitionStructure of unliganded HSV gD reveals a mechanism for receptor-mediated activation of virus entry.Effects of herpes simplex virus on structure and function of nectin-1/HveC.Structure-based mutagenesis of herpes simplex virus glycoprotein D defines three critical regions at the gD-HveA/HVEM binding interface.Function of herpes simplex virus type 1 gD mutants with different receptor-binding affinities in virus entry and fusionNectin-2-mediated entry of a syncytial strain of herpes simplex virus via pH-independent fusion with the plasma membrane of Chinese hamster ovary cells.Approaches to enhance the efficacy of DNA vaccines.The soluble amino-terminal region of HVEM mediates efficient herpes simplex virus type 1 infection of gD receptor-negative cells.Mutations in the N termini of herpes simplex virus type 1 and 2 gDs alter functional interactions with the entry/fusion receptors HVEM, nectin-2, and 3-O-sulfated heparan sulfate but not with nectin-1.Role of mannose-6-phosphate receptors in herpes simplex virus entry into cells and cell-to-cell transmission.Viral determinants of the variable sensitivity of herpes simplex virus strains to gD-mediated interferenceStructure-function analysis of soluble forms of herpes simplex virus glycoprotein D.Cross-linking of glycoprotein oligomers during herpes simplex virus type 1 entry.Antigenic structure of soluble herpes simplex virus (HSV) glycoprotein D correlates with inhibition of HSV infectionCharacterization of a BHK(TK-) cell clone resistant to postattachment entry by herpes simplex virus types 1 and 2Glycoprotein D of herpes simplex virus (HSV) binds directly to HVEM, a member of the tumor necrosis factor receptor superfamily and a mediator of HSV entryPartial resistance to gD-mediated interference conferred by mutations affecting herpes simplex virus type 1 gC and gK.HSV trafficking and development of gene therapy vectors with applications in the nervous system.Herpes simplex virus triggers activation of calcium-signaling pathwaysNectin-1-specific entry of herpes simplex virus 1 is sufficient for infection of the cornea and viral spread to the trigeminal ganglia
P2860
Q24291800-8BA795C4-DCFC-4E8A-B7B0-9156EB571003Q24311876-5DEB181F-C6A9-40E5-82F4-C252993165B1Q24315117-B528E889-B7D6-4200-B337-085C5686B97AQ24319105-8571A9FB-402E-4A87-A8C7-A79EAF1356A3Q24523691-C804F3E4-A764-4676-9802-D0060E43E72DQ24524264-152E5247-DE52-4B59-BF93-F38F11EC6E9BQ24538731-4E223C5D-86A3-42BC-8D9A-3444730D610DQ24658082-6BAB971D-8700-410D-A3FE-379CF5CBF16AQ24679497-36E4824A-E62F-44F2-AA26-3BE7C0ACF639Q28587515-E05F6A75-BA13-4DD9-8A9D-4C7AB834CB20Q33650502-474741DF-539B-4D37-A30D-9A72BCD58E5BQ33695839-DD08C242-5A9D-47AD-B552-7EBD22C7E39DQ33782593-A4B85BCD-0E98-46AA-8833-7DC8BE9C2993Q33783740-2EC52FE7-965C-4F8E-95C4-7C38B50ABBFBQ33785620-511A0609-A7FA-4045-8111-C110166193E1Q33819243-1B7838C1-A5DC-43BC-A540-28E43C122CB6Q33847925-D0F1F10B-EF2C-48BE-846E-C223E30A24E4Q33879094-6C6C3A59-0AEC-421A-86EA-612B0AEF2936Q33906507-7E026C8C-739C-4CA3-8C28-7B2E6BC9BDE6Q34092761-EFFDEDC7-DDAF-4FBF-941D-B6ACD31AB92DQ34295959-E000AFFD-10E4-4451-8B81-6A2FC2FD162CQ34324896-C5784B62-DF3E-4BEB-9B21-CDB9490FEC50Q34970789-46E0C7B2-99FE-4B22-BF4E-79C3269D86A9Q35105049-7A232DB6-1173-464D-B278-5E86D1CF517EQ35182202-0AC315DB-EEAA-484A-8C1A-DA70839923DCQ35605327-3A2B9287-4905-41F8-AED0-59F367D21E98Q35743279-4C9581F3-4860-419F-979C-54F61B19D3CEQ35774736-0EDC3A45-A5F3-445F-9F0D-8BC335B668A5Q35803200-7BC5618F-4B4A-4C31-9854-2E21D64BF74EQ35839774-A3F3FFDA-60D5-4118-8BC0-657E6B758795Q35845315-DFBF526C-AC72-4FC8-92C9-3CE671BC2B39Q35861628-B5B3601D-4DB5-4F3C-904C-4B48DCBDC8AEQ35868099-A86D0106-F515-46FC-A762-E6D760B1830EQ35880763-6DA68865-75A6-4672-94DE-B2C6626C3256Q35889603-2CB2C4A2-29D2-4CE2-882D-C2519C597C37Q35890209-C8253BE2-7DEC-408F-85C4-5045BFB36E72Q35896453-D9CFFB08-0300-463A-A449-C275FBB1EE31Q36134871-6E29E9DB-B1BC-488C-93EE-4B4A6328F5A7Q36324514-61528616-5050-4EFA-A32E-2E76675C0036Q36441418-17FDB999-AC82-48AF-B66A-CA53736EA100
P2860
Single amino acid substitutions in gD of herpes simplex virus 1 confer resistance to gD-mediated interference and cause cell-type-dependent alterations in infectivity.
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
1994年论文
@zh
1994年论文
@zh-cn
name
Single amino acid substitution ...... nt alterations in infectivity.
@en
type
label
Single amino acid substitution ...... nt alterations in infectivity.
@en
prefLabel
Single amino acid substitution ...... nt alterations in infectivity.
@en
P2093
P356
P1433
P1476
Single amino acid substitution ...... nt alterations in infectivity.
@en
P2093
P356
10.1006/VIRO.1994.1098
P407
P577
1994-02-01T00:00:00Z