Chimeric nectin1-poliovirus receptor molecules identify a nectin1 region functional in herpes simplex virus entry.
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Cellular localization of nectin-1 and glycoprotein D during herpes simplex virus infectionMutations 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.Structure of Herpes Simplex Virus Glycoprotein D Bound to the Human Receptor Nectin-1Prominent role of the Ig-like V domain in trans-interactions of nectins. Nectin3 and nectin 4 bind to the predicted C-C'-C"-D beta-strands of the nectin1 V domainNectin4/PRR4, a new afadin-associated member of the nectin family that trans-interacts with nectin1/PRR1 through V domain interactionDeletion of the second immunoglobulin-like domain of nectin-1 alters its intracellular processing and localization and ability to mediate entry of herpes simplex virusThe soluble ectodomain of herpes simplex virus gD contains a membrane-proximal pro-fusion domain and suffices to mediate virus entrySoluble V domain of Nectin-1/HveC enables entry of herpes simplex virus type 1 (HSV-1) into HSV-resistant cells by binding to viral glycoprotein DThe nectin-1alpha transmembrane domain, but not the cytoplasmic tail, influences cell fusion induced by HSV-1 glycoproteins.Amino acid substitutions in the V domain of nectin-1 (HveC) that impair entry activity for herpes simplex virus types 1 and 2 but not for Pseudorabies virus or bovine herpesvirus 1.Crystal structure of the V domain of human Nectin-like molecule-1/Syncam3/Tsll1/Igsf4b, a neural tissue-specific immunoglobulin-like cell-cell adhesion molecule.The domains of glycoprotein D required to block apoptosis induced by herpes simplex virus 1 are largely distinct from those involved in cell-cell fusion and binding to nectin1Effects of herpes simplex virus on structure and function of nectin-1/HveC.HIV-associated disruption of tight and adherens junctions of oral epithelial cells facilitates HSV-1 infection and spread.Herpesvirus entry: an updateSubstitution in the murine nectin1 receptor of a single conserved amino acid at a position distal from the herpes simplex virus gD binding site confers high-affinity binding to gD.Herpes simplex virus glycoprotein K, but not its syncytial allele, inhibits cell-cell fusion mediated by the four fusogenic glycoproteins, gD, gB, gH, and gL.Entry of herpes simplex virus mediated by chimeric forms of nectin1 retargeted to endosomes or to lipid rafts occurs through acidic endosomes.The herpes simplex virus JMP mutant enters receptor-negative J cells through a novel pathway independent of the known receptors nectin1, HveA, and nectin2.Implication of Soluble Forms of Cell Adhesion Molecules in Infectious Disease and Tumor: Insights from Transgenic Animal Models.
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P2860
Chimeric nectin1-poliovirus receptor molecules identify a nectin1 region functional in herpes simplex virus entry.
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
2001年论文
@zh
2001年论文
@zh-cn
name
Chimeric nectin1-poliovirus re ...... in herpes simplex virus entry.
@en
Chimeric nectin1-poliovirus re ...... in herpes simplex virus entry.
@nl
type
label
Chimeric nectin1-poliovirus re ...... in herpes simplex virus entry.
@en
Chimeric nectin1-poliovirus re ...... in herpes simplex virus entry.
@nl
prefLabel
Chimeric nectin1-poliovirus re ...... in herpes simplex virus entry.
@en
Chimeric nectin1-poliovirus re ...... in herpes simplex virus entry.
@nl
P2093
P2860
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Chimeric nectin1-poliovirus re ...... in herpes simplex virus entry.
@en
P2093
Campadelli Fiume G
Dubreuil P
P2860
P304
P356
10.1128/JVI.75.17.7987-7994.2001
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P577
2001-09-01T00:00:00Z