Interactions between the two surface proteins of rotavirus may alter the receptor-binding specificity of the virus
about
The rhesus rotavirus VP4 sialic acid binding domain has a galectin fold with a novel carbohydrate binding site.Integrins alpha2beta1 and alpha4beta1 can mediate SA11 rotavirus attachment and entry into cells.The VP5 domain of VP4 can mediate attachment of rotaviruses to cells.Biochemical characterization of rotavirus receptors in MA104 cellsReassortment in vivo: driving force for diversity of human rotavirus strains isolated in the United Kingdom between 1995 and 1999.Initial interaction of rotavirus strains with N-acetylneuraminic (sialic) acid residues on the cell surface correlates with VP4 genotype, not species of origin.Specificity and affinity of sialic acid binding by the rhesus rotavirus VP8* coreStructures of rotavirus reassortants demonstrate correlation of altered conformation of the VP4 spike and expression of unexpected VP4-associated phenotypesInteraction of rotaviruses with Hsc70 during cell entry is mediated by VP5Diversity in Indian equine rotaviruses: identification of genotype G10,P6[1] and G1 strains and a new VP7 genotype (G16) strain in specimens from diarrheic foals in India.Functional and structural analysis of the sialic acid-binding domain of rotavirusesIntegrin-using rotaviruses bind alpha2beta1 integrin alpha2 I domain via VP4 DGE sequence and recognize alphaXbeta2 and alphaVbeta3 by using VP7 during cell entryRotaviruses induce an early membrane permeabilization of MA104 cells and do not require a low intracellular Ca2+ concentration to initiate their replication cycle.The spike protein VP4 defines the endocytic pathway used by rotavirus to enter MA104 cells.Endoplasmic reticulum chaperones are involved in the morphogenesis of rotavirus infectious particles.VP7 mediates the interaction of rotaviruses with integrin alphavbeta3 through a novel integrin-binding site.Rotaviruses reach late endosomes and require the cation-dependent mannose-6-phosphate receptor and the activity of cathepsin proteases to enter the cell.Trypsin cleavage stabilizes the rotavirus VP4 spike.Virus-like particle-induced fusion from without in tissue culture cells: role of outer-layer proteins VP4 and VP7.Characterization of neuraminidase-resistant mutants derived from rotavirus porcine strain OSU.
P2860
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P2860
Interactions between the two surface proteins of rotavirus may alter the receptor-binding specificity of the virus
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
1996年论文
@zh
1996年论文
@zh-cn
name
Interactions between the two s ...... nding specificity of the virus
@ast
Interactions between the two s ...... nding specificity of the virus
@en
type
label
Interactions between the two s ...... nding specificity of the virus
@ast
Interactions between the two s ...... nding specificity of the virus
@en
prefLabel
Interactions between the two s ...... nding specificity of the virus
@ast
Interactions between the two s ...... nding specificity of the virus
@en
P2093
P2860
P1433
P1476
Interactions between the two s ...... nding specificity of the virus
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P2093
P2860
P304
P407
P577
1996-02-01T00:00:00Z