The rhesus rotavirus outer capsid protein VP4 functions as a hemagglutinin and is antigenically conserved when expressed by a baculovirus recombinant.
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Rotavirus architecture at subnanometer resolutionpH-Induced Conformational Change of the Rotavirus VP4 Spike: Implications for Cell Entry and Antibody NeutralizationHumoral immune responses to VP4 and its cleavage products VP5* and VP8* in infants vaccinated with rhesus rotavirus.Attachment and growth of human rotaviruses RV-3 and S12/85 in Caco-2 cells depend on VP4.Integrins alpha2beta1 and alpha4beta1 can mediate SA11 rotavirus attachment and entry into cells.Proteolysis of monomeric recombinant rotavirus VP4 yields an oligomeric VP5* coreDevelopment, characterization, and diagnostic applications of monoclonal antibodies against bovine rotavirusSpecificity and affinity of sialic acid binding by the rhesus rotavirus VP8* coreAssembly of highly infectious rotavirus particles recoated with recombinant outer capsid proteins.Rotavirus vaccines: an overview.Mapping the hemagglutination domain of rotaviruses.Functional and structural analysis of the sialic acid-binding domain of rotavirusesIsolation and identification of group A rotaviruses among neonatal diarrheic calves, Morocco.Recombinant outer capsid glycoprotein (VP7) of rotavirus expressed in insect cells induces neutralizing antibodies in rabbits.Quantification of systemic and local immune responses to individual rotavirus proteins during rotavirus infection in mice.The nonstructural glycoprotein of rotavirus affects intracellular calcium levelsCharacterization of virus-like particles produced by the expression of rotavirus capsid proteins in insect cellsHuman rotavirus K8 strain represents a new VP4 serotype.Murine rotavirus genes encoding outer capsid proteins VP4 and VP7 are not major determinants of host range restriction and virulenceIdentification and baculovirus expression of the VP4 protein of the human group B rotavirus ADRV.Location of intrachain disulfide bonds in the VP5* and VP8* trypsin cleavage fragments of the rhesus rotavirus spike protein VP4.The amino-terminal half of rotavirus SA114fM VP4 protein contains a hemagglutination domain and primes for neutralizing antibodies to the virus.Antibodies to the trypsin cleavage peptide VP8 neutralize rotavirus by inhibiting binding of virions to target cells in culture.VP4-specific intestinal antibody response to rotavirus in a murine model of heterotypic infection.Expression of the OSU rotavirus outer capsid protein VP4 by an adenovirus recombinant.Rotavirus YM gene 4: analysis of its deduced amino acid sequence and prediction of the secondary structure of the VP4 protein.NS35 and not vp7 is the soluble rotavirus protein which binds to target cells.Immunization with baculovirus-expressed VP4 protein passively protects against simian and murine rotavirus challengeImmunization with baculovirus-expressed recombinant rotavirus proteins VP1, VP4, VP6, and VP7 induces CD8+ T lymphocytes that mediate clearance of chronic rotavirus infection in SCID mice.Rotavirus gene structure and function.α-enolase autoantibodies cross-reactive to viral proteins in a mouse model of biliary atresia.DNA amplification-restricted transcription-translation: rapid analysis of rhesus rotavirus neutralization sites.Rotavirus capsid protein VP5* permeabilizes membranes.Expression and functional characterization of bluetongue virus VP2 protein: role in cell entry.Effect of mutations in VP5 hydrophobic loops on rotavirus cell entryVirus-like particle-induced fusion from without in tissue culture cells: role of outer-layer proteins VP4 and VP7.Binding to sialic acids is not an essential step for the entry of animal rotaviruses to epithelial cells in culture.Expression of bovine herpesvirus 1 glycoprotein gIV by recombinant baculovirus and analysis of its immunogenic properties.Hemagglutination by a human rotavirus isolate as evidence for transmission of animal rotaviruses to humans.Discrete domains within the rotavirus VP5* direct peripheral membrane association and membrane permeability.
P2860
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P2860
The rhesus rotavirus outer capsid protein VP4 functions as a hemagglutinin and is antigenically conserved when expressed by a baculovirus recombinant.
description
1989 nî lūn-bûn
@nan
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
1989年论文
@zh
1989年论文
@zh-cn
name
The rhesus rotavirus outer cap ...... by a baculovirus recombinant.
@ast
The rhesus rotavirus outer cap ...... by a baculovirus recombinant.
@en
type
label
The rhesus rotavirus outer cap ...... by a baculovirus recombinant.
@ast
The rhesus rotavirus outer cap ...... by a baculovirus recombinant.
@en
prefLabel
The rhesus rotavirus outer cap ...... by a baculovirus recombinant.
@ast
The rhesus rotavirus outer cap ...... by a baculovirus recombinant.
@en
P2093
P2860
P1433
P1476
The rhesus rotavirus outer cap ...... d by a baculovirus recombinant
@en
P2093
E R Mackow
H B Greenberg
J W Barnett
P2860
P304
P407
P577
1989-04-01T00:00:00Z