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Open AccessJournal ArticleDOI

Genetic mapping indicates that VP4 is the rotavirus cell attachment protein in vitro and in vivo.

TLDR
Income and binding assays indicate that gene 4 encodes the rotavirus protein which mediates attachment to cells in culture for both sialic acid-dependent and -independent strains, and VP4 appears to function as the cell attachment protein in vivo as well as in vitro.
Abstract
To identify the rotavirus protein which mediates attachment to cells in culture, viral reassortants between the simian rotavirus strain RRV and the murine strains EHP and EW or between the simian strain SA-11 and the human strain DS-1 were isolated. These parental strains differ in the requirement for sialic acid to bind and infect cells in culture. Infectivity and binding assays with the parental and reassortant rotaviruses indicate that gene 4 encodes the rotavirus protein which mediates attachment to cells in culture for both sialic acid-dependent and -independent strains. Using ligated intestinal segments of newborn mice and reassortants obtained between the murine strain EW and RRV, we developed an in vivo infectivity assay. In this system, the infectivity of EW was not affected by prior treatment of the enterocytes with neuraminidase, while neuraminidase treatment reduced the infectivity of a reassortant carrying gene 4 from RRV on an EW background more than 80% relative to the controls. Thus, VP4 appears to function as the cell attachment protein in vivo as well as in vitro.

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Citations
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Journal ArticleDOI

Uniformity of rotavirus strain nomenclature proposed by the Rotavirus Classification Working Group (RCWG).

TL;DR: With increasing numbers of complete RV genome sequences becoming available, a standardized RV strain nomenclature system is needed, and the RCWG proposes that individual RV strains are named as follows: RV group/species of origin/country of identification/common name/year of identification /G- and P-type.
Journal ArticleDOI

The rhesus rotavirus VP4 sialic acid binding domain has a galectin fold with a novel carbohydrate binding site

TL;DR: From the fit of the VP8* core into the virion spikes, it is proposed that VP4 arose from the insertion of a host carbohydrate binding domain into a viral membrane interaction protein.
Journal ArticleDOI

Rotavirus contains integrin ligand sequences and a disintegrin-like domain that are implicated in virus entry into cells.

TL;DR: It is shown that Rotavirus VP4 and VP7 contain tripeptide sequences previously shown to act as recognition sites for integrins in extracellular matrix proteins, which blocked rotavirus infection of cells shown to express alpha2beta1 and beta2integrins.
Journal ArticleDOI

Integrin alpha(v)beta(3) mediates rotavirus cell entry.

TL;DR: Findings implicate αvβ3 integrin as a cellular receptor common to neuraminidase-sensitive and neuraminidsase-resistant rotaviruses, and support the hypothesis that this integrin could determine, at least in part, the cellular susceptibility to rotavirus strains.
Book ChapterDOI

Rotavirus Proteins: Structure and Assembly

TL;DR: This review focuses on the current understanding of the structural basis of the molecular processes that govern the replication of rotavirus.
References
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Journal ArticleDOI

Serotypic Similarity and Diversity of Rotaviruses of Mammalian and Avian Origin as Studied by Plaque-Reduction Neutralization

TL;DR: A surprising observation that emerged from this study was the existence of a rotavirus (porcine strain SB-1A) bridging serotypes 4 and 5, which was identified in both humans and pigs.
Journal ArticleDOI

Human milk mucin inhibits rotavirus replication and prevents experimental gastroenteritis.

TL;DR: A macromolecular component of human milk is isolated that inhibits the replication of rotaviruses in tissue culture and prevents the development of gastroenteritis in an animal model system.
Journal ArticleDOI

Characterization of virus-like particles produced by the expression of rotavirus capsid proteins in insect cells.

TL;DR: The ability to express individual proteins or to coexpress different subsets of proteins provides a system with which to examine the interactions of the rotavirus structural proteins, the role of individual proteins in virus morphogenesis, and the feasibility of a subunit vaccine.
Journal ArticleDOI

Virus receptors: binding, adhesion strengthening, and changes in viral structure.

TL;DR: Virus receptors are one determinant of virus host range and tissue tropism and data indicating that binding is a multistep process are accumulating.
Journal ArticleDOI

Identification of the rotaviral gene that codes for hemagglutination and protease-enhanced plaque formation

TL;DR: Temperature-sensitive mutants of bovine rotavirus, UK Compton strain, and rhesus monkey rotav virus were used to derive 16 reassortants by coinfection of MA104 cells, indicating that these two rotaviral functions segregated independently.
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