An avirulent G1 glycoprotein variant of La Crosse bunyavirus with defective fusion function.
AUTOR(ES)
Gonzalez-Scarano, F
RESUMO
La Crosse virus, a member of the California serogroup of the family Bunyaviridae, causes encephalitis in humans and laboratory rodents. A variant virus (V22) selected with a monoclonal antibody against the large (G1) glycoprotein showed diminished neuroinvasiveness after peripheral inoculation. This variant has an alteration in its fusion function, requiring a lower pH for the activation of fusion and demonstrating reduced efficiency of cell-to-cell fusion of BHK-21 cultures. V22 was studied in detail following the infection by intraperitoneal or intracerebral routes in suckling, weanling, or adult CD-1 mice. It exhibited a marked reduction in its ability to replicate in striated muscle and to produce viremia; however, after intracerebral injection V22 virus replicated almost as rapidly in brain as its parent, La Crosse virus. V22 virus thus represents an example of reduced neuroinvasiveness associated with an alteration at a specific epitope of the G1 glycoprotein. This same epitope also influences the fusion activity of the glycoprotein.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=254862Documentos Relacionados
- Neuroattenuation of an avirulent bunyavirus variant maps to the L RNA segment.
- Anti-mRNAs in La Crosse bunyavirus-infected cells.
- Mutants of Saccharomyces cerevisiae with defective vacuolar function.
- Human cytomegalovirus IE2 86-kilodalton protein binds p53 but does not abrogate G1 checkpoint function.
- Comparison of the sequences and coding of La Crosse and snowshoe hare bunyavirus S RNA species.