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MeSH Review:

Encephalitis Virus, Murray Valley

Lee, E. et al., Roehrig, J.T. et al., Winkler, G. et al., Lobigs, M., Stocks, C.E. et al., et al.

Blitvich, Scanlon, Shiell, Mackenzie, Pham, Hall,

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Disease relevance of Encephalitis Virus, Murray Valley

The Murray Valley encephalitis virus prM protein confers acid resistance to virus particles and alters the expression of epitopes within the R2 domain of E glycoprotein [1].
We have evaluated the antiviral effect of the sulfated polysaccharides, suramin, pentosan polysulfate (PPS) and PI-88, which are currently approved or in trial for clinical use, against dengue virus (DEN) and the encephalitic flaviviruses, Japanese encephalitis virus, West Nile virus, and Murray Valley encephalitis virus [2].
Immune response to a Murray Valley encephalitis virus epitope expressed in the flagellin of an attenuated strain of Salmonella [3].

High impact information on Encephalitis Virus, Murray Valley

In this study, the requirement for the proteolytic function of the viral proteinase NS3 for correct processing of a polyprotein segment encompassing the Murray Valley encephalitis virus structural proteins is shown [4].
In this study, we used cDNA of Murray Valley encephalitis virus (MVE) to examine features of the structural polyprotein which allow this regulation of a luminal cleavage by a cytoplasmic protease [5].
A synthetic peptide to the E glycoprotein of Murray Valley encephalitis virus defines multiple virus-reactive T- and B-cell epitopes [6].
In this study, we examined the intramolecular disulfide bond arrangement of NS1 of Murray Valley encephalitis virus and elucidated three of the six cysteine-pairing arrangements [7].
Protective immune responses to the E and NS1 proteins of Murray Valley encephalitis virus in hybrids of flavivirus-resistant mice [8].

Chemical compound and disease context of Encephalitis Virus, Murray Valley

Proteins specified by Murray Valley encephalitis virus were labelled during virus growth in Vero and in PS cells, and separated by polyacrylamide gel electrophoresis [9].
Endoglycosidase F digestion revealed the presence of a single asparagine-linked oligosaccharide side chain in TBE virus (Western and Far Eastern subtype), Louping III virus, Murray Valley encephalitis virus, and Rocio virus [10].
In contrast, the envelope glycoprotein of Murray Valley encephalitis virus (MVEV) did bind to concanavalin A under similar conditions and was readily labelled with radioactive mannose [11].

Biological context of Encephalitis Virus, Murray Valley

T-helper cell and associated antibody response to synthetic peptides of the E glycoprotein of Murray Valley encephalitis virus [12].

Gene context of Encephalitis Virus, Murray Valley

These results correlate with, and expand on, our previous observations based on a smaller set of synthetic peptides derived from the E-glycoprotein of Murray Valley encephalitis virus and suggest that synthetic peptides can function as E-glycoprotein Th-cell epitopes [13].

References

The Murray Valley encephalitis virus prM protein confers acid resistance to virus particles and alters the expression of epitopes within the R2 domain of E glycoprotein. Guirakhoo, F., Bolin, R.A., Roehrig, J.T. Virology (1992) [Pubmed]
Antiviral effect of the heparan sulfate mimetic, PI-88, against dengue and encephalitic flaviviruses. Lee, E., Pavy, M., Young, N., Freeman, C., Lobigs, M. Antiviral Res. (2006) [Pubmed]
Immune response to a Murray Valley encephalitis virus epitope expressed in the flagellin of an attenuated strain of Salmonella. Whittle, B.L., Lee, E., Weir, R.C., Verma, N.K. J. Med. Microbiol. (1997) [Pubmed]
Flavivirus premembrane protein cleavage and spike heterodimer secretion require the function of the viral proteinase NS3. Lobigs, M. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
Signal peptidase cleavage at the flavivirus C-prM junction: dependence on the viral NS2B-3 protease for efficient processing requires determinants in C, the signal peptide, and prM. Stocks, C.E., Lobigs, M. J. Virol. (1998) [Pubmed]
A synthetic peptide to the E glycoprotein of Murray Valley encephalitis virus defines multiple virus-reactive T- and B-cell epitopes. Mathews, J.H., Roehrig, J.T., Brubaker, J.R., Hunt, A.R., Allan, J.E. J. Virol. (1992) [Pubmed]
Determination of the intramolecular disulfide bond arrangement and biochemical identification of the glycosylation sites of the nonstructural protein NS1 of Murray Valley encephalitis virus. Blitvich, B.J., Scanlon, D., Shiell, B.J., Mackenzie, J.S., Pham, K., Hall, R.A. J. Gen. Virol. (2001) [Pubmed]
Protective immune responses to the E and NS1 proteins of Murray Valley encephalitis virus in hybrids of flavivirus-resistant mice. Hall, R.A., Brand, T.N., Lobigs, M., Sangster, M.Y., Howard, M.J., Mackenzie, J.S. J. Gen. Virol. (1996) [Pubmed]
The proteins of Murray Valley encephalitis virus. Westaway, E.G. J. Gen. Virol. (1975) [Pubmed]
Studies on the glycosylation of flavivirus E proteins and the role of carbohydrate in antigenic structure. Winkler, G., Heinz, F.X., Kunz, C. Virology (1987) [Pubmed]
Envelope protein of the flavivirus Kunjin is apparently not glycosylated. Wright, P.J. J. Gen. Virol. (1982) [Pubmed]
T-helper cell and associated antibody response to synthetic peptides of the E glycoprotein of Murray Valley encephalitis virus. Mathews, J.H., Allan, J.E., Roehrig, J.T., Brubaker, J.R., Uren, M.F., Hunt, A.R. J. Virol. (1991) [Pubmed]
T-helper cell epitopes on the E-glycoprotein of dengue 2 Jamaica virus. Roehrig, J.T., Risi, P.A., Brubaker, J.R., Hunt, A.R., Beaty, B.J., Trent, D.W., Mathews, J.H. Virology (1994) [Pubmed]

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