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Partial nucleotide sequence of the Murray Valley encephalitis virus genome

Dalgarno, Lynn and Trent, Dennis W. and Strauss, James H. and Rice, Charles M. (1986) Partial nucleotide sequence of the Murray Valley encephalitis virus genome. Journal of Molecular Biology, 187 (3). pp. 309-323. ISSN 0022-2836. https://resolver.caltech.edu/CaltechAUTHORS:20160321-150517299

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Abstract

The sequence of 5400 bases corresponding to the 5'-terminal half of the Murray Valley encephalitis virus genome has been determined. The genome contains a 5' non-coding region of about 97 nucleotides, followed by a single continuous open reading frame that encodes the structural proteins followed by the non-structural proteins. Amino acid sequence homology between the Murray Valley encephalitis and yellow fever (Rice et al 1985) polyproteins is 42% over the region sequenced. The start points of the various Murray Valley encephalitis virus-coded proteins have been assigned on the basis of this homology and a consistent set of potential proteolytic cleavage sites identified, the sequences of which are similar in Murray Valley encephalitis and yellow fever. The deduced Murray Valley encephalitis gene order is 5'-C-prM (M)-E-NS1-ns2a-ns2b-NS3-3'. The genome organization of Murray Valley encephalitis and yellow fever appears to be identical and the sizes of the predicted virus-coded proteins similar between the two viruses. Both viruses encode a basic capsid protein followed by three glycoproteins: the glycoproteins appear to have the conventional topology of N terminus outside with a C-terminal membrane-spanning domain. There are conserved glycosylation sites in prM, the precursor to the M protein of the virion, and in NS1, a non-structural protein of uncertain function. The glycosylation sites in E, the major envelope protein of the virion, are not conserved as to position. We predict the existence, in flavivirus-infected cells, of two small, hydrophobic peptides, ns2a and ns2b, which show only limited amino acid sequence homology. Finally, about half of the amino acid sequence of NS3 has been obtained: NS3 is a hydrophilic non-structural protein that shows 55% amino acid sequence similarity between Murray Valley encephalitis and yellow fever over the region sequenced and is probably involved in RNA replication.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1016/0022-2836(86)90435-3DOIArticle
http://www.sciencedirect.com/science/article/pii/0022283686904353PublisherArticle
Additional Information:© 1986 Academic Press Inc. (London) Ltd. (Received 13 August 1985) We are grateful for helpful discussions with numerous colleagues, including C. Blair, G. Cleaves, F. Heinz, E. Strauss and G Wengler, many of whom furnished preprints of work prior to publication. E. M. Lenches furnished excellent technical assistance and the computer programs of T. Hunkapiller and the computing facility of L. Hood were of great value in producing the Figures. This work was supported in part by grants AI20612 and AI10793 from NIH and grant PCM83-16856 from NSF.
Funders:
Funding AgencyGrant Number
NIHAI20612
NIHAI10793
NSFPCM83-16856
Issue or Number:3
Record Number:CaltechAUTHORS:20160321-150517299
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20160321-150517299
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:65559
Collection:CaltechAUTHORS
Deposited By: Donna Wrublewski
Deposited On:22 Mar 2016 19:32
Last Modified:03 Oct 2019 09:48

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