Partial nucleotide sequence of the Murray Valley encephalitis virus genome. Comparison of the encoded polypeptides with yellow fever virus structural and non-structural proteins

Lynn Dalgarno, Dennis W. Trent, James H. Strauss, Charles M. Rice

Research output: Contribution to journalArticle

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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.

Original languageEnglish (US)
Pages (from-to)309-323
Number of pages15
JournalJournal of Molecular Biology
Volume187
Issue number3
DOIs
StatePublished - Feb 5 1986

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Murray Valley encephalitis virus
Yellow fever virus
Genome
Coccidioidomycosis
Encephalitis
Yellow Fever
Peptides
Proteins
Amino Acid Sequence Homology
Viruses
Glycosylation
Virion
Amino Acid Sequence
Glycoproteins
Flavivirus
Polyproteins
Gene Order
Capsid Proteins
Open Reading Frames
Nucleotides

ASJC Scopus subject areas

  • Virology

Cite this

Partial nucleotide sequence of the Murray Valley encephalitis virus genome. Comparison of the encoded polypeptides with yellow fever virus structural and non-structural proteins. / Dalgarno, Lynn; Trent, Dennis W.; Strauss, James H.; Rice, Charles M.

In: Journal of Molecular Biology, Vol. 187, No. 3, 05.02.1986, p. 309-323.

Research output: Contribution to journalArticle

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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.",
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