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Nonstructural proteins nsP3 and nsP4 of Ross River and O'Nyong-nyong viruses: Sequence and comparison with those of other alphaviruses

Strauss, Ellen G. and Levinson, Randy and Rice, Charles M. and Dalrymple, Joel and Strauss, James H. (1988) Nonstructural proteins nsP3 and nsP4 of Ross River and O'Nyong-nyong viruses: Sequence and comparison with those of other alphaviruses. Virology, 164 (1). pp. 265-274. ISSN 0042-6822. http://resolver.caltech.edu/CaltechAUTHORS:20160307-152610274

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Abstract

We have sequenced the nsP3 and nsP4 region of two alphaviruses, Ross River virus and O'Nyong-nyong virus, in order to examine these viruses for the presence or absence of an opal termination codon present between nsP3 and nsP4 in many alphaviruses. We found that Ross River virus possesses an in-phase opal termination codon between nsP3 and nsP4, whereas in O'Nyong-nyong virus this termination codon is replaced by an arginine codon. Previous studies have shown that two other alphaviruses, Sindbis virus and Middelburg virus, possess an opal termination codon separating nsP3 and nsP4 [E. G. Strauss, C. M. Rice, and J. H. Strauss (1983), Proc. Natl. Acad. Sci. USA 80, 5271-5275], whereas Semliki Forest virus possesses an arginine codon in lieu of the opal codon [K. Takkinen (1986), Nucleic Acids Res. 14, 5667-5682]. Thus, of the five alphaviruses examined to date, three possess the opal codon and two do not. Production of nsP4 requires readthrough of the opal codon in those alphaviruses that possess this termination codon and the function of the termination codon may be to regulate the amount of nsP4 produced. It is an open question then as to whether alphaviruses with no termination codon use other mechanisms to regulate the activity of this gene. The nsP4s of these five alphaviruses are highly conserved, sharing 71-76% amino acid sequence similarity, and all five contain the Gly-Asp-Asp motif found in many RNA virus replicases. The nsP3s are somewhat less conserved, sharing 52-73% amino acid sequence similarity throughout most of the protein, but each possesses a nonconserved C-terminal domain of 134 to 246 amino acids of unknown function.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1016/0042-6822(88)90644-7DOIArticle
http://www.sciencedirect.com/science/article/pii/0042682288906447PublisherArticle
Additional Information:© 1988 Academic Press, Inc. Received November 13, 1987; accepted January 15, 1988. Stimulating discussions with M. J. and S. Schlesinger and with L. Dalgarno contributed greatly to the development of this project. Computer programs written by T. Hunkapiller were used throughout this project and the computer facilities of L. Hood are gratefully acknowledged. E. Lenches provided expert technical assistance. This work was supported by Grants AI 20612 and AI 10793 from NIH, by Grant DMB-8316856 from NSF, and by a contract from the U.S. Army Medical Development Command. C.M.R. is a Pew Scholar in the Biomedical Sciences.
Funders:
Funding AgencyGrant Number
NIHAI 20612
NIHAI 10793
NSFDMB-8316856
Army Medical Development CommandUNSPECIFIED
Pew Charitable TrustUNSPECIFIED
Record Number:CaltechAUTHORS:20160307-152610274
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:20160307-152610274
Official Citation:Ellen G. Strauss, Randy Levinson, Charles M. Rice, Joel Dalrymple, James H. Strauss, Nonstructural proteins nsP3 and nsP4 of Ross River and O'Nyong-nyong viruses: Sequence and comparison with those of other alphaviruses, Virology, Volume 164, Issue 1, May 1988, Pages 265-274, ISSN 0042-6822, http://dx.doi.org/10.1016/0042-6822(88)90644-7. (http://www.sciencedirect.com/science/article/pii/0042682288906447)
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:65157
Collection:CaltechAUTHORS
Deposited By: Donna Wrublewski
Deposited On:08 Mar 2016 03:57
Last Modified:08 Mar 2016 03:57

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