Abstract
The S1 genes of the three serotypes of reovirus have been cloned and sequenced. The S1 genes encode protein sigma 1, the protein against which serotype-specific neutralizing antibodies are directed; it is also the reovirus hemagglutinin and cell-attachment protein and is a major determinant of host range/tissue specificity and of the nature of the interaction of reovirus with cells of the immune system. The S1 genes of serotypes 1, 2, and 3 are 1458, 1442, and 1416 nucleotides long, respectively. They possess untranslated regions 13, 13, and 12 nucleotides long at their 5' termini and 188, 229, and 36 nucleotides long at their 3' termini. They possess two open reading frames. The first starts with a "weak" initiation codon and extends for 418, 399, and 455 codons, respectively; this is the size expected for the sigma 1 proteins. The other reading frame starts at a "strong" initiation codon about 70 residues downstream from the 5' terminus but extends for only about 120 codons, being terminated by 3 in-phase termination codons in all three genes. The proteins encoded by these short open reading frames are quite basic. The serotype 1 and 2 S1 genes are much more closely related to each other (28% homology) than to the serotype 3 S1 gene (5% and 9% homology, respectively). These figures are based on direct homology calculations, adjusted for 25% random coincidence. Serologic evidence and hydrophobicity profiles agree that the sigma 1 proteins of serotypes 1 and 2 are much more closely related to each other (about 40% homology) than to that of serotype 3 (only about 20% homology). The fact that the serotype 1 and 2 S1 genes are much more closely related to each other than to the serotype 3 S1 gene is remarkable since for all other nine reovirus genes the serotype 1 and 3 genes are much more closely related to each other than to the serotype 2 gene. Mechanisms that may effect this remarkable evolutionary pattern are discussed.
Full text
PDFSelected References
These references are in PubMed. This may not be the complete list of references from this article.
- Cashdollar L. W., Chmelo R., Esparza J., Hudson G. R., Joklik W. K. Molecular cloning of the complete genome of reovirus serotype 3. Virology. 1984 Feb;133(1):191–196. doi: 10.1016/0042-6822(84)90438-0. [DOI] [PubMed] [Google Scholar]
- Cashdollar L. W., Esparza J., Hudson G. R., Chmelo R., Lee P. W., Joklik W. K. Cloning the double-stranded RNA genes of reovirus: sequence of the cloned S2 gene. Proc Natl Acad Sci U S A. 1982 Dec;79(24):7644–7648. doi: 10.1073/pnas.79.24.7644. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Cenatiempo Y., Twardowski T., Shoeman R., Ernst H., Brot N., Weissbach H., Shatkin A. J. Two initiation sites detected in the small s1 species of reovirus mRNA by dipeptide synthesis in vitro. Proc Natl Acad Sci U S A. 1984 Feb;81(4):1084–1088. doi: 10.1073/pnas.81.4.1084. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Fontana A., Weiner H. L. Interaction of reovirus with cell surface receptors. II. Generation of suppressor T cells by the hemagglutinin of reovirus type 3. J Immunol. 1980 Dec;125(6):2660–2664. [PubMed] [Google Scholar]
- Gaillard R. K., Joklik W. K. The antigenic determinants of most of the proteins coded by the three serotypes of reovirus are highly conserved during evolution. Virology. 1980 Dec;107(2):533–536. doi: 10.1016/0042-6822(80)90321-9. [DOI] [PubMed] [Google Scholar]
- Gaillard R. K., Jr, Joklik W. K. Quantitation of the relatedness of reovirus serotypes 1, 2, and 3 at the gene level. Virology. 1982 Nov;123(1):152–164. doi: 10.1016/0042-6822(82)90302-6. [DOI] [PubMed] [Google Scholar]
- Hayes E. C., Lee P. W., Miller S. E., Joklik W. K. The interaction of a series of hybridoma IgGs with reovirus particles. Demonstration that the core protein lambda 2 is exposed on the particle surface. Virology. 1981 Jan 15;108(1):147–155. doi: 10.1016/0042-6822(81)90534-1. [DOI] [PubMed] [Google Scholar]
- Kauffman R. S., Lee S., Finberg R. Cytolytic T-cell mediated lysis of reovirus-infected cells: requirements for infectious virus, viral particles, and viral proteins in infected target cells. Virology. 1983 Dec;131(2):265–273. doi: 10.1016/0042-6822(83)90495-6. [DOI] [PubMed] [Google Scholar]
- Kozak M. Analysis of ribosome binding sites from the s1 message of reovirus. Initiation at the first and second AUG codons. J Mol Biol. 1982 Apr 25;156(4):807–820. doi: 10.1016/0022-2836(82)90143-7. [DOI] [PubMed] [Google Scholar]
- Kozak M. Possible role of flanking nucleotides in recognition of the AUG initiator codon by eukaryotic ribosomes. Nucleic Acids Res. 1981 Oct 24;9(20):5233–5252. doi: 10.1093/nar/9.20.5233. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
- Lee P. W., Hayes E. C., Joklik W. K. Protein sigma 1 is the reovirus cell attachment protein. Virology. 1981 Jan 15;108(1):156–163. doi: 10.1016/0042-6822(81)90535-3. [DOI] [PubMed] [Google Scholar]
- Messing J., Crea R., Seeburg P. H. A system for shotgun DNA sequencing. Nucleic Acids Res. 1981 Jan 24;9(2):309–321. doi: 10.1093/nar/9.2.309. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rose G. D., Roy S. Hydrophobic basis of packing in globular proteins. Proc Natl Acad Sci U S A. 1980 Aug;77(8):4643–4647. doi: 10.1073/pnas.77.8.4643. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sharpe A. H., Fields B. N. Reovirus inhibition of cellular DNA synthesis: role of the S1 gene. J Virol. 1981 Apr;38(1):389–392. doi: 10.1128/jvi.38.1.389-392.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Smith R. E., Zweerink H. J., Joklik W. K. Polypeptide components of virions, top component and cores of reovirus type 3. Virology. 1969 Dec;39(4):791–810. doi: 10.1016/0042-6822(69)90017-8. [DOI] [PubMed] [Google Scholar]
- Spriggs D. R., Kaye K., Fields B. N. Topological analysis of the reovirus type 3 hemagglutinin. Virology. 1983 May;127(1):220–224. doi: 10.1016/0042-6822(83)90385-9. [DOI] [PubMed] [Google Scholar]
- Weiner H. L., Drayna D., Averill D. R., Jr, Fields B. N. Molecular basis of reovirus virulence: role of the S1 gene. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5744–5748. doi: 10.1073/pnas.74.12.5744. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Weiner H. L., Fields B. N. Neutralization of reovirus: the gene responsible for the neutralization antigen. J Exp Med. 1977 Nov 1;146(5):1305–1310. doi: 10.1084/jem.146.5.1305. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Weiner H. L., Greene M. I., Fields B. N. Delayed hypersensitivity in mice infected with reovirus. I. Identification of host and viral gene products responsible for the immune response. J Immunol. 1980 Jul;125(1):278–282. [PubMed] [Google Scholar]
- Weiner H. L., Ramig R. F., Mustoe T. A., Fields B. N. Identification of the gene coding for the hemagglutinin of reovirus. Virology. 1978 May 15;86(2):581–584. doi: 10.1016/0042-6822(78)90099-5. [DOI] [PubMed] [Google Scholar]
- Zweerink H. J., Joklik W. K. Studies on the intracellular synthesis of reovirus-specified proteins. Virology. 1970 Jul;41(3):501–518. doi: 10.1016/0042-6822(70)90171-6. [DOI] [PubMed] [Google Scholar]
- Zweerink H. J., McDowell M. J., Joklik W. K. Essential and nonessential noncapsid reovirus proteins. Virology. 1971 Sep;45(3):716–723. doi: 10.1016/0042-6822(71)90185-1. [DOI] [PubMed] [Google Scholar]