Skip to main content
PMC home page
Journal of Virology logoLink to Journal of Virology
. 1989 Feb;63(2):600–606. doi: 10.1128/jvi.63.2.600-606.1989

Vaccinia virus encodes two proteins that are structurally related to members of the plasma serine protease inhibitor superfamily.

G J Kotwal 1, B Moss 1
PMCID: PMC247729  PMID: 2783466

Abstract

Nucleotide sequencing adjacent to the right inverted terminal repetition of the vaccinia virus genome revealed two genes encoding polypeptides that are structurally related to members of the plasma serine protease inhibitor superfamily (SPI). Inclusion in the superfamily is based on extensive amino acid sequence similarities as well as a consensus sequence adjacent to the active-site region near the carboxyl ends of the proteins. The genes designated SPI-1 and SPI-2 are located 10,000 and 17,000 base pairs from the right end of the genome, respectively. The predicted SPI-1 polypeptide is 11 amino acids longer than that of SPI-2, and the deduced masses are 40,471 and 38,125 daltons, respectively. Similarities between SPI-1 and SPI-2 are indicated by the percentage of identical amino acids (44%) and corresponding hydrophobicity plots. The maximum amino acid sequence diversity occurs precisely in the putative active-site region, suggesting that SPI-1 and SPI-2 may inhibit different proteases. SPI-2 is homologous to a previously described cowpox virus gene (D. J. Pickup, B. S. Ink, W. Hu, C. A. Ray, and W. K. Joklik, Proc. Natl. Acad. Sci. USA 83:7698-7702, 1986). Evidence for a cowpox virus homolog of SPI-1 was obtained by DNA hybridization. Thus, the presence of two genes that belong to the plasma serine protease inhibitor superfamily may be characteristic of orthopoxviruses.

Full text

PDF
600

Images in this article

602Image
on p.602
603Image
on p.603

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Baroudy B. M., Venkatesan S., Moss B. Incompletely base-paired flip-flop terminal loops link the two DNA strands of the vaccinia virus genome into one uninterrupted polynucleotide chain. Cell. 1982 Feb;28(2):315–324. doi: 10.1016/0092-8674(82)90349-x. [DOI] [PubMed] [Google Scholar]
  2. Birnboim H. C., Doly J. A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res. 1979 Nov 24;7(6):1513–1523. doi: 10.1093/nar/7.6.1513. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Buller R. M., Smith G. L., Cremer K., Notkins A. L., Moss B. Decreased virulence of recombinant vaccinia virus expression vectors is associated with a thymidine kinase-negative phenotype. 1985 Oct 31-Nov 6Nature. 317(6040):813–815. doi: 10.1038/317813a0. [DOI] [PubMed] [Google Scholar]
  4. Dallo S., Esteban M. Isolation and characterization of attenuated mutants of vaccinia virus. Virology. 1987 Aug;159(2):408–422. doi: 10.1016/0042-6822(87)90480-6. [DOI] [PubMed] [Google Scholar]
  5. DeFilippes F. M. Restriction enzyme mapping of vaccinia virus DNA. J Virol. 1982 Jul;43(1):136–149. doi: 10.1128/jvi.43.1.136-149.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Esposito J. J., Cabradilla C. D., Nakano J. H., Obijeski J. F. Intragenomic sequence transposition in monkeypox virus. Virology. 1981 Mar;109(2):231–243. doi: 10.1016/0042-6822(81)90495-5. [DOI] [PubMed] [Google Scholar]
  7. Garon C. F., Barbosa E., Moss B. Visualization of an inverted terminal repetition in vaccinia virus DNA. Proc Natl Acad Sci U S A. 1978 Oct;75(10):4863–4867. doi: 10.1073/pnas.75.10.4863. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Hattori M., Sakaki Y. Dideoxy sequencing method using denatured plasmid templates. Anal Biochem. 1986 Feb 1;152(2):232–238. doi: 10.1016/0003-2697(86)90403-3. [DOI] [PubMed] [Google Scholar]
  9. Hill R. E., Hastie N. D. Accelerated evolution in the reactive centre regions of serine protease inhibitors. Nature. 1987 Mar 5;326(6108):96–99. doi: 10.1038/326096a0. [DOI] [PubMed] [Google Scholar]
  10. Hill R. E., Shaw P. H., Boyd P. A., Baumann H., Hastie N. D. Plasma protease inhibitors in mouse and man: divergence within the reactive centre regions. Nature. 1984 Sep 13;311(5982):175–177. doi: 10.1038/311175a0. [DOI] [PubMed] [Google Scholar]
  11. Kotwal G. J., Moss B. Vaccinia virus encodes a secretory polypeptide structurally related to complement control proteins. Nature. 1988 Sep 8;335(6186):176–178. doi: 10.1038/335176a0. [DOI] [PubMed] [Google Scholar]
  12. Kyte J., Doolittle R. F. A simple method for displaying the hydropathic character of a protein. J Mol Biol. 1982 May 5;157(1):105–132. doi: 10.1016/0022-2836(82)90515-0. [DOI] [PubMed] [Google Scholar]
  13. Lipman D. J., Pearson W. R. Rapid and sensitive protein similarity searches. Science. 1985 Mar 22;227(4693):1435–1441. doi: 10.1126/science.2983426. [DOI] [PubMed] [Google Scholar]
  14. Maxam A. M., Gilbert W. Sequencing end-labeled DNA with base-specific chemical cleavages. Methods Enzymol. 1980;65(1):499–560. doi: 10.1016/s0076-6879(80)65059-9. [DOI] [PubMed] [Google Scholar]
  15. Moss B., Winters E., Cooper J. A. Deletion of a 9,000-base-pair segment of the vaccinia virus genome that encodes nonessential polypeptides. J Virol. 1981 Nov;40(2):387–395. doi: 10.1128/jvi.40.2.387-395.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Moss B., Winters E., Cooper N. Instability and reiteration of DNA sequences within the vaccinia virus genome. Proc Natl Acad Sci U S A. 1981 Mar;78(3):1614–1618. doi: 10.1073/pnas.78.3.1614. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Moyer R. W., Graves R. L., Rothe C. T. The white pock (mu) mutants of rabbit poxvirus. III. Terminal DNA sequence duplication and transposition in rabbit poxvirus. Cell. 1980 Nov;22(2 Pt 2):545–553. doi: 10.1016/0092-8674(80)90364-5. [DOI] [PubMed] [Google Scholar]
  18. Moyer R. W., Rothe C. T. The white pock mutants of rabbit poxvirus. I. Spontaneous host range mutants contain deletions. Virology. 1980 Apr 15;102(1):119–132. doi: 10.1016/0042-6822(80)90075-6. [DOI] [PubMed] [Google Scholar]
  19. Panicali D., Davis S. W., Mercer S. R., Paoletti E. Two major DNA variants present in serially propagated stocks of the WR strain of vaccinia virus. J Virol. 1981 Mar;37(3):1000–1010. doi: 10.1128/jvi.37.3.1000-1010.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Pickup D. J., Bastia D., Stone H. O., Joklik W. K. Sequence of terminal regions of cowpox virus DNA: arrangement of repeated and unique sequence elements. Proc Natl Acad Sci U S A. 1982 Dec;79(23):7112–7116. doi: 10.1073/pnas.79.23.7112. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Pickup D. J., Ink B. S., Hu W., Ray C. A., Joklik W. K. Hemorrhage in lesions caused by cowpox virus is induced by a viral protein that is related to plasma protein inhibitors of serine proteases. Proc Natl Acad Sci U S A. 1986 Oct;83(20):7698–7702. doi: 10.1073/pnas.83.20.7698. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Pickup D. J., Ink B. S., Parsons B. L., Hu W., Joklik W. K. Spontaneous deletions and duplications of sequences in the genome of cowpox virus. Proc Natl Acad Sci U S A. 1984 Nov;81(21):6817–6821. doi: 10.1073/pnas.81.21.6817. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Sanger F., Coulson A. R., Barrell B. G., Smith A. J., Roe B. A. Cloning in single-stranded bacteriophage as an aid to rapid DNA sequencing. J Mol Biol. 1980 Oct 25;143(2):161–178. doi: 10.1016/0022-2836(80)90196-5. [DOI] [PubMed] [Google Scholar]
  24. Schmitt J. F., Stunnenberg H. G. Sequence and transcriptional analysis of the vaccinia virus HindIII I fragment. J Virol. 1988 Jun;62(6):1889–1897. doi: 10.1128/jvi.62.6.1889-1897.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Southern E. M. Detection of specific sequences among DNA fragments separated by gel electrophoresis. J Mol Biol. 1975 Nov 5;98(3):503–517. doi: 10.1016/s0022-2836(75)80083-0. [DOI] [PubMed] [Google Scholar]
  26. Staden R. Computer methods to locate signals in nucleic acid sequences. Nucleic Acids Res. 1984 Jan 11;12(1 Pt 2):505–519. doi: 10.1093/nar/12.1part2.505. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Weir J. P., Moss B. Nucleotide sequence of the vaccinia virus thymidine kinase gene and the nature of spontaneous frameshift mutations. J Virol. 1983 May;46(2):530–537. doi: 10.1128/jvi.46.2.530-537.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Wieslander L. A simple method to recover intact high molecular weight RNA and DNA after electrophoretic separation in low gelling temperature agarose gels. Anal Biochem. 1979 Oct 1;98(2):305–309. doi: 10.1016/0003-2697(79)90145-3. [DOI] [PubMed] [Google Scholar]
  29. Wittek R., Menna A., Müller H. K., Schümperli D., Boseley P. G., Wyler R. Inverted terminal repeats in rabbit poxvirus and vaccinia virus DNA. J Virol. 1978 Oct;28(1):171–181. doi: 10.1128/jvi.28.1.171-181.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Wittek R., Moss B. Tandem repeats within the inverted terminal repetition of vaccinia virus DNA. Cell. 1980 Aug;21(1):277–284. doi: 10.1016/0092-8674(80)90135-x. [DOI] [PubMed] [Google Scholar]
  31. Wittek R., Müller H. K., Wyler R. Length heterogeneity in the DNA of vaccinia virus is eliminated on cloning the virus. FEBS Lett. 1978 Jun 1;90(1):41–46. doi: 10.1016/0014-5793(78)80293-2. [DOI] [PubMed] [Google Scholar]
  32. Yuen L., Moss B. Oligonucleotide sequence signaling transcriptional termination of vaccinia virus early genes. Proc Natl Acad Sci U S A. 1987 Sep;84(18):6417–6421. doi: 10.1073/pnas.84.18.6417. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Journal of Virology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES