Skip to main content
PMC home page
Infection and Immunity logoLink to Infection and Immunity
. 1993 Aug;61(8):3318–3326. doi: 10.1128/iai.61.8.3318-3326.1993

Repeats in an extracellular protein of weakly pathogenic strains of Streptococcus suis type 2 are absent in pathogenic strains.

H E Smith 1, F H Reek 1, U Vecht 1, A L Gielkens 1, M A Smits 1
PMCID: PMC281006  PMID: 8335363

Abstract

Streptococcus suis type 2 strains that are pathogenic for pigs produce a 110-kDa extracellular protein factor (EF). Nonpathogenic and weakly pathogenic strains do not produce EF or produce a protein (EF*) that is immunologically related to EF. To study the pathogenesis of S. suis type 2 in pigs and to develop tools and methods for the control of S. suis type 2 infections, we cloned and characterized the genes encoding EF and various EF* proteins. Analysis of the deduced amino acid sequences showed that the first 833 amino acids at the N terminus of the EF and EF* proteins were nearly identical. The proteins differed, however, at their C termini. Unlike the 110-kDa EF protein, the EF* proteins contained several repeated units of 76 amino acids. The number and arrangement of the repeats in the EF* proteins varied. The data suggest that the gene encoding EF could have evolved from an epf* gene by a specific deletion event. The lack of repeated amino acid units in the EF protein may be related to virulence.

Full text

PDF
3318

Images in this article

3319Image
on p.3319
3322Image
on p.3322

Selected References

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

  1. Arends J. P., Zanen H. C. Meningitis caused by Streptococcus suis in humans. Rev Infect Dis. 1988 Jan-Feb;10(1):131–137. doi: 10.1093/clinids/10.1.131. [DOI] [PubMed] [Google Scholar]
  2. Bron S., Holsappel S., Venema G., Peeters B. P. Plasmid deletion formation between short direct repeats in Bacillus subtilis is stimulated by single-stranded rolling-circle replication intermediates. Mol Gen Genet. 1991 Apr;226(1-2):88–96. doi: 10.1007/BF00273591. [DOI] [PubMed] [Google Scholar]
  3. Burton Z., Burgess R. R., Lin J., Moore D., Holder S., Gross C. A. The nucleotide sequence of the cloned rpoD gene for the RNA polymerase sigma subunit from E coli K12. Nucleic Acids Res. 1981 Jun 25;9(12):2889–2903. doi: 10.1093/nar/9.12.2889. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Clifton-Hadley F. A. Streptococcus suis type 2 infections. Br Vet J. 1983 Jan-Feb;139(1):1–5. doi: 10.1016/s0007-1935(17)30581-x. [DOI] [PubMed] [Google Scholar]
  5. Fahnestock S. R., Alexander P., Nagle J., Filpula D. Gene for an immunoglobulin-binding protein from a group G streptococcus. J Bacteriol. 1986 Sep;167(3):870–880. doi: 10.1128/jb.167.3.870-880.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Gill D. R., Salmond G. P. The identification of the Escherichia coli ftsY gene product: an unusual protein. Mol Microbiol. 1990 Apr;4(4):575–583. doi: 10.1111/j.1365-2958.1990.tb00626.x. [DOI] [PubMed] [Google Scholar]
  7. Hollingshead S. K., Fischetti V. A., Scott J. R. Complete nucleotide sequence of type 6 M protein of the group A Streptococcus. Repetitive structure and membrane anchor. J Biol Chem. 1986 Feb 5;261(4):1677–1686. [PubMed] [Google Scholar]
  8. Hollingshead S. K., Fischetti V. A., Scott J. R. Size variation in group A streptococcal M protein is generated by homologous recombination between intragenic repeats. Mol Gen Genet. 1987 May;207(2-3):196–203. doi: 10.1007/BF00331578. [DOI] [PubMed] [Google Scholar]
  9. Jones K. F., Hollingshead S. K., Scott J. R., Fischetti V. A. Spontaneous M6 protein size mutants of group A streptococci display variation in antigenic and opsonogenic epitopes. Proc Natl Acad Sci U S A. 1988 Nov;85(21):8271–8275. doi: 10.1073/pnas.85.21.8271. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Konings R. N., Verhoeven E. J., Peeters B. P. pKUN, vectors for the separate production of both DNA strands of recombinant plasmids. Methods Enzymol. 1987;153:12–34. doi: 10.1016/0076-6879(87)53045-2. [DOI] [PubMed] [Google Scholar]
  11. 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]
  12. Murray N. E., Brammar W. J., Murray K. Lambdoid phages that simplify the recovery of in vitro recombinants. Mol Gen Genet. 1977 Jan 7;150(1):53–61. doi: 10.1007/BF02425325. [DOI] [PubMed] [Google Scholar]
  13. Peeters B. P., de Boer J. H., Bron S., Venema G. Structural plasmid instability in Bacillus subtilis: effect of direct and inverted repeats. Mol Gen Genet. 1988 Jun;212(3):450–458. doi: 10.1007/BF00330849. [DOI] [PubMed] [Google Scholar]
  14. Platt T. Transcription termination and the regulation of gene expression. Annu Rev Biochem. 1986;55:339–372. doi: 10.1146/annurev.bi.55.070186.002011. [DOI] [PubMed] [Google Scholar]
  15. 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]
  16. Signäs C., Raucci G., Jönsson K., Lindgren P. E., Anantharamaiah G. M., Hök M., Lindberg M. Nucleotide sequence of the gene for a fibronectin-binding protein from Staphylococcus aureus: use of this peptide sequence in the synthesis of biologically active peptides. Proc Natl Acad Sci U S A. 1989 Jan;86(2):699–703. doi: 10.1073/pnas.86.2.699. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Smith H. E., Vecht U., Gielkens A. L., Smits M. A. Cloning and nucleotide sequence of the gene encoding the 136-kilodalton surface protein (muramidase-released protein) of Streptococcus suis type 2. Infect Immun. 1992 Jun;60(6):2361–2367. doi: 10.1128/iai.60.6.2361-2367.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Tinoco I., Jr, Borer P. N., Dengler B., Levin M. D., Uhlenbeck O. C., Crothers D. M., Bralla J. Improved estimation of secondary structure in ribonucleic acids. Nat New Biol. 1973 Nov 14;246(150):40–41. doi: 10.1038/newbio246040a0. [DOI] [PubMed] [Google Scholar]
  19. Vecht U., Arends J. P., van der Molen E. J., van Leengoed L. A. Differences in virulence between two strains of Streptococcus suis type II after experimentally induced infection of newborn germ-free pigs. Am J Vet Res. 1989 Jul;50(7):1037–1043. [PubMed] [Google Scholar]
  20. Vecht U., Wisselink H. J., Jellema M. L., Smith H. E. Identification of two proteins associated with virulence of Streptococcus suis type 2. Infect Immun. 1991 Sep;59(9):3156–3162. doi: 10.1128/iai.59.9.3156-3162.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Vecht U., Wisselink H. J., van Dijk J. E., Smith H. E. Virulence of Streptococcus suis type 2 strains in newborn germfree pigs depends on phenotype. Infect Immun. 1992 Feb;60(2):550–556. doi: 10.1128/iai.60.2.550-556.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Vecht U., van Leengoed L. A., Verheijen E. R. Streptococcus suis infections in pigs in the Netherlands (Part I). Vet Q. 1985 Oct;7(4):315–321. doi: 10.1080/01652176.1985.9694005. [DOI] [PubMed] [Google Scholar]
  23. Welch R. A. Pore-forming cytolysins of gram-negative bacteria. Mol Microbiol. 1991 Mar;5(3):521–528. doi: 10.1111/j.1365-2958.1991.tb00723.x. [DOI] [PubMed] [Google Scholar]
  24. Wren B. W. A family of clostridial and streptococcal ligand-binding proteins with conserved C-terminal repeat sequences. Mol Microbiol. 1991 Apr;5(4):797–803. doi: 10.1111/j.1365-2958.1991.tb00752.x. [DOI] [PubMed] [Google Scholar]
  25. von Heijne G. A new method for predicting signal sequence cleavage sites. Nucleic Acids Res. 1986 Jun 11;14(11):4683–4690. doi: 10.1093/nar/14.11.4683. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Infection and Immunity are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES