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. 1996 Sep;178(17):5327–5329. doi: 10.1128/jb.178.17.5327-5329.1996

Insertional inactivation of the gene for collagen-binding protein has a pleiotropic effect on the phenotype of Staphylococcus aureus.

S A Hienz 1, M Palma 1, J I Flock 1
PMCID: PMC178336  PMID: 8752357

Abstract

This report describes phenotypical changes caused by the insertional inactivation of the gene for the collagen-binding protein in Staphylococcus aureus PH100. Insertional inactivation resulted in reductions in the amount of fibronectin-binding protein in PH100 and the ability of intact cells to aggregate in the presence of fibronectin. However, the capacity of PH100 to adhere to immobilized fibronectin remained the same.

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Selected References

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  1. Cheung A. L., Koomey J. M., Butler C. A., Projan S. J., Fischetti V. A. Regulation of exoprotein expression in Staphylococcus aureus by a locus (sar) distinct from agr. Proc Natl Acad Sci U S A. 1992 Jul 15;89(14):6462–6466. doi: 10.1073/pnas.89.14.6462. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Cheung A. L., Wolz C., Yeaman M. R., Bayer A. S. Insertional inactivation of a chromosomal locus that modulates expression of potential virulence determinants in Staphylococcus aureus. J Bacteriol. 1995 Jun;177(11):3220–3226. doi: 10.1128/jb.177.11.3220-3226.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Cheung A. L., Yeaman M. R., Sullam P. M., Witt M. D., Bayer A. S. Role of the sar locus of Staphylococcus aureus in induction of endocarditis in rabbits. Infect Immun. 1994 May;62(5):1719–1725. doi: 10.1128/iai.62.5.1719-1725.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Flock J. I., Fröman G., Jönsson K., Guss B., Signäs C., Nilsson B., Raucci G., Hök M., Wadström T., Lindberg M. Cloning and expression of the gene for a fibronectin-binding protein from Staphylococcus aureus. EMBO J. 1987 Aug;6(8):2351–2357. doi: 10.1002/j.1460-2075.1987.tb02511.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Flock J. I., Hienz S. A., Heimdahl A., Schennings T. Reconsideration of the role of fibronectin binding in endocarditis caused by Staphylococcus aureus. Infect Immun. 1996 May;64(5):1876–1878. doi: 10.1128/iai.64.5.1876-1878.1996. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Fröman G., Switalski L. M., Speziale P., Hök M. Isolation and characterization of a fibronectin receptor from Staphylococcus aureus. J Biol Chem. 1987 May 15;262(14):6564–6571. [PubMed] [Google Scholar]
  7. Harrington D. J., Russell R. R. Multiple changes in cell wall antigens of isogenic mutants of Streptococcus mutans. J Bacteriol. 1993 Sep;175(18):5925–5933. doi: 10.1128/jb.175.18.5925-5933.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Jenkinson H. F., Easingwood R. A. Insertional inactivation of the gene encoding a 76-kilodalton cell surface polypeptide in Streptococcus gordonii Challis has a pleiotropic effect on cell surface composition and properties. Infect Immun. 1990 Nov;58(11):3689–3697. doi: 10.1128/iai.58.11.3689-3697.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. 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]
  10. Liang O. D., Ascencio F., Fransson L. A., Wadström T. Binding of heparan sulfate to Staphylococcus aureus. Infect Immun. 1992 Mar;60(3):899–906. doi: 10.1128/iai.60.3.899-906.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Markwell M. A. A new solid-state reagent to iodinate proteins. I. Conditions for the efficient labeling of antiserum. Anal Biochem. 1982 Sep 15;125(2):427–432. doi: 10.1016/0003-2697(82)90025-2. [DOI] [PubMed] [Google Scholar]
  12. McGavin M. H., Krajewska-Pietrasik D., Rydén C., Hök M. Identification of a Staphylococcus aureus extracellular matrix-binding protein with broad specificity. Infect Immun. 1993 Jun;61(6):2479–2485. doi: 10.1128/iai.61.6.2479-2485.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Navarre W. W., Schneewind O. Proteolytic cleavage and cell wall anchoring at the LPXTG motif of surface proteins in gram-positive bacteria. Mol Microbiol. 1994 Oct;14(1):115–121. doi: 10.1111/j.1365-2958.1994.tb01271.x. [DOI] [PubMed] [Google Scholar]
  14. Patti J. M., Boles J. O., Hök M. Identification and biochemical characterization of the ligand binding domain of the collagen adhesin from Staphylococcus aureus. Biochemistry. 1993 Oct 26;32(42):11428–11435. doi: 10.1021/bi00093a021. [DOI] [PubMed] [Google Scholar]
  15. Patti J. M., Bremell T., Krajewska-Pietrasik D., Abdelnour A., Tarkowski A., Rydén C., Hök M. The Staphylococcus aureus collagen adhesin is a virulence determinant in experimental septic arthritis. Infect Immun. 1994 Jan;62(1):152–161. doi: 10.1128/iai.62.1.152-161.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Patti J. M., Jonsson H., Guss B., Switalski L. M., Wiberg K., Lindberg M., Hök M. Molecular characterization and expression of a gene encoding a Staphylococcus aureus collagen adhesin. J Biol Chem. 1992 Mar 5;267(7):4766–4772. [PubMed] [Google Scholar]
  17. Schneewind O., Fowler A., Faull K. F. Structure of the cell wall anchor of surface proteins in Staphylococcus aureus. Science. 1995 Apr 7;268(5207):103–106. doi: 10.1126/science.7701329. [DOI] [PubMed] [Google Scholar]
  18. Smeltzer M. S., Hart M. E., Iandolo J. J. Phenotypic characterization of xpr, a global regulator of extracellular virulence factors in Staphylococcus aureus. Infect Immun. 1993 Mar;61(3):919–925. doi: 10.1128/iai.61.3.919-925.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]

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