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Molecular co-operation between protein PAM and streptokinase for plasmin acquisition by Streptococcus pyogenes.

På svenska

Author

  • Ulrika Ringdahl
  • M Svensson
  • AC Wistedt
  • T Renné
  • R Keller
  • W Muller-Esterl
  • Ulf Sjöbring

Summary, in English

Bacterial surface-associated plasmin formation is believed to contribute to invasion, although the underlying molecular mechanisms are poorly understood. To define the components necessary for plasmin generation on group A streptococci we used strain AP53 which exposes an M-like protein ("PAM") that contains a plasminogen-binding sequence with two 13-amino acid residues long tandem repeats (a1 and a2). Utilizing an Escherichia coli-streptococcal shuttle vector, we replaced a 29-residue long sequence segment of Arp4, an M-like protein that does not bind plasminogen, with a single (a1) or the combined a1a2 repeats of PAM. When expressed in E. coli, the purified chimeric Arp/PAM proteins both bound plasminogen, as well as plasmin, and when used to transform group A streptococcal strains lacking the plasminogen-binding ability, transformants with the Arp/PAM constructs efficiently bound plasminogen. Moreover, when grown in the presence of plasminogen, both Arp/PAM- and PAM-expressing streptococci acquired surface-bound plasmin. In contrast, plasminogen activation failed to occur on PAM- and Arp/PAM-expressing streptococci carrying an inactivated streptokinase gene: this block was overcome by exogenous streptokinase. Together, these results provide evidence for an unusual co-operation between a surface-bound protein, PAM, and a secreted protein, streptokinase, resulting in bacterial acquisition of a host protease that is likely to spur parasite invasion of host tissues.

Publishing year

1998

Language

English

Pages

6424-6430

Publication/Series

Journal of Biological Chemistry

Volume

273

Issue

11

Document type

Journal article

Publisher

American Society for Biochemistry and Molecular Biology

Topic

  • Microbiology in the medical area
  • Immunology in the medical area

Status

Published

ISBN/ISSN/Other

  • ISSN: 1083-351X