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

Ringdahl, Ulrika LU ; Svensson, M ; Wistedt, AC ; Renné, T ; Keller, R ; Muller-Esterl, W and Sjöbring, Ulf LU (1998) In Journal of Biological Chemistry 273(11). p.6424-6430
Abstract
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... (More)
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. (Less)
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author
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organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
273
issue
11
pages
6424 - 6430
publisher
American Society for Biochemistry and Molecular Biology
external identifiers
  • scopus:0032513149
ISSN
1083-351X
language
English
LU publication?
yes
id
32619b37-50e8-437f-a810-58ed94456a24 (old id 1216574)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/9497374
http://www.jbc.org/content/273/11/6424.long
date added to LUP
2016-04-04 14:21:29
date last changed
2025-10-14 10:04:30
@article{32619b37-50e8-437f-a810-58ed94456a24,
  abstract     = {{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.}},
  author       = {{Ringdahl, Ulrika and Svensson, M and Wistedt, AC and Renné, T and Keller, R and Muller-Esterl, W and Sjöbring, Ulf}},
  issn         = {{1083-351X}},
  language     = {{eng}},
  number       = {{11}},
  pages        = {{6424--6430}},
  publisher    = {{American Society for Biochemistry and Molecular Biology}},
  series       = {{Journal of Biological Chemistry}},
  title        = {{Molecular co-operation between protein PAM and streptokinase for plasmin acquisition by Streptococcus pyogenes.}},
  url          = {{http://www.ncbi.nlm.nih.gov/pubmed/9497374}},
  volume       = {{273}},
  year         = {{1998}},
}