Molecular co-operation between protein PAM and streptokinase for plasmin acquisition by Streptococcus pyogenes.
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1216574
- author
- Ringdahl, Ulrika LU ; Svensson, M ; Wistedt, AC ; Renné, T ; Keller, R ; Muller-Esterl, W and Sjöbring, Ulf LU
- organization
- publishing date
- 1998
- 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
- 2022-01-30 01:50:21
@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}}, }