Analysis of plasminogen-binding M proteins of Streptococcus pyogenes.
(2000) In Methods 21(2). p.143-150- Abstract
- Group A streptococci are common human pathogens that cause a variety of infections. They express M proteins which are important cell wall-bound type-specific virulence factors. We have found that a set of strains, associated primarily with skin infections, express M proteins that bind plasminogen and plasmin with high affinity. The binding is mediated by a 13-amino-acid internal repeated sequence located in the N-terminal surface-exposed portion of these M proteins. This sequence binds to kringle 2 in plasminogen, a domain that is not involved in the interaction with streptokinase, a potent group A streptococcal activator of plasminogen. It could be demonstrated that plasminogen, absorbed from plasma by growing group A streptococci... (More)
- Group A streptococci are common human pathogens that cause a variety of infections. They express M proteins which are important cell wall-bound type-specific virulence factors. We have found that a set of strains, associated primarily with skin infections, express M proteins that bind plasminogen and plasmin with high affinity. The binding is mediated by a 13-amino-acid internal repeated sequence located in the N-terminal surface-exposed portion of these M proteins. This sequence binds to kringle 2 in plasminogen, a domain that is not involved in the interaction with streptokinase, a potent group A streptococcal activator of plasminogen. It could be demonstrated that plasminogen, absorbed from plasma by growing group A streptococci expressing the plasminogen-binding M proteins, could be activated by exogenous and endogenous streptokinase, thereby providing the bacteria with a surface-associated enzyme that could act on the tissue barriers in the infected host. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1216538
- author
- Sjöbring, Ulf LU and Ringdahl, Ulrika LU
- organization
- publishing date
- 2000
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Methods
- volume
- 21
- issue
- 2
- pages
- 143 - 150
- publisher
- Elsevier
- external identifiers
-
- scopus:0034431160
- ISSN
- 1095-9130
- language
- English
- LU publication?
- yes
- id
- 78a70406-7f70-4b1d-872e-52880728632b (old id 1216538)
- alternative location
- http://www.ncbi.nlm.nih.gov/pubmed/10816375
- http://www.sciencedirect.com/science/article/pii/S104620230090985X
- date added to LUP
- 2016-04-04 14:31:43
- date last changed
- 2022-01-30 02:11:46
@article{78a70406-7f70-4b1d-872e-52880728632b, abstract = {{Group A streptococci are common human pathogens that cause a variety of infections. They express M proteins which are important cell wall-bound type-specific virulence factors. We have found that a set of strains, associated primarily with skin infections, express M proteins that bind plasminogen and plasmin with high affinity. The binding is mediated by a 13-amino-acid internal repeated sequence located in the N-terminal surface-exposed portion of these M proteins. This sequence binds to kringle 2 in plasminogen, a domain that is not involved in the interaction with streptokinase, a potent group A streptococcal activator of plasminogen. It could be demonstrated that plasminogen, absorbed from plasma by growing group A streptococci expressing the plasminogen-binding M proteins, could be activated by exogenous and endogenous streptokinase, thereby providing the bacteria with a surface-associated enzyme that could act on the tissue barriers in the infected host.}}, author = {{Sjöbring, Ulf and Ringdahl, Ulrika}}, issn = {{1095-9130}}, language = {{eng}}, number = {{2}}, pages = {{143--150}}, publisher = {{Elsevier}}, series = {{Methods}}, title = {{Analysis of plasminogen-binding M proteins of Streptococcus pyogenes.}}, url = {{http://www.ncbi.nlm.nih.gov/pubmed/10816375}}, volume = {{21}}, year = {{2000}}, }