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Analysis of plasminogen-binding M proteins of Streptococcus pyogenes.

Sjöbring, Ulf LU and Ringdahl, Ulrika LU (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)
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author
organization
publishing date
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
2013-10-09 15:50:55
date last changed
2016-11-20 04:31:45
@misc{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    = {ARRAY(0x9b948d8)},
  series       = {Methods},
  title        = {Analysis of plasminogen-binding M proteins of Streptococcus pyogenes.},
  volume       = {21},
  year         = {2000},
}