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Streptokinase activates plasminogen bound to human group C and G streptococci through M-like proteins.

Ben Nasr, A; Wistedt, A; Ringdahl, Ulrika LU and Sjöbring, Ulf LU (1994) In European Journal of Biochemistry 222(2). p.267-276
Abstract
An ability to interact with plasminogen or plasmin could provide micro-organisms with a mechanism for invasion. Thus, group A, C and G streptococci secrete streptokinase which binds and activates plasminogen. Some streptococci also express surface structures which bind plasminogen without causing its activation. Plasminogen-binding surface proteins were extracted from one group C and one group G streptococcal isolate. Both proteins were found to bind plasmin, fibrinogen and serum albumin in addition to plasminogen. Gene fragments encoding the streptococcal proteins were amplified by PCR and were subsequently cloned and expressed in Escherichia coli. DNA sequence determination revealed for both genes open reading frames encoding proteins... (More)
An ability to interact with plasminogen or plasmin could provide micro-organisms with a mechanism for invasion. Thus, group A, C and G streptococci secrete streptokinase which binds and activates plasminogen. Some streptococci also express surface structures which bind plasminogen without causing its activation. Plasminogen-binding surface proteins were extracted from one group C and one group G streptococcal isolate. Both proteins were found to bind plasmin, fibrinogen and serum albumin in addition to plasminogen. Gene fragments encoding the streptococcal proteins were amplified by PCR and were subsequently cloned and expressed in Escherichia coli. DNA sequence determination revealed for both genes open reading frames encoding proteins which contained repetitive domains and a carboxyl-terminal unrepeated region that were typical of M and M-like proteins. Though the amino-terminal regions of the group C and G streptococcal proteins demonstrated a rather high overall similarity between themselves, they were not similar to the variable regions of other M-like proteins with one exception: there was a 46% identity between the first 22 amino acids of the group G streptococcal protein and the corresponding sequence of PAM, the plasminogen-binding M-like protein of type M53 group A streptococci. Like the proteins extracted from the streptococci, the recombinant proteins bound plasminogen, fibrinogen and albumin. The three plasma proteins bound to separate sites on the streptococcal M-like proteins. Plasminogen bound by the group C and G streptococcal proteins was readily activated by streptokinase, providing evidence for a functional link between the secreted plasminogen-activator and proteins exposed on the bacterial surface. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
European Journal of Biochemistry
volume
222
issue
2
pages
267 - 276
publisher
Wiley-Blackwell
external identifiers
  • Scopus:0028360283
ISSN
0014-2956
language
English
LU publication?
yes
id
3ff84f2f-6d00-4ea4-93a6-c4143ac1f165 (old id 1216606)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/8020466
http://onlinelibrary.wiley.com/doi/10.1111/j.1432-1033.1994.tb18865.x/abstract
date added to LUP
2013-10-09 15:37:09
date last changed
2016-10-13 04:54:23
@misc{3ff84f2f-6d00-4ea4-93a6-c4143ac1f165,
  abstract     = {An ability to interact with plasminogen or plasmin could provide micro-organisms with a mechanism for invasion. Thus, group A, C and G streptococci secrete streptokinase which binds and activates plasminogen. Some streptococci also express surface structures which bind plasminogen without causing its activation. Plasminogen-binding surface proteins were extracted from one group C and one group G streptococcal isolate. Both proteins were found to bind plasmin, fibrinogen and serum albumin in addition to plasminogen. Gene fragments encoding the streptococcal proteins were amplified by PCR and were subsequently cloned and expressed in Escherichia coli. DNA sequence determination revealed for both genes open reading frames encoding proteins which contained repetitive domains and a carboxyl-terminal unrepeated region that were typical of M and M-like proteins. Though the amino-terminal regions of the group C and G streptococcal proteins demonstrated a rather high overall similarity between themselves, they were not similar to the variable regions of other M-like proteins with one exception: there was a 46% identity between the first 22 amino acids of the group G streptococcal protein and the corresponding sequence of PAM, the plasminogen-binding M-like protein of type M53 group A streptococci. Like the proteins extracted from the streptococci, the recombinant proteins bound plasminogen, fibrinogen and albumin. The three plasma proteins bound to separate sites on the streptococcal M-like proteins. Plasminogen bound by the group C and G streptococcal proteins was readily activated by streptokinase, providing evidence for a functional link between the secreted plasminogen-activator and proteins exposed on the bacterial surface.},
  author       = {Ben Nasr, A and Wistedt, A and Ringdahl, Ulrika and Sjöbring, Ulf},
  issn         = {0014-2956},
  language     = {eng},
  number       = {2},
  pages        = {267--276},
  publisher    = {ARRAY(0x963b3b8)},
  series       = {European Journal of Biochemistry},
  title        = {Streptokinase activates plasminogen bound to human group C and G streptococci through M-like proteins.},
  volume       = {222},
  year         = {1994},
}