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Identification of a plasminogen-binding motif in PAM, a bacterial surface protein.

Wistedt, AC; Ringdahl, Ulrika LU ; Muller-Esterl, W and Sjöbring, Ulf LU (1995) In Molecular Microbiology 18(3). p.569-578
Abstract
Surface-associated plasmin(ogen) may contribute to the invasive properties of various cells. Analysis of plasmin(ogen)-binding surface proteins is therefore of interest. The N-terminal variable regions of M-like (ML) proteins from five different group A streptococcal serotypes (33, 41, 52, 53 and 56) exhibiting the plasminogen-binding phenotype were cloned and expressed in Escherichia coli. The recombinant proteins all bound plasminogen with high affinity. The binding involved the kringle domains of plasminogen and was blocked by a lysine analogue, 6-aminohexanoic acid, indicating that lysine residues in the M-like proteins participate in the interaction. Sequence analysis revealed that the proteins contain common 13-16-amino-acid tandem... (More)
Surface-associated plasmin(ogen) may contribute to the invasive properties of various cells. Analysis of plasmin(ogen)-binding surface proteins is therefore of interest. The N-terminal variable regions of M-like (ML) proteins from five different group A streptococcal serotypes (33, 41, 52, 53 and 56) exhibiting the plasminogen-binding phenotype were cloned and expressed in Escherichia coli. The recombinant proteins all bound plasminogen with high affinity. The binding involved the kringle domains of plasminogen and was blocked by a lysine analogue, 6-aminohexanoic acid, indicating that lysine residues in the M-like proteins participate in the interaction. Sequence analysis revealed that the proteins contain common 13-16-amino-acid tandem repeats, each with a single central lysine residue. Experiments with fusion proteins and a 30-amino-acid synthetic peptide demonstrated that these repeats harbour the major plasminogen-binding site in the ML53 protein, as well as a binding site for the tissue-type plasminogen activator. Replacement of the lysine in the first repeat with alanine reduced the plasminogen-binding capacity of the ML53 protein by 80%. The results precisely localize the binding domain in a plasminogen surface receptor, thereby providing a unique ligand for the analysis of interactions between kringles and proteins with internal kringle-binding determinants. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Molecular Microbiology
volume
18
issue
3
pages
569 - 578
publisher
Wiley-Blackwell
external identifiers
  • Scopus:0001122618
ISSN
1365-2958
language
English
LU publication?
yes
id
cec24f25-7517-4d12-b4dc-5d45b7968124 (old id 1216591)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/8748039
http://onlinelibrary.wiley.com/doi/10.1111/j.1365-2958.1995.mmi_18030569.x/abstract
date added to LUP
2013-10-09 15:39:30
date last changed
2016-12-04 04:49:22
@misc{cec24f25-7517-4d12-b4dc-5d45b7968124,
  abstract     = {Surface-associated plasmin(ogen) may contribute to the invasive properties of various cells. Analysis of plasmin(ogen)-binding surface proteins is therefore of interest. The N-terminal variable regions of M-like (ML) proteins from five different group A streptococcal serotypes (33, 41, 52, 53 and 56) exhibiting the plasminogen-binding phenotype were cloned and expressed in Escherichia coli. The recombinant proteins all bound plasminogen with high affinity. The binding involved the kringle domains of plasminogen and was blocked by a lysine analogue, 6-aminohexanoic acid, indicating that lysine residues in the M-like proteins participate in the interaction. Sequence analysis revealed that the proteins contain common 13-16-amino-acid tandem repeats, each with a single central lysine residue. Experiments with fusion proteins and a 30-amino-acid synthetic peptide demonstrated that these repeats harbour the major plasminogen-binding site in the ML53 protein, as well as a binding site for the tissue-type plasminogen activator. Replacement of the lysine in the first repeat with alanine reduced the plasminogen-binding capacity of the ML53 protein by 80%. The results precisely localize the binding domain in a plasminogen surface receptor, thereby providing a unique ligand for the analysis of interactions between kringles and proteins with internal kringle-binding determinants.},
  author       = {Wistedt, AC and Ringdahl, Ulrika and Muller-Esterl, W and Sjöbring, Ulf},
  issn         = {1365-2958},
  language     = {eng},
  number       = {3},
  pages        = {569--578},
  publisher    = {ARRAY(0xd900710)},
  series       = {Molecular Microbiology},
  title        = {Identification of a plasminogen-binding motif in PAM, a bacterial surface protein.},
  volume       = {18},
  year         = {1995},
}