Identification of a plasminogen-binding motif in PAM, a bacterial surface protein.
(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:
https://lup.lub.lu.se/record/1216591
- author
- Wistedt, AC ; Ringdahl, Ulrika LU ; Muller-Esterl, W and Sjöbring, Ulf LU
- organization
- publishing date
- 1995
- 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
- 2016-04-04 14:28:52
- date last changed
- 2025-10-14 11:28:57
@article{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 = {{Wiley-Blackwell}},
series = {{Molecular Microbiology}},
title = {{Identification of a plasminogen-binding motif in PAM, a bacterial surface protein.}},
url = {{http://www.ncbi.nlm.nih.gov/pubmed/8748039}},
volume = {{18}},
year = {{1995}},
}