Cargando…
Interaction of streptococcal plasminogen binding proteins with the host fibrinolytic system
The ability to take advantage of plasminogen and its activated form plasmin is a common mechanism used by commensal as well as pathogenic bacteria in interaction with their respective host. Hence, a huge variety of plasminogen binding proteins and activation mechanisms exist. This review solely focu...
Autores principales: | , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2013
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3837353/ https://www.ncbi.nlm.nih.gov/pubmed/24319673 http://dx.doi.org/10.3389/fcimb.2013.00085 |
_version_ | 1782292428831588352 |
---|---|
author | Fulde, Marcus Steinert, Michael Bergmann, Simone |
author_facet | Fulde, Marcus Steinert, Michael Bergmann, Simone |
author_sort | Fulde, Marcus |
collection | PubMed |
description | The ability to take advantage of plasminogen and its activated form plasmin is a common mechanism used by commensal as well as pathogenic bacteria in interaction with their respective host. Hence, a huge variety of plasminogen binding proteins and activation mechanisms exist. This review solely focuses on the genus Streptococcus and, in particular, on the so-called non-activating plasminogen binding proteins. Based on structural and functional differences, as well as on their mode of surface linkaging, three groups can be assigned: M-(like) proteins, surface displayed cytoplasmatic proteins with enzymatic activities (“moonlighting proteins”) and other surface proteins. Here, the plasminogen binding sites and the interaction mechanisms are compared. Recent findings on the functional consequences of these interactions on tissue degradation and immune evasion are summarized. |
format | Online Article Text |
id | pubmed-3837353 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-38373532013-12-06 Interaction of streptococcal plasminogen binding proteins with the host fibrinolytic system Fulde, Marcus Steinert, Michael Bergmann, Simone Front Cell Infect Microbiol Microbiology The ability to take advantage of plasminogen and its activated form plasmin is a common mechanism used by commensal as well as pathogenic bacteria in interaction with their respective host. Hence, a huge variety of plasminogen binding proteins and activation mechanisms exist. This review solely focuses on the genus Streptococcus and, in particular, on the so-called non-activating plasminogen binding proteins. Based on structural and functional differences, as well as on their mode of surface linkaging, three groups can be assigned: M-(like) proteins, surface displayed cytoplasmatic proteins with enzymatic activities (“moonlighting proteins”) and other surface proteins. Here, the plasminogen binding sites and the interaction mechanisms are compared. Recent findings on the functional consequences of these interactions on tissue degradation and immune evasion are summarized. Frontiers Media S.A. 2013-11-22 /pmc/articles/PMC3837353/ /pubmed/24319673 http://dx.doi.org/10.3389/fcimb.2013.00085 Text en Copyright © 2013 Fulde, Steinert and Bergmann. http://creativecommons.org/licenses/by/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Microbiology Fulde, Marcus Steinert, Michael Bergmann, Simone Interaction of streptococcal plasminogen binding proteins with the host fibrinolytic system |
title | Interaction of streptococcal plasminogen binding proteins with the host fibrinolytic system |
title_full | Interaction of streptococcal plasminogen binding proteins with the host fibrinolytic system |
title_fullStr | Interaction of streptococcal plasminogen binding proteins with the host fibrinolytic system |
title_full_unstemmed | Interaction of streptococcal plasminogen binding proteins with the host fibrinolytic system |
title_short | Interaction of streptococcal plasminogen binding proteins with the host fibrinolytic system |
title_sort | interaction of streptococcal plasminogen binding proteins with the host fibrinolytic system |
topic | Microbiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3837353/ https://www.ncbi.nlm.nih.gov/pubmed/24319673 http://dx.doi.org/10.3389/fcimb.2013.00085 |
work_keys_str_mv | AT fuldemarcus interactionofstreptococcalplasminogenbindingproteinswiththehostfibrinolyticsystem AT steinertmichael interactionofstreptococcalplasminogenbindingproteinswiththehostfibrinolyticsystem AT bergmannsimone interactionofstreptococcalplasminogenbindingproteinswiththehostfibrinolyticsystem |