Cooperative Plasminogen Recruitment to the Surface of Streptococcus canis via M Protein and Enolase Enhances Bacterial Survival
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منابع مشابه
Cooperative Plasminogen Recruitment to the Surface of Streptococcus canis via M Protein and Enolase Enhances Bacterial Survival
UNLABELLED Streptococcus canis is a zoonotic pathogen capable of causing serious invasive diseases in domestic animals and humans. Surface-exposed M proteins and metabolic enzymes have been characterized as major virulence determinants in various streptococcal species. Recently, we have identified SCM, the M-like protein of S. canis, as the major receptor for miniplasminogen localized on the ba...
متن کاملSCM, a novel M-like protein from Streptococcus canis, binds (mini)-plasminogen with high affinity and facilitates bacterial transmigration.
Streptococcus canis is an important zoonotic pathogen capable of causing serious invasive diseases in domestic animals and humans. In the present paper we report the binding of human plasminogen to S. canis and the recruitment of proteolytically active plasmin on its surface. The binding receptor for plasminogen was identified as a novel M-like protein designated SCM (S. canis M-like protein). ...
متن کاملSCM, the M Protein of Streptococcus canis Binds Immunoglobulin G
The M protein of Streptococcus canis (SCM) is a virulence factor and serves as a surface-associated receptor with a particular affinity for mini-plasminogen, a cleavage product of the broad-spectrum serine protease plasmin. Here, we report that SCM has an additional high-affinity immunoglobulin G (IgG) binding activity. The ability of a particular S. canis isolate to bind to IgG significantly c...
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Borrelia burgdorferi is the causative agent of Lyme disease, the most commonly reported arthropod-borne disease in the United States. B. burgdorferi is a highly invasive bacterium, yet lacks extracellular protease activity. In order to aid in its dissemination, B. burgdorferi binds plasminogen, a component of the hosts' fibrinolytic system. Plasminogen bound to the surface of B. burgdorferi can...
متن کاملStreptococcus mutans Surface -Enolase Binds Salivary Mucin MG2 and Human Plasminogen
Matrix-assisted laser desorption ionization–time of flight mass spectrometry analysis identified enolase as a cell surface component of Streptococcus mutans, which was confirmed by enzyme-linked immunosorbent assay, Western blotting, and transmission electron microscopy. Surface enolase was demonstrated to bind to human plasminogen and salivary mucin MG2. The results suggested a role for enolas...
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ژورنال
عنوان ژورنال: mBio
سال: 2013
ISSN: 2161-2129,2150-7511
DOI: 10.1128/mbio.00629-12