Surface displaced alfa-enolase of Lactobacillus plantarum is a fibronectin binding protein
نویسندگان
چکیده
منابع مشابه
Surface displaced alfa-enolase of Lactobacillus plantarum is a fibronectin binding protein
BACKGROUND Lactic acid bacteria of the genus Lactobacillus and Bifidobacterium are one of the most important health promoting groups of the human intestinal microbiota. Their protective role within the gut consists in out competing invading pathogens for ecological niches and metabolic substrates. Among the features necessary to provide health benefits, commensal microorganisms must have the ab...
متن کاملMycoplasma synoviae enolase is a plasminogen/fibronectin binding protein
BACKGROUND Mycoplasma synoviae is an avian pathogen that can lead to respiratory tract infections and arthritis in chickens and turkeys, resulting in serious economic losses to the poultry industry. Enolase reportedly plays important roles in several bacterial pathogens, but its role in M. synoviae has not been established. Therefore, in this study, the enolase encoding gene (eno) of M. synovia...
متن کاملBorrelia burgdorferi Enolase Is a Surface-Exposed Plasminogen Binding Protein
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 کاملIdentification of binding sites of Lactobacillus plantarum enolase involved in the interaction with human plasminogen.
The enolase EnoA1 of Lactobacillus plantarum is here shown to interact with human plasminogen (Plg). By sequence alignment of EnoA1 with Streptococcus pneumoniae and Bifidobacterium lactis enolases, we identified BS1 and BS2 Plg-binding sites. A structure prediction of EnoA1 showed lysine residues in position 255 (BS2), and 422 (BS1) exposed on protein surface. A lysine residue in position 259 ...
متن کاملCharacterization of a fibronectin-binding protein from Lactobacillus casei BL23.
AIMS To characterize the functionality of the Lactobacillus casei BL23 fbpA gene encoding a putative fibronectin-binding protein. METHODS AND RESULTS Adhesion tests showed that L. casei BL23 binds immobilized and soluble fibronectin in a protease-sensitive manner. A mutant with inactivated fbpA showed a decrease in binding to immobilized fibronectin and a strong reduction in the surface hydro...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Microbial Cell Factories
سال: 2009
ISSN: 1475-2859
DOI: 10.1186/1475-2859-8-14