The metalloprotease PrtV from Vibrio cholerae
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چکیده
منابع مشابه
The metalloprotease PrtV from Vibrio cholerae Purification and properties
The Vibrio metalloprotease PrtV was purified from the culture supernatant of a Vibrio cholerae derivative that is deficient in several other secreted peptidases, including the otherwise abundant hemagglutinin/protease HapA. The PrtV is synthesized as a 102 kDa protein, but undergoes several N- and C-terminal processing steps during V. cholerae envelope translocation and prolonged incubation. Pu...
متن کاملDomain isolation, expression, purification and proteolytic activity of the metalloprotease PrtV from Vibrio cholerae.
The metalloprotease PrtV from Vibrio cholerae serves an important function for the bacteria's ability to invade the mammalian host cell. The protein belongs to the family of M6 proteases, with a characteristic zinc ion in the catalytic active site. PrtV constitutes a 918 amino acids (102 kDa) multidomain pre-pro-protein that so far has only been expressed in V. cholerae. Structural studies requ...
متن کاملCalcium binding by the PKD1 domain regulates interdomain flexibility in Vibrio cholerae metalloprotease PrtV☆
Vibrio cholerae, the causative agent of cholera, releases several virulence factors including secreted proteases when it infects its host. These factors attack host cell proteins and break down tissue barriers and cellular matrix components such as collagen, laminin, fibronectin, keratin, elastin, and they induce necrotic tissue damage. The secreted protease PrtV constitutes one virulence facto...
متن کاملStructure of the N‐terminal domain of the metalloprotease PrtV from V ibrio cholerae
The metalloprotease PrtV from Vibrio cholerae serves an important function for the ability of bacteria to invade the mammalian host cell. The protein belongs to the family of M6 proteases, with a characteristic zinc ion in the catalytic active site. PrtV constitutes a 918 amino acids (102 kDa) multidomain pre-pro-protein that undergoes several N- and C-terminal modifications to form a catalytic...
متن کاملOuter Membrane Vesicle-Mediated Export of Processed PrtV Protease from Vibrio cholerae
BACKGROUND Outer membrane vesicles (OMVs) are known to release from almost all Gram-negative bacteria during normal growth. OMVs carry different biologically active toxins and enzymes into the surrounding environment. We suggest that OMVs may therefore be able to transport bacterial proteases into the target host cells. We present here an analysis of the Vibrio cholerae OMV-associated protease ...
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ژورنال
عنوان ژورنال: FEBS Journal
سال: 2008
ISSN: 1742-464X
DOI: 10.1111/j.1742-4658.2008.06470.x