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YadA bacterial adhesin protein domain
In molecular biology, YadA is a protein domain which is short for ''Yersinia'' adhesin A. These proteins have strong sequence and structural homology, particularly at their C-terminal end. The function is to promote their pathogenicity and virulence in host cells, though cell adhesion. YadA is found in three pathogenic species of ''Yersinia'', ''Y. pestis,'' ''Y. pseudotuberculosis'', and ''Y. enterocolitica''. The YadA domain is encoded for by a virulence plasmid in ''Yersinia'', which encodes a type-III secretion (T3S) system consisting of the Ysc injectisome and the
Yop effectors.
==Function==
Essentially, the main function of the YadA domain is to help cell adhesion and to increase virulence. YadA is a collagen-binding outer membrane protein. It forms the fibrillar matrix on the bacterial cell surface. This aids cell attachment and helps the bacteria invade eukaryotic cells. Additionally, by forming the fibrillar matrix, the YadA domain protects the bacteria by facilitating agglutination resistance, serum resistance, complement inactivation and phagocytosis resistance.
The importance of adhesins to YadA function and ''Yersinia'' survival is huge. Attachment further allows more interactions and increase of biofilm formation to aid bacterial colonization. In ''Yersinia'', it helps initiate the infectious process in host cells and are critical virulence factors. Additionally, bacteria have the ability to regulate adhesin expression, meaning that when ''Yersinia'' no longer requires YadA, it can be turned off. Furthermore, YadA expression is mainly temperature regulated, at 37 degrees Celsius. It also has two molecular regulators: an activator, VirF and a repressor, YmoA.
抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』
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