ausblenden:
Schlagwörter:
Aeromonas/me [Metabolism]; Aeromonas/py [Pathogenicity]; *Aeromonas/ul [Ultrastructure]; Bacterial Proteins/ch [Chemistry]; Cations, Divalent/me [Metabolism]; Edetic Acid; Egtazic Acid; Microscopy, Electron; Protein Conformation; Support, Non-U.S. Gov't; Virulence/ph [Physiology]
Zusammenfassung:
The fish pathogen Aeromonas salmonicida possesses a regular surface layer (or A-layer) which is an important virulence determinant. The A-protein, a single bilobed protein organized in a p4 lattice of M4C4 arrangement with two morphological domains, comprises this layer. The role of divalent cations in the A-layer structure was studied to better understand A-protein subunit interactions affecting structural flexibility and function. Divalent cation bridges were found to be involved in the integrity of the A-layer. Two novel A-layer patterns were formed as the result of growth under calcium limitation or by chelation of divalent cations with EDTA or EGTA, thereby constituting the first reported case of formation of distinct regular arrays upon divalent cation depletion. Furthermore, under these conditions A-protein was sometimes released as tetrameric units, rather than in monomeric form. The formation of the two novel patterns is best explained by a sequence of structural rearrangements, following disruption of only one of the two A-layer morphological units, that is, those held together by divalent cation bridges. The free tetrameric units represent four A-protein subunits clustered around the unaffected four-fold axis.
