TY - JOUR T1 - AggA is required for aggregation and increased biofilm formation of a hyper-aggregating mutant of Shewanella oneidensis MR-1. JF - Microbiology Y1 - 2006 A1 - De Windt, Wim A1 - Gao, Haichun A1 - Krömer, Wolfgang A1 - Van Damme, Petra A1 - Dick, Jan A1 - Jan Mast A1 - Boon, Nico A1 - Zhou, Jizhong A1 - Verstraete, Willy KW - Bacterial Adhesion KW - Bacterial Proteins KW - Biofilms KW - Gene Expression Regulation, Bacterial KW - Mutation KW - Oligonucleotide Array Sequence Analysis KW - Proteomics KW - Shewanella AB -

Shewanella oneidensis COAG, a hyper-aggregating mutant of MR-1, was isolated from a rifampicin-challenged culture. Compared to the wild-type, COAG exhibited increased biofilm formation on glass carrier material. The role of surface-located proteins in the process of COAG auto-aggregation was confirmed by different proteolytic treatments of the aggregates. All of the tested proteolytic enzymes resulted in deflocculation within 3 h of incubation. In order to examine the altered expression of outer-membrane proteins in COAG, membrane-enriched cell preparations were analysed by proteomics and the protein pattern was compared to that of MR-1. From the proteomics results, it was hypothesized that the agglutination protein AggA, associated with the secretion of a putative RTX protein, was involved in the hyper-aggregating phenotype. These results were confirmed with a DNA microarray study of COAG versus MR-1. An insertional mutation in the S. oneidensis COAG aggA locus resulted in loss of the hyper-aggregating properties and the increased biofilm-forming capability. The insertional mutation resulted in strongly decreased attachment during the initial stage of biofilm formation. By complementing this mutation with the vector pCM62, expressing the aggA gene, this effect could be nullified and biofilm formation was restored to at least the level of the MR-1 wild-type.

VL - 152 CP - Pt 3 U1 - http://www.ncbi.nlm.nih.gov/pubmed/16514152?dopt=Abstract M3 - 10.1099/mic.0.28204-0 ER -