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A high-molecular-weight outer membrane protein of Xanthomonas oryzae pv. oryzae exhibits similarity to non-fimbrial adhesins of animal pathogenic bacteria and is required for optimum virulence by Suvendra K. Ray; R. Rajeshwari; Yogendra Sharma; Ramesh V. Sonti is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Summary Transposon insertions in a novel 3.798 kb open reading frame (ORF) of the rice pathogen, __Xanthomonas oryzae__ pv. __oryzae__ (__Xoo__) cause virulence deficiency and altered colony/lawn morphology. This ORF encodes a protein, XadA, of 1265 amino acids that exhibits significant similarity to non‐fimbrial adhesins of animal pathogenic bacteria such as __Yersinia__ YadA and __Moraxella__ UspA1. An interesting feature is that the YadA similarity region is repeated six times within the XadA sequence and encompasses almost the entire length of the protein. Anti‐XadA antibodies identified a 110 kDa outer membrane protein that was sensitive to protease treatment of whole cells. XadA expression is induced in minimal medium. Homology modelling suggests that XadA adopts a β‐helix conformation‐like pertactin, a non‐fimbrial adhesin of __Bordetella pertussis__. This work is the first characterization of a non‐fimbrial adhesin‐like molecule in a plant pathogenic bacterium. It extends our knowledge about the repertoire of homologous virulence factors that are deployed by animal and plant pathogenic bacteria to include functions potentially involved in adhesion.

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Author

Suvendra K. Ray; R. Rajeshwari; Yogendra Sharma; Ramesh V. Sonti

Publisher

John Wiley and Sons; Wiley (Blackwell Publishing); Blackwell Publishing Inc.; Wiley (ISSN 0950-382X)

Published

2002

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)