Studies on flagellin glycosylation and pathogenicity of Pseudomonas syringae

Abstract

Isolates of the phytopathogenic bacterium Pseudomonas syringae can be classified into more than 50 pathovars on the basis of virulence for host plant species. Our previous studies have shown that P. syringae flagellin elicits hypersensitive reactions (HR) in nonhost plants. Although the deduced amino acid sequences of the flagellin proteins of P. syringae pv. tabaci 6605 (Pta6605) and P. syringae pv. glycinea race 4 (Pgl4) are identical, the flagellin protein of Pgl4 causes cell death in nonhost tobacco cells, whereas that of Pta6605 does not. Further, the flagellin proteins of these two pathovars are glycosylated. In this study, we describe genetic and structural analyses of the glycosylation of flagellin in Pgl4 and Pta6605.