O. Rossier et al., The Xanthomonas Hrp type III system secretes proteins from plant and mammalian bacterial pathogens, P NAS US, 96(16), 1999, pp. 9368-9373
Citations number
52
Categorie Soggetti
Multidisciplinary
Journal title
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Studies of essential pathogenicity determinants in Gram-negative bacteria h
ave revealed the conservation of type III protein secretion systems that al
low delivery of virulence factors into host cells from plant and animal pat
hogens. Ten of 21 Hrp proteins of the plant pathogen Xanthomonas campestris
pv, vesicatoria have been suggested to be part of a type III machinery, He
re, we report the hrp-dependent secretion of two avirulence proteins, AvrBs
3 and AvrRxv, by X. campestris pv. vesicatoria strains that constitutively
express hrp genes. Secretion occurred without leakage of a cytoplasmic mark
er in minimal medium containing BSA, at pH 5.4, Secretion was strictly hrp-
dependent because a mutant carrying a deletion in hrcV, a conserved hrp gen
e, did not secrete AvrBs3 and AvrRxv. Moreover, the Hrp system of X. campes
tris pv, vesicatoria was able to secrete proteins from two other plant path
ogens: PopA, a protein secreted via the Hrp system in Ralstonia solanacearu
m, and AvrB, an avirulence protein from Pseudomonas syringae pv, glycinea.
Interestingly, X, campestris pv, vesicatoria also secreted YopE, a type III
-secreted cytotoxin of the mammalian pathogen Yersinia pseudotuberculosis i
n a hrp-dependent manner. YerA, a YopE-specific chaperone, was required for
YopE stability but not for secretion in X. campestris pv. vesicatoria. Our
results demonstrate the functional conservation of the type In system of X
. campestris for secretion of proteins from both plant and mammalian pathog
ens and imply recognition of their respective secretion signals.