Ha. Davies et al., INDUCTION OF EXTRACELLULAR-MATRIX GLYCOPROTEINS IN BRASSICA PETIOLES BY WOUNDING AND IN RESPONSE TO XANTHOMONAS-CAMPESTRIS, Molecular plant-microbe interactions, 10(7), 1997, pp. 812-820
A panel of monoclonal antibodies that recognize plant extracellular ma
trix glycoproteins previously implicated in plant-microbe interactions
was used to study the effects of pathogen inoculation and wounding on
glycoproteins in petioles of Brassica campestris. The panel of monocl
onal comprised two sets: JIM11, JIM12, and JIM20 recognize epitopes ca
rried on hydroxyproline-rich glycoproteins (HRGPs) (M. Smallwood, A. B
even, N. Donovan, S. J. Neill, J. Peart, K. Roberts, and J. P. Knox, P
lant J. 5:237-246, 1994); MAC204 and MAC265 recognize glycoproteins of
the Rhizobium infection thread (K. A. VandenBosch, D. J. Bradley, S.
Perotto, G. W. Butcher, and N. J. Brewin, EMBO J. 8:335-342, 1989). Wo
unding or inoculation of petioles with avirulent strains of pathovars
of Xanthomonas campestris induced the synthesis of two new groups of a
ntigens: gp160 ran as a smear on sodium dodecyl sulfate-polyacrylamide
gel electrophoresis (SDS-PAGE) with apparent molecular mass from 120
to 200 kDa and was recognized by JIM20 and MAC204; gpS remained in the
stacking gel on SDS-PAGE and was recognized by JIM11, JIM20, and MAC2
04. The response to virulent strains of pathovars of X. campestris was
either less pronounced or absent. gpS comprised several components th
at were resolved by cation-exchange chromatography. Some of these comp
onents were characterized as extensin-like HRGPs. The level of inducti
on of the gpS group of antigens by virulent strains was not altered by
mutation of a number of genes required for basic pathogenicity or by
heat-killing the bacteria.