Natural disulfide bond-disrupted mutants of AVR4 of the tomato pathogen Cladosporium fulvum are sensitive to proteolysis, circumvent Cf-4-mediated resistance, but retain their chitin binding ability.

@article{Burg2003NaturalDB,
  title={Natural disulfide bond-disrupted mutants of AVR4 of the tomato pathogen Cladosporium fulvum are sensitive to proteolysis, circumvent Cf-4-mediated resistance, but retain their chitin binding ability.},
  author={Harrold A van den Burg and Nienke Westerink and Kees-Jan Françoijs and Ronelle Roth and Esmeralda Woestenenk and Sjef Boeren and Pierre J. G. M. de Wit and M. Joosten and Jacques J.M. Vervoort},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 30},
  pages={27340-6}
}
The extracellular AVR4 elicitor of the pathogenic fungus Cladosporium fulvum induces defense responses in the tomato genotype Cf-4. Here, the four disulfide bonds of AVR4 were identified as Cys-11-41, Cys-21-27, Cys-35-80, and Cys-57-72 by partial reduction with Tris-(2-carboxyethyl)-phosphine hydrochloride, subsequent cyanylation, and base-catalyzed chain cleavage. The resulting peptide fragments were analyzed by mass spectrometry. Sequence homology and the disulfide bond pattern revealed that… CONTINUE READING