@Article{IPB-2157,
author = {Fiegen, M. and Knogge, W.},
title = {{Amino acid alterations in isoforms of the effector protein NIP1 from Rhynchosporium secalis have similar effects on its avirulence- and virulence-associated activities on barley}},
year = {2002},
pages = {299-302},
journal = {Physiol. Mol. Plant Pathol.},
doi = {10.1006/pmpp.2002.0442},
volume = {61},
abstract = {The secreted effector protein NIP1 from the barley pathogen Rhynchosporium secalis is a specific elicitor of defense reactions in host plants carrying the resistance gene Rrs1. In addition, it has activities associated with fungal virulence; independent of the plant genotype it stimulates the plant plasma membrane H\+-ATPase and induces leaf necrosis. Four NIP1 isoforms differing in single amino acid residues were isolated from various naturally occurring fungal strains. All three activities of the protein (race specificity, H\+-ATPase stimulation, necrosis induction) were affected by the amino acid alterations in a similar way suggesting that they are mediated through a single plant receptor.}    
}