Open AccessThe interaction between endo polygalacturonase from Fusarium moniliforme and PGIP from Phaseolus vulgaris studied by surface plasmon resonance and mass spectrometry.
Author(s) -
Mattei Benedetta,
Cervone Felice,
Roepstorff Peter
Publication year - 2001
Publication title -
comparative and functional genomics
Language(s) - English
Resource type - Journals
eISSN - 1532-6268
pISSN - 1531-6912
DOI - 10.1002/cfg.113
Subject(s) - pectinase , phaseolus , surface plasmon resonance , chemistry , mass spectrometry , cell wall , fusarium , biochemistry , chromatography , botany , biology , enzyme , nanotechnology , nanoparticle , materials science
A combination of surface plasmon resonance (SPR) and matrix‐assisted laser‐desorption‐ionization‐time‐of‐flightmass spectrometry (MALDI‐TOF‐MS) was used to study the interaction between endo polygalacturonase(PG) from Fusarium moniliforme and a polygalacturonase‐inhibitingprotein (PGIP) from Phaseolus vulgaris . PG hydrolyses the homogalacturonanof the plant cell wall and is considered an important pathogenicity factorof many fungi. PGIP is a specific inhibitor of fungal PGs and is thought tobe involved in plant defence against phytopathogenic fungi. SPR was used eitherto study the effect of the PG glycosylation on the formation of the complexwith PGIP, and as a sensitive affinity capture of an interacting peptide froma mixture of PG fragments obtained by limited proteolysis. Mass spectrometryallowed to characterise the interacting peptide eluted from the sensor surface.Copyright © 2001 John Wiley & Sons, Ltd.