<p>This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.</p> <p>A combination of surface plasmon resonance (SPR) and matrix-assisted laser-desorptionionization-
time-of-flight mass spectrometry (MALDI-TOF-MS) was used to study the
interaction between <italic>endo</italic>polygalacturonase (PG) from <italic>Fusarium moniliforme</italic> and
a polygalacturonase-inhibiting protein (PGIP) from <italic>Phaseolus vulgaris.</italic> PG hydrolyses the
homogalacturonan of the plant cell wall and is considered an important pathogenicity
factor of many fungi. PGIP is a specific inhibitor of fungal PGs and is thought to be
involved in plant defence against phytopathogenic fungi. SPR was used either to study the
effect of the PG glycosylation on the formation of the complex with PGIP, and as a
sensitive affinity capture of an interacting peptide from a mixture of PG fragments
obtained by limited proteolysis. Mass spectrometry allowed to characterise the interacting
peptide eluted from the sensor surface.</p>
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Comp Funct Genomics. 2001 Dec; 2(6):359-364