The interaction between endopolygalacturonase from Fusarium moniliforme and PGIP from Phaseolus Vulgaris studied by surface plasmon resonance and mass spectrometry

B Mattei, F Cervone, Peter Roepstorff

Publikation: Bidrag til tidsskriftKonferenceartikelForskningpeer review

Resumé

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 endopolygalacturonase (PG) from Fusarium moniliforme and a polygalacturonase-inhibiting protein (PGIP) from Phaseolus vulgaris. 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.

OriginalsprogEngelsk
TidsskriftComparative and Functional Genomics
Vol/bind2
Udgave nummer6
Sider (fra-til)359-364
ISSN1531-6912
DOI
StatusUdgivet - 2001

Fingeraftryk

Polygalacturonase
Phaseolus
Surface Plasmon Resonance
Fusarium
Proteins
Peptides
Plant Cells
Glycosylation
Cell Wall
Proteolysis

Citer dette

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title = "The interaction between endopolygalacturonase from Fusarium moniliforme and PGIP from Phaseolus Vulgaris studied by surface plasmon resonance and mass spectrometry",
abstract = "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 endopolygalacturonase (PG) from Fusarium moniliforme and a polygalacturonase-inhibiting protein (PGIP) from Phaseolus vulgaris. 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.",
author = "B Mattei and F Cervone and Peter Roepstorff",
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The interaction between endopolygalacturonase from Fusarium moniliforme and PGIP from Phaseolus Vulgaris studied by surface plasmon resonance and mass spectrometry. / Mattei, B; Cervone, F; Roepstorff, Peter.

I: Comparative and Functional Genomics, Bind 2, Nr. 6, 2001, s. 359-364.

Publikation: Bidrag til tidsskriftKonferenceartikelForskningpeer review

TY - GEN

T1 - The interaction between endopolygalacturonase from Fusarium moniliforme and PGIP from Phaseolus Vulgaris studied by surface plasmon resonance and mass spectrometry

AU - Mattei, B

AU - Cervone, F

AU - Roepstorff, Peter

PY - 2001

Y1 - 2001

N2 - 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 endopolygalacturonase (PG) from Fusarium moniliforme and a polygalacturonase-inhibiting protein (PGIP) from Phaseolus vulgaris. 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.

AB - 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 endopolygalacturonase (PG) from Fusarium moniliforme and a polygalacturonase-inhibiting protein (PGIP) from Phaseolus vulgaris. 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.

U2 - 10.1002/cfg.113

DO - 10.1002/cfg.113

M3 - Conference article

VL - 2

SP - 359

EP - 364

JO - Comparative and Functional Genomics

JF - Comparative and Functional Genomics

SN - 1531-6912

IS - 6

ER -