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Mapping glycans onto specific N-linked glycosylation sites of Pyrus communis PGIP redefines the interface for EPG-PGIP interactions. J Proteome Res 2009 Feb;8(2):673-80

Date

12/17/2008

Pubmed ID

19072240

Pubmed Central ID

PMC4141487

DOI

10.1021/pr800855f

Scopus ID

2-s2.0-61849140680   19 Citations

Abstract

Polygalacturonase inhibiting proteins (PGIPs) are members of the leucine rich repeat family of proteins, involved in plant defense against fungal pathogens. PGIPs exhibit a remarkable degree of specificity in terms of their ability to bind and inhibit their target molecules, the endopolygalacturonases (EPGs). This specificity has been attributed for certain EPG/PGIP combinations to differences in primary sequence, but this explanation is unable to account for the full range of binding and inhibitory activities observed. In this paper, we have fully characterized the glycosylation on the PGIP derived from Pyrus communis and demonstrated, using a combination of PNGaseF and PNGaseA in (18)O-water, that the Pyrus communis PGIP utilizes all seven potential sites of N-linked glycosylation. Further, we demonstrate that certain sites appear to be modified only by glycans bearing alpha3-linked core fucosylation, while others are occupied by a mixture of fucosylated and nonfucosylated glycans. Modeling of the carbohydrates onto a homologous structure of PGIP indicates potential roles for glycosylation in mediating the interactions of PGIPs with EPGs.

Author List

Lim JM, Aoki K, Angel P, Garrison D, King D, Tiemeyer M, Bergmann C, Wells L

Author

Kazuhiro Aoki PhD Associate Professor in the Cell Biology, Neurobiology and Anatomy department at Medical College of Wisconsin




MESH terms used to index this publication - Major topics in bold

Antifungal Agents
Carbohydrate Conformation
Carbohydrate Sequence
Glycosylation
Models, Molecular
Molecular Sequence Data
Plant Proteins
Polygalacturonase
Polysaccharides
Protein Conformation
Pyrus