| Literature DB >> 32611768 |
Wiebke Haeger1, Jana Henning1, David G Heckel1, Yannick Pauchet2, Roy Kirsch2.
Abstract
Plant cell wall-associated polygalacturonase-inhibiting proteins (PGIPs) are widely distributed in the plant kingdom. They play a crucial role in plant defense against phytopathogens by inhibiting microbial polygalacturonases (PGs). PGs hydrolyze the cell wall polysaccharide pectin and are among the first enzymes to be secreted during plant infection. Recent studies demonstrated that herbivorous insects express their own PG multi-gene families, raising the question whether PGIPs also inhibit insect PGs and protect plants from herbivores. Preliminary evidence suggested that PGIPs may negatively influence larval growth of the leaf beetle Phaedon cochleariae (Coleoptera: Chrysomelidae) and identified BrPGIP3 from Chinese cabbage (Brassica rapa ssp. pekinensis) as a candidate. PGIPs are predominantly studied in planta because their heterologous expression in microbial systems is problematic and instability and aggregation of recombinant PGIPs has complicated in vitro inhibition assays. To minimize aggregate formation, we heterologously expressed BrPGIP3 fused to a glycosylphosphatidylinositol (GPI) membrane anchor, immobilizing it on the extracellular surface of insect cells. We demonstrated that BrPGIP3_GPI inhibited several P. cochleariae PGs in vitro, providing the first direct evidence of an interaction between a plant PGIP and an animal PG. Thus, plant PGIPs not only confer resistance against phytopathogens, but may also aid in defense against herbivorous beetles.Entities:
Keywords: GH28; LRR protein; aggregation; enzyme; enzyme inhibitor; herbivorous insect; insect; plant; plant cell wall; plant defense; plant protection; plant-insect interaction; polygalacturonase; polygalacturonase-inhibiting protein; protein aggregation
Year: 2020 PMID: 32611768 PMCID: PMC7450104 DOI: 10.1074/jbc.RA120.014027
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157