ArticleWorld journal of microbiology & biotechnology2026
Multifaceted roles of CcGpi7, a phosphoethanolamine transferase, in physiology and virulence of Corynespora cassiicola.
Article in World journal of microbiology & biotechnology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Gpi7 gene, encoding the catalytic subunit of GPI ethanolamine-phosphate (Etn-P) transferase II, is primarily involved in the synthesis, maturation, and sorting of GPI-anchored proteins (GPI-APs), thereby playing a crucial part in cell wall functions and host-pathogen interactions. This study aimed to investigate the role of Gpi7 (here designated CcGpi7) in Corynespora cassiicola, a devastating fungal pathogen causing leaf spot in cucumber and many other cash crops. We systematically identified and inventoried 138 GPI-APs in C. cassiicola, followed by a detailed structural characterization of the CcGpi7 protein that is strongly induced during infection. Homologous recombination was employed to construct a CcGpi7-deleted mutant (ΔCcGpi7) and its corresponding complementary strain (cCcGpi7). Compared with the wild type and cCcGpi7, deletion of CcGpi7 led to markedly reduced vegetative growth and conidia formation. The ΔCcGpi7 mutant displayed obvious defects in cell wall architecture, manifested as enhanced susceptibility to cell wall-perturbing agents and degrading enzymes. Under stress conditions, ΔCcGpi7 exhibited increased sensitivity to KCl but reduced sensitivity to sorbitol and H
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