Proteomics

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Comparative secretome analysis of Magnaporthe oryzae identified N-glycosylation proteins involved in fungal pathogenicity and cell wall integrity


ABSTRACT: Plant fungal pathogens secrete numerous proteins into the apoplast at the plant-fungus contact sites to facilitate colonization. Only a limited number of secreted proteins have been functionally characterized in Magnaporthe oryzae, the causal agent of blast disease in rice (Oryza sativa). Intriguingly, the ∆alg3 mutant of M. oryzae, which -1, 3-mannosyltransferase ALG3, shows strong defects in fungal cell wall integrity and virulence, indicating a potential effect on the secretion of multiple proteins. Therefore, in this study, we used a proteomics approach, comparing wild type and ∆alg3 mutants, to identify 51 proteins that require ALG3 for proper secretion. Elucidation of the comparative secretome of M. oryzae improves our understanding of the proteins that require ALG3 for secretion, and of their function in fungal virulence and cell wall integrity.

ORGANISM(S): Magnaporthe Oryzae P131

SUBMITTER: Xunli LU  

PROVIDER: PXD024706 | iProX | Fri Mar 12 00:00:00 GMT 2021

REPOSITORIES: iProX

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Comparative Secretome Analysis of Magnaporthe oryzae Identified Proteins Involved in Virulence and Cell Wall Integrity.

Liu Ning N   Qi Linlu L   Huang Manna M   Chen Deng D   Yin Changfa C   Zhang Yiying Y   Wang Xingbin X   Yuan Guixin G   Wang Rui-Jin RJ   Yang Jun J   Peng You-Liang YL   Lu Xunli X  

Genomics, proteomics & bioinformatics 20210718 4


Plant fungal pathogens secrete numerous proteins into the apoplast at the plant-fungus contact sites to facilitate colonization. However, only a few secretory proteins were functionally characterized in Magnaporthe oryzae, the fungal pathogen causing rice blast disease worldwide. Asparagine-linked glycosylation 3 (Alg3) is an α-1,3-mannosyltransferase functioning in the N-glycan synthesis of N-glycosylated secretory proteins. Fungal pathogenicity and cell wall integrity are impaired in Δalg3 mut  ...[more]

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