A fungal substrate mimicking molecule suppresses plant immunity via an inter-kingdom conserved motif.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
05 04 2019
05 04 2019
Historique:
received:
29
08
2018
accepted:
11
03
2019
entrez:
7
4
2019
pubmed:
7
4
2019
medline:
10
5
2019
Statut:
epublish
Résumé
Ustilago maydis is a biotrophic fungus causing corn smut disease in maize. The secreted effector protein Pit2 is an inhibitor of papain-like cysteine proteases (PLCPs) essential for virulence. Pit2 inhibitory function relies on a conserved 14 amino acids motif (PID14). Here we show that synthetic PID14 peptides act more efficiently as PLCP inhibitors than the full-length Pit2 effector. Mass spectrometry shows processing of Pit2 by maize PLCPs, which releases an inhibitory core motif from the PID14 sequence. Mutational analysis demonstrates that two conserved residues are essential for Pit2 function. We propose that the Pit2 effector functions as a substrate mimicking molecule: Pit2 is a suitable substrate for apoplastic PLCPs and its processing releases the embedded inhibitor peptide, which in turn blocks PLCPs to modulate host immunity. Remarkably, the PID14 core motif is present in several plant associated fungi and bacteria, indicating the existence of a conserved microbial inhibitor of proteases (cMIP).
Identifiants
pubmed: 30952847
doi: 10.1038/s41467-019-09472-8
pii: 10.1038/s41467-019-09472-8
pmc: PMC6450895
doi:
Substances chimiques
Fungal Proteins
0
Virulence Factors
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1576Commentaires et corrections
Type : CommentIn
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