Plant immunity suppression by an exo-β-1,3-glucanase and an elongation factor 1α of the rice blast fungus

Hang Liu, Xunli Lu, Mengfei Li, Zhiqin Lun, Xia Yan, Changfa Yin, Guixin Yuan, Xingbin Wang, Ning Liu, Di Liu, Mian Wu, Ziluolong Luo, Yan Zhang, Vijai Bhadauria, Jun Yang, Nicholas J. Talbot and You-Liang Peng ()
Additional contact information
Hang Liu: China Agricultural University
Xunli Lu: China Agricultural University
Mengfei Li: China Agricultural University
Zhiqin Lun: China Agricultural University
Xia Yan: University of East Anglia, Norwich Research Park
Changfa Yin: China Agricultural University
Guixin Yuan: China Agricultural University
Xingbin Wang: China Agricultural University
Ning Liu: China Agricultural University
Di Liu: China Agricultural University
Mian Wu: China Agricultural University
Ziluolong Luo: China Agricultural University
Yan Zhang: China Agricultural University
Vijai Bhadauria: China Agricultural University
Jun Yang: China Agricultural University
Nicholas J. Talbot: University of East Anglia, Norwich Research Park
You-Liang Peng: China Agricultural University

Nature Communications, 2023, vol. 14, issue 1, 1-16

Abstract: Abstract Fungal cell walls undergo continual remodeling that generates β-1,3-glucan fragments as products of endo-glycosyl hydrolases (GHs), which can be recognized as pathogen-associated molecular patterns (PAMPs) and trigger plant immune responses. How fungal pathogens suppress those responses is often poorly understood. Here, we study mechanisms underlying the suppression of β-1,3-glucan-triggered plant immunity by the blast fungus Magnaporthe oryzae. We show that an exo-β-1,3-glucanase of the GH17 family, named Ebg1, is important for fungal cell wall integrity and virulence of M. oryzae. Ebg1 can hydrolyze β-1,3-glucan and laminarin into glucose, thus suppressing β-1,3-glucan-triggered plant immunity. However, in addition, Ebg1 seems to act as a PAMP, independent of its hydrolase activity. This Ebg1-induced immunity appears to be dampened by the secretion of an elongation factor 1 alpha protein (EF1α), which interacts and co-localizes with Ebg1 in the apoplast. Future work is needed to understand the mechanisms behind Ebg1-induced immunity and its suppression by EF1α.

Date: 2023
References: View references in EconPapers View complete reference list from CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-023-41175-z Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-41175-z

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-023-41175-z

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().