The grapevine aspartic protease gene family: characterization and expression modulation in response to Plasmopara viticola.
Aspartic proteases
Defense
Downy mildew
Plant-pathogen interaction
Vitis vinifera
Journal
Journal of plant research
ISSN: 1618-0860
Titre abrégé: J Plant Res
Pays: Japan
ID NLM: 9887853
Informations de publication
Date de publication:
May 2022
May 2022
Historique:
received:
31
12
2021
accepted:
28
03
2022
pubmed:
16
4
2022
medline:
11
5
2022
entrez:
15
4
2022
Statut:
ppublish
Résumé
Grapevine aspartic proteases gene family is characterized and five VviAPs appear to be involved in grapevine defense against downy mildew. Grapevine (Vitis vinifera L.) is one of the most important crops worldwide. However, it is highly susceptible to the downy mildew disease caused by Plasmopara viticola (Berk. & Curt.) Berl. & De Toni. To minimize the use of fungicides used to control P. viticola, it is essential to gain a deeper comprehension on this pathosystem and proteases have gained particular interest in the past decade. Proteases were shown to actively participate in plant-pathogen interactions, not only in the processes that lead to plant cell death, stress responses and protein processing/degradation but also as components of the recognition and signalling pathways. The aim of this study was to identify and characterize the aspartic proteases (APs) involvement in grapevine defense against P. viticola. A genome-wide search and bioinformatics characterization of the V. vinifera AP gene family was conducted and a total of 81 APs proteins, coded by 65 genes, were found. VviAPs proteins can be divided into three categories, similar to those previously described for other plants. Twelve APs coding genes were selected, and expression analysis was conducted at several time-points after inoculation in both compatible and incompatible interactions. Five grapevine APs may be involved in grapevine tolerance against P. viticola. Our findings provide an overall understanding of the VviAPs gene family and establish better groundwork to further describe the roles of VviAPs in defense against P. viticola.
Identifiants
pubmed: 35426578
doi: 10.1007/s10265-022-01390-z
pii: 10.1007/s10265-022-01390-z
doi:
Substances chimiques
Peptide Hydrolases
EC 3.4.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
501-515Subventions
Organisme : Fundação para a Ciência e a Tecnologia
ID : UIDP/04046/2020
Organisme : Fundação para a Ciência e a Tecnologia
ID : PTDC/BIA-BQM/28539/2017
Organisme : Fundação para a Ciência e a Tecnologia
ID : IF/00819/2015
Informations de copyright
© 2022. The Author(s) under exclusive licence to The Botanical Society of Japan.
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