PXD017769

PXD017769 is an original dataset announced via ProteomeXchange.

Title	The Hypervariable Amino-Terminus of P1 Protease Modulates Potyviral Replication and Host Defense Responses
Description	The replication of many RNA viruses involves the translation of polyproteins, whose processing by endopeptidases is a critical step for the release of functional subunits. P1 is the first protease encoded in plant potyvirus genomes; once activated by an as-yet-unknown host factor, it acts in cis on its own C-terminal end, hydrolyzing the P1-HCPro junction. Earlier research suggests that P1 cooperates with HCPro to inhibit host RNA silencing defenses. Using Plum pox virus as a model, we show that although P1 does not have a major direct role in RNA silencing suppression, it can indeed modulate HCPro function by its self-cleavage activity. To study P1 protease regulation, we used bioinformatic analysis and in vitro activity experiments to map the core C-terminal catalytic domain. We present evidence that the hypervariable region that precedes the protease domain is predicted as intrinsically disordered, and that it behaves as a negative regulator of P1 proteolytic activity in in vitro cleavage assays. In viral infections, removal of the P1 protease antagonistic regulator is associated with greater symptom severity, induction of salicylate-dependent pathogenesis-related proteins, and reduced viral loads. We suggest that fine modulation of a viral protease activity has evolved to keep viral amplification below host-detrimental levels, and thus to maintain higher long-term replicative capacity.
HostingRepository	PRIDE
AnnounceDate	2020-08-11
AnnouncementXML	Submission_2020-08-10_23:59:05.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD017769
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Sergio Ciordia
SpeciesList	scientific name: Nicotiana benthamiana; NCBI TaxID: 4100;
ModificationList	iTRAQ4plex; Methylthio; Oxidation
Instrument	TripleTOF 5600

Revision	Datetime	Status	ChangeLog Entry
0	2020-02-27 07:52:42	ID requested
⏵ 1	2020-08-10 23:59:06	announced

Pasin F, Sim, ó, n-Mateo C, Garc, í, a JA, The hypervariable amino-terminus of P1 protease modulates potyviral replication and host defense responses. PLoS Pathog, 10(3):e1003985(2014) [pubmed]

submitter keyword: Nicotiana benthamiana, Plum pox virus, NahG, Salicylic acid

Juan Antonio García
contact affiliation	Departamento de Genética Molecular de Plantas, Centro Nacional de Biotecnología (CNB-CSIC), Madrid, Spain.
contact email	jagarcia@cnb.csic.es
lab head
Sergio Ciordia
contact affiliation	Spanish National Center for Biotechnology
contact email	sciordia@cnb.csic.es
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD017769
     1. Label: PRIDE project
     2. Name: The Hypervariable Amino-Terminus of P1 Protease Modulates Potyviral Replication and Host Defense Responses