PXD019208

PXD019208 is an original dataset announced via ProteomeXchange.

Title	Protein S-Nitrosylation of host and viral proteins upon fibroblast infection with Human Cytomegalovirus
Description	Human Cytomegalovirus (HCMV) is a ubiquitous pathogen that has co-evolved with its host and in doing so, is highly efficient in undermining antiviral responses that limit successful infections. As a result, HCMV infections are highly problematic in individuals with weakened or underdeveloped immune systems including transplant recipients and newborns. Understanding how HCMV controls the microenvironment of an infected cell so as to favor productive replication is of critical importance. To this end, we took an unbiased proteomics approach to identify the highly reversible, stress induced, post-translational modification (PTM), protein S-nitrosylation, on viral proteins to determine the biological impact on viral replication. We identified protein S-nitrosylation of 13 viral proteins during infection of highly permissive fibroblasts. One of these proteins, pp71, is critical for efficient viral replication, as it undermines host antiviral responses, including STING activation. By exploiting site-directed mutagenesis of the specific amino acids we identified in pp71 as protein S-nitrosylated, we found this pp71 PTM diminishes its ability to undermine antiviral responses induced by the STING pathway. Our results suggest a model in which protein S-nitrosylation may function as a host response to viral infection that limits viral spread.
HostingRepository	PRIDE
AnnounceDate	2020-07-03
AnnouncementXML	Submission_2020-09-28_00:30:38.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Ebbing de Jong
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	biotinylated residue
Instrument	LTQ Orbitrap Elite

Revision	Datetime	Status	ChangeLog Entry
0	2020-05-14 18:57:38	ID requested
1	2020-07-02 23:26:11	announced
⏵ 2	2020-09-28 00:30:39	announced	2020-09-28: Updated publication reference for PubMed record(s): 32581105.

Nukui M, Roche KL, Jia J, Fox PL, Murphy EA, Protein S-Nitrosylation of Human Cytomegalovirus pp71 Inhibits Its Ability To Limit STING Antiviral Responses. J Virol, 94(17):(2020) [pubmed]

submitter keyword: HCMV, cytomegalovirus, Protein S-Nitrosylation

Eain Murphy
contact affiliation	Associate Professor Microbiology and Immunology Department Upstate Medical University Weiskotten Hall Rm. 2273 766 Irving Avenue Syracuse, NY 13210 Tel 315.464.5870
contact email	murphye1@upstate.edu
lab head
Ebbing de Jong
contact affiliation	SUNY Upstate Medical University
contact email	dejonge@upstate.edu
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2020/07/PXD019208

PRIDE project URI

• PRIDE
  1. PXD019208
     1. Label: PRIDE project
     2. Name: Protein S-Nitrosylation of host and viral proteins upon fibroblast infection with Human Cytomegalovirus