{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["78(11)"],"submitter":["Shaw ML"],"pubmed_abstract":["In previous reports it was demonstrated that the Nipah virus V and W proteins have interferon (IFN) antagonist activity due to their ability to block signaling from the IFN-alpha/beta receptor (J. J. Rodriguez, J. P. Parisien, and C. M. Horvath, J. Virol. 76:11476-11483, 2002; M. S. Park et al., J. Virol. 77:1501-1511, 2003). The V, W, and P proteins are all encoded by the same viral gene and share an identical 407-amino-acid N-terminal region but have distinct C-terminal sequences. We now show that the P protein also has anti-IFN function, confirming that the common N-terminal domain is responsible for the antagonist activity. Truncation of this N-terminal domain revealed that amino acids 50 to 150 retain the ability to block IFN and to bind STAT1, a key component of the IFN signaling pat"],"journal":["Journal of virology"],"pagination":["5633-41"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC415790"],"repository":["biostudies-literature"],"pubmed_title":["Nipah virus V and W proteins have a common STAT1-binding domain yet inhibit STAT1 activation from the cytoplasmic and nuclear compartments, respectively."],"pmcid":["PMC415790"],"pubmed_authors":["Garcia-Sastre A","Palese P","Basler CF","Shaw ML"],"additional_accession":[]},"is_claimable":false,"name":"Nipah virus V and W proteins have a common STAT1-binding domain yet inhibit STAT1 activation from the cytoplasmic and nuclear compartments, respectively.","description":"In previous reports it was demonstrated that the Nipah virus V and W proteins have interferon (IFN) antagonist activity due to their ability to block signaling from the IFN-alpha/beta receptor (J. J. Rodriguez, J. P. Parisien, and C. M. Horvath, J. Virol. 76:11476-11483, 2002; M. S. Park et al., J. Virol. 77:1501-1511, 2003). The V, W, and P proteins are all encoded by the same viral gene and share an identical 407-amino-acid N-terminal region but have distinct C-terminal sequences. We now show that the P protein also has anti-IFN function, confirming that the common N-terminal domain is responsible for the antagonist activity. Truncation of this N-terminal domain revealed that amino acids 50 to 150 retain the ability to block IFN and to bind STAT1, a key component of the IFN signaling pat","dates":{"release":"2004-01-01T00:00:00Z","publication":"2004 Jun","modification":"2025-04-03T22:33:09.321Z","creation":"2019-03-27T00:50:28Z"},"accession":"S-EPMC415790","cross_references":{"pubmed":["15140960"],"doi":["10.1128/JVI.78.11.5633-5641.2004","10.1128/jvi.78.11.5633-5641.2004"]}}