Mutation of YMYL in the Nipah virus matrix protein abrogates budding and alters subcellular localization

Michael J. Ciancanelli, Christopher F. Basler

Research output: Contribution to journalArticlepeer-review

127 Scopus citations

Abstract

Matrix (M) proteins reportedly direct the budding of paramyxoviruses from infected cells. In order to begin to characterize the assembly process for the highly lethal, emerging paramyxovirus Nipah virus (NiV), we have examined the budding of NiV M. We demonstrated that expression of the NiV M protein is sufficient to produce budding virus-like particles (VLPs) that are physically and morphologically similar to NiV. We identified in NiV M a sequence, YMYL, with similarity to the YPDL late domain found in the equine infectious anemia virus Gag protein. When the YMYL within NiV M was mutated, VLP release was abolished and M was relocalized to the nucleus, but the mutant M proteins retained oligomerization activity. When YMYL was fused to a late-domain mutant of the Ebola virus VP40 matrix protein, VP40 budding was restored. These results suggest that the YMYL sequence may act as a trafficking signal and a late domain for NiV M.

Original languageEnglish
Pages (from-to)12070-12078
Number of pages9
JournalJournal of Virology
Volume80
Issue number24
DOIs
StatePublished - Dec 2006

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