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Journal of Virology, December 2006, p. 12070-12078, Vol. 80, No. 24
0022-538X/06/$08.00+0     doi:10.1128/JVI.01743-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Mutation of YMYL in the Nipah Virus Matrix Protein Abrogates Budding and Alters Subcellular Localization{triangledown}

Michael J. Ciancanelli and Christopher F. Basler*

Department of Microbiology, Mount Sinai School of Medicine, New York, New York 10029

Received 11 August 2006/ Accepted 19 September 2006

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.

* Corresponding author: Mailing address: Department of Microbiology, Box 1124, Mount Sinai School of Medicine, 1 Gustave L. Levy Place, New York, NY 10029. Phone: (212) 241-4847. Fax: (212) 534-1684. E-mail: chris.basler{at}mssm.edu.

{triangledown} Published ahead of print on 27 September 2006.

Journal of Virology, December 2006, p. 12070-12078, Vol. 80, No. 24
0022-538X/06/$08.00+0     doi:10.1128/JVI.01743-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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