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Journal of Virology, July 2004, p. 7823-7827, Vol. 78, No. 14
0022-538X/04/$08.00+0 DOI: 10.1128/JVI.78.14.7823-7827.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.
Functional Analysis of Late-Budding Domain Activity Associated with the PSAP Motif within the Vesicular Stomatitis Virus M Protein
Takashi Irie,1 Jillian M. Licata,1 Himangi R. Jayakar,2 Michael A. Whitt,2,3 Peter Bell,4 and Ronald N. Harty1*
Department of Pathobiology, School of Veterinary Medicine,1
Cell Morphology Core, Gene Therapy Program, Division of Medical Genetics, School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104,4
GTx, Inc.,2
Department of Molecular Sciences, University of Tennessee Health Science Center, Memphis, Tennessee 381633
Received 21 January 2004/
Accepted 24 February 2004
A PPPY motif within the M protein of vesicular stomatitis virus (VSV) functions as a late-budding domain (L-domain); however, L-domain activity has yet to be associated with a downstream PSAP motif. VSV recombinants with mutations in the PPPY and/or PSAP motif were recovered by reverse genetics and examined for growth kinetics, plaque size, and budding efficiency by electron microscopy. Results indicate that unlike the PPPY motif, the PSAP motif alone does not possess L-domain activity. Finally, the insertion of the human immunodeficiency virus type 1 p6 L-domain and flanking sequences into the PSAP region of M protein rescued budding of a PPPY mutant of VSV to wild-type levels.
* Corresponding author. Mailing address: Department of Pathobiology, School of Veterinary Medicine, University of Pennsylvania, 3800 Spruce St., Philadelphia, PA 19104-6049. Phone: (215) 573-4485. Fax: (215) 898-7887. E-mail:
rharty{at}vet.upenn.edu.
Journal of Virology, July 2004, p. 7823-7827, Vol. 78, No. 14
0022-538X/04/$08.00+0 DOI: 10.1128/JVI.78.14.7823-7827.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.
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