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J Virol, February 1998, p. 1103-1107, Vol. 72, No. 2
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

The Major Site of Phosphorylation within the Rous Sarcoma Virus MA Protein Is Not Required for Replication

Timothy D. Nelle,^1, Michael F. Verderame,² Jonathan Leis,³ and John W. Wills^1,*

Department of Microbiology and Immunology,¹ and Department of Medicine,² Pennsylvania State University College of Medicine, Hershey, Pennsylvania 17033, and Department of Biochemistry, Case Western Reserve University School of Medicine, Cleveland, Ohio 44106³

Received 21 July 1997/Accepted 22 October 1997

About one-third of the MA protein in Rous sarcoma virus (RSV) is phosphorylated. Previous analyses of this fraction have suggested that serine residues 68 and 106 are the major sites of phosphorylation. As a follow-up to that study, we have characterized mutants which have these putative phosphorylation sites changed to alanine, either separately or together. None of the substitutions (S68A, S106A, or S68/106A) had an effect on the budding efficiency or infectivity of the virus. Upon examination of the ³²P-labeled viral proteins, we found that the S68A substitution did not affect phosphorylation in vivo at all. In contrast, the S106A substitution prevented all detectable phosphorylation of MA, suggesting that there is only one major site of phosphorylation in MA. We also found that the RSV MA protein is phosphorylated on tyrosine, but the amount was low and detectable only with large numbers of virions and an antibody specific for phosphotyrosine.

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^* Corresponding author. Mailing address: Department of Microbiology and Immunology, College of Medicine, Pennsylvania State University, Hershey, PA 17033. Phone: (717) 531-3528. Fax: (717) 531-6522. E-mail: jwills{at}bcmic.hmc.psu.edu.

Present address: Virology Division, United States Army Medical Research Institute of Infectious Diseases, Fort Detrick, MD 21702.

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