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Journal of Virology, May 1999, p. 3682-3691, Vol. 73, No. 5
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Spliced mRNA Encoding the Murine Cytomegalovirus Chemokine Homolog Predicts a beta  Chemokine of Novel Structure

Margaret R. MacDonald,1,* Mary W. Burney,1 Stuart B. Resnick,2 and Herbert W. Virgin IV2

Department of Pediatrics1 and Center for Immunology and Departments of Pathology and Molecular Biology,2 Washington University School of Medicine, St. Louis, Missouri 63110

Received 9 November 1998/Accepted 22 January 1999

A viral mRNA of the late kinetic class expressed by murine cytomegalovirus (MCMV) contains an open reading frame (ORF) whose predicted protein, designated MCK-1, has homology to beta  chemokines (M. R. MacDonald, X.-Y. Li, and H. W. Virgin IV, J. Virol. 71:1671-1678, 1997). The present study analyzed further the structure of the transcript in infected fibroblast cells. A splicing event removed the MCK-1 stop codon, bringing a downstream ORF into frame with the chemokine homolog and demonstrating that the MCK-1 ORF was an exon of a larger gene. The predicted 31.4-kDa protein, designated MCK-2, contains a putative amino-terminal signal sequence and a beta  chemokine domain, followed by a carboxyl-terminal domain without significant homology to known proteins. Quantitative analysis of mRNA forms in MCMV-infected fibroblast cells at late times after infection indicated that the viral chemokine RNA was predominantly spliced. There was no evidence for expression of RNA encoding either MCK-1 or MCK-2 at immediate early or early times after infection with MCMV. Monoclonal antibodies generated against bacterially expressed MCK-2 recognized multiple proteins in the range of ~30 to ~45 kDa in Western blot analysis of MCK-2 expressed in transfected COS cells. The monoclonal antibodies immunoprecipitated a similar group of proteins in transfected COS cells metabolically labeled with radioactive cysteine. Radiolabelled protein of apparent higher molecular mass was immunoprecipitated from culture medium overlying the transfected cells, suggesting that posttranslationally modified MCK-2 can be secreted. Two proteins with apparent molecular mass suggestive of posttranslational modification were detected by Western blot analysis of cells harvested at late times after infection with MCMV. These studies show that MCMV encodes and expresses a beta  chemokine homolog with a novel predicted structure.

* Corresponding author. Mailing address: Department of Pediatrics, Campus Box 8116, Washington University School of Medicine, Number One Children's Place, St. Louis, MO 63110. Phone: (314) 454-2890. Fax: (314) 454-2836. E-mail: peggym{at}pathbox.wustl.edu.

Journal of Virology, May 1999, p. 3682-3691, Vol. 73, No. 5
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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