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1 Department of Microbiology, University of Western Australia, Queen Elizabeth II Medical Centre, Nedlands, Western Australia, 6009, Australia
and2 Laboratory of Molecular Biology, MRC, Hills Road, and Division of Virology, Department of Pathology, University of Cambridge, Cambridge CB2 2QH, U.K.
DNA sequence analysis of the genome of the Smith strain of murine cytomegalovirus (MCMV) revealed an open reading frame (ORF) with amino acid sequence identity to glycoprotein L (gL) of other herpesviruses. The ORF is 822 bp in size and has the capacity to encode a protein of 274 amino acids. It has significant identity with the gL genes of human CMV and human herpesvirus 6. The coding sequence of the gL gene of MCMV strain K181 was also determined, and expressed in Escherichia coli as a fusion protein with glutathione S-transferase using the pGEX expression system. Two antibody-binding regions were identified on the basis of the reactivity of a series of truncated gL constructs with anti-MCMV antibodies. One was mapped to residues 1 to 38 and the other between residues 230 and 274. Polyclonal antibodies specific to gL were raised against the full-length gL fusion protein. The antisera were shown to react with a 46K protein present in purified virions by Western blotting. Treatment of purified virions with endoglycosidase-H or -F resulted in reductions in Mr of the 46K species to 42K and 31K, respectively. The antisera did not exhibit any neutralizing activity in a plaque reduction assay.
Present address: Department of Microbiology, University of Western Australia, Queen Elizabeth II Medical Centre, Nedlands, Western Australia, 6009, Australia.
Present address: Department of Virology, Westmead Hospital, Sydney, 2145, Australia.
Received 9 May 1994;
accepted 19 July 1994.
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