NUCLEOTIDE-SEQUENCES OF THE GENES ENCODING THE PUTATIVE ATTACHMENT GLYCOPROTEIN(G) OF MOUSE AND TISSUE CULTURE-PASSAGED STRAINS OF PNEUMONIA VIRUS OF MICE

Citation
Js. Randhawa et al., NUCLEOTIDE-SEQUENCES OF THE GENES ENCODING THE PUTATIVE ATTACHMENT GLYCOPROTEIN(G) OF MOUSE AND TISSUE CULTURE-PASSAGED STRAINS OF PNEUMONIA VIRUS OF MICE, Virology, 207(1), 1995, pp. 240-245
Citations number
25
Categorie Soggetti
Virology
Journal title
ISSN journal
00426822
Volume
207
Issue
1
Year of publication
1995
Pages
240 - 245
Database
ISI
SICI code
0042-6822(1995)207:1<240:NOTGET>2.0.ZU;2-7
Abstract
The sequences of the genes encoding the putative attachment (G) protei ns of pathogenic (strain J3666) mouse lung-passaged and nonpathogenic (strain 15) tissue culture-passaged strains of pneumonia virus of mice (PVM) have been determined. In both cases the major polypeptide was s ynthesised from the second open reading frame (ORF), a feature also fo und in the G gene of respiratory syncytial (RS) virus, another pneumov irus. However, the ORFs of the G genes of the two PVM strains were ini tialed at different nucleotide positions in the mRNA and comparison of hydrophobicity profiles revealed the presence of the putative amino-t erminal cytoplasmic domain in the strain J3666 G protein and its absen ce in the predicted G protein of PVM strain 15. In common with the G p rotein of RS virus, the gene product of both PVM strains contained a h igh serine, threonine, and proline content Indirect immunofluorescence analysis of BSC-1 cells expressing the G gene products confirmed the surface location of the proteins. Thus, the absence of a cytoplasmic d omain does not interfere with the translocation of the G protein of PV M strain 15. In vitro translation of mRNA from the two PVM genes direc ted the synthesis of a larger polypeptide with the G gene of PVM strai n J3666 than was seen with the strain 15 G gene. In addition, a second protein was seen with strain J3666 mRNA which was the same size as th e strain 15 G protein. (C) 1995 Academic Press, Inc.