Nucleic Acids Research, 1985, Vol. 13, No. 21 7795-7812
© 1985
Articles |
Respiratory syncytial virus envelope glycoprotein (G) has a novel structure
Laboratory of Infectious Diseases, National Institute of Allergy and Infectious Diseases Bethesda, MD 20205 1Basic Research Program, Litton Bionetics, Inc., FCRF Frederick, MD 21701 2Laboratory of Immunogenetics, National Institute of Allergy and Infectious Diseases Bethesda, MD 20205 3Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases Bethesda, MD 20205 4Department of Virology, State Bacteriological Laboratory and Karolinska Institute S-105 21, Stockholm, Sweden 5Laboratory of Molecular Microbology, National Institute of Allergy and Infectious Diseases Bethesda, MD 20205
*To whom correspondence should be addressed at LMM/NIAID, Bldg. 550, Frederick Cancer Research Facility, Frederick, MD 21701, USA
Received May 6, 1985. Revised October 7, 1985. Accepted October 7, 1985.
Amino acid sequence of human respiratory syncytial virus envelope glycoprotein (G) was deduced from the DNA sequence of a recombinant plasmid and confirmed by limited amino add microsequendng of purified 90K G protein. The calculated molecular mass of the protein encoded by the only long open reading frame of 298 amino acids was 32,588 daltons and was somewhat smaller than the 36K polypeptide translated in vitro from mRNA selected by this plasmid. Inspection of the sequence revealed a single hydrophobic domain of 23 amino acids capable of membrane insertion at 41 residues from the N-terminus. There was no N-terminal signal sequence and the hydrophilic N-terminal 20 residues probably represent the cytoplasmic tail of the protein. The N-terminally oriented membrane insertion was somewhat analogous to paramyxovirus hemagglutinin-neuraminidase (HN) and influenza neuraminidase (NA). The protein was moderately hydrophilic and rich in hydroxy-amino adds. It was both N- and O-glycosylated with the latter contributing significantly to the net molecular mass 90K.
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