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Nucleic Acids Research, 1985, Vol. 13, No. 5 1559-1574
© 1985

Articles

Respiratory syncytial virus fusion glycoprotein: nucleotide sequence of mRNA, identification of cleavage activation site and amino acid sequence of N-terminus of F1 subunit

Narayanasamy Elango, Masanobu Satake, John E. Coligan1, Erling Norrby2, Ena Camargo and Sundararajan Venkatesan*

Laboratory of Infectious Diseases Bethesda, MD 20205 1Laboratory of Immunogenetics, National Institute of Allergy and Infectious Diseases Bethesda, MD 20205 2Department of Virology, Bacteriological Laboratory and Karolinska Institute, School of Medicine 5-10521, Stockholm, Sweden

*To whom correspondence should be addressed

Received December 12, 1984. Accepted February 5, 1985.

The amino acid sequence of respiratory syncytial virus fusion protein (Fo) was deduced from the sequence of a partial cDNA clone of mRNA and from the 5' mRNA sequence obtained by primer extension and dideoxysequencing. The encoded protein of 574 amino acids is extremely hydrophobic and has a molecular weight of 63371 daltons. The site of proteolytic cleavage within this protein was accurately mapped by determining a partial amino acid sequence of the N-terminus of the larger subunit (F1) purified by radioimnunoprecipitation using monoclonal antibodies. Alignment of the N-terminus of the F1 subunit within the deduced amino acid sequence of permitted us to identify a sequence of lys-lys-arg-lys-arg-arg at the C-terminus of the smaller N-terminal F2 subunit that appears to represent the cleavage/activation domain. Five potential sites of glycosylation, four within the F2 subunit, were also identified. Three extremely hydrophobic domains are present in the protein; a) the N-terminal signal sequence, b) the N-terminus of the F1 subunit that is analogous to the N-terminus of the paramyxovirus F1 subunit and the HA2 subunit of influenza virus hemagglutinin, and c) the putative membrane anchorage domain near the C-terminus of F1.


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