The mumps virus fusion protein mRNA sequence and homology among the paramyxoviridae proteins.

نویسندگان

  • N Elango
  • T M Varsanyi
  • J Kövamees
  • E Norrby
چکیده

The complete nucleotide sequence of the fusion protein (F) mRNA of the virulent SBL-1 strain of mumps virus has been determined by sequencing cDNA clones and mRNA and confirmed by partially sequencing the genomic RNA. The mRNA was 1721 nucleotides long excluding the poly(A) sequence and had one long open reading frame which encoded a protein of 538 amino acids with a calculated Mr of 58,791. The predicted amino acid sequence had a proteolytic cleavage/activation site, Arg Arg His Lys Arg, cleavage at which yields proteins F2 and F1. The uncleaved protein contained three highly hydrophobic regions: (i) the amino-terminal signal peptide, (ii) the amino-terminal region of F1 and (iii) the carboxy-terminal membrane anchorage domain. There were seven potential N-glycosylation sites, two in F2 and five in F1. Comparison of the virulent strain F protein sequence with that of an avirulent strain of mumps virus showed a difference of 14 amino acids. Among paramyxoviruses, mumps virus fusion protein shows the highest degree of homology with the fusion proteins of simian virus 5 and Newcastle disease virus.

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عنوان ژورنال:
  • The Journal of general virology

دوره 70 ( Pt 4)  شماره 

صفحات  -

تاریخ انتشار 1989