Amino-terminal amino acid sequences of structural proteins of three flaviviruses

John R. Bell, Richard M. Kinney, Dennis W. Trent, Edith M. Lenches, Lynn Dalgarno, James H. Strauss

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Abstract

N-terminal amino acid sequences of structural proteins of three flaviviruses, yellow fever, St. Louis encephalitis, and dengue-2 viruses, have been obtained. The glycoproteins of these three viruses are 52-60% conserved in the region sequenced, depending upon which pair of viruses are compared, and 40% of the amino acids are invariant in all three viruses. Thus, flaviviruses are closely related and have in all probability descended from a common ancestor. Furthermore, residues important in the secondary structure of proteins are conserved, suggesting that the overall conformation of the glycoproteins is the same in all three viruses while considerable variation in the primary sequence can be accommodated. The N-terminal regions of the nucleocapsid proteins of yellow fever and St. Louis encephalitis viruses show markedly less homology (25%) and this region is highly basic with one-quarter (yellow fever) or one-third (St. Louis encephalitis) of the residues being lysine or arginine. N-terminal sequences for the M protein of yellow fever and for NV2(GP19) of St. Louis encephalitis viruses are also reported.

Original languageEnglish (US)
Pages (from-to)224-229
Number of pages6
JournalVirology
Volume143
Issue number1
DOIs
StatePublished - May 1985

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ASJC Scopus subject areas

  • Virology

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Bell, J. R., Kinney, R. M., Trent, D. W., Lenches, E. M., Dalgarno, L., & Strauss, J. H. (1985). Amino-terminal amino acid sequences of structural proteins of three flaviviruses. Virology, 143(1), 224-229. https://doi.org/10.1016/0042-6822(85)90110-2