A tentative model of formation of structural proteins of tick-borne encephalitis virus (flavivirus).

FEBS letters ·Vol. 200 ·No. 2 ·1986-05-12 ·Pages 314-6

Lyapustin VN, Svitkin YuV, Ugarova TYu, Lashkevich VA, Agol VI

Abstract

The time course of tick-borne encephalitis virus cell-free protein synthesis was studied by using either [35S]-methionine or formyl[35S]methionyl-tRNAMet/f as substrates, and the [35S]methionine-labelled products were compared by fingerprinting tryptic peptides. An intermediate in the protein processing, the polypeptide doublet p36/33, was characterized and a tentative model for flavivirus structural protein synthesis and processing was proposed.

MeSH Terms

Amino Acid Sequence Encephalitis Viruses, Tick-Borne/metabolism Models, Biological RNA, Transfer, Amino Acyl/metabolism RNA, Transfer, Met Sulfur Radioisotopes Viral Proteins/biosynthesis Viral Structural Proteins

Chemicals

RNA, Transfer, Amino Acyl RNA, Transfer, Met Sulfur Radioisotopes Viral Proteins Viral Structural Proteins tRNA, formylmethionine-

Authors & Affiliations

5 authors, click to expand affiliations / ORCID

Lyapustin V N

Svitkin YuV

Ugarova TYu

Lashkevich V A

Agol V I

Article Info

Journal

FEBS letters

Abbr.

FEBS Lett

ISSN

0014-5793

DOI

10.1016/0014-5793(86)81159-0

Published

1986-05-12

Pages

314-6

Language

English

Region

England

NLM ID

0155157

Subset

External Links

PubMed source DOI: 10.1016/0014-5793(86)81159-0 View journal details

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A tentative model of formation of structural proteins of tick-borne encephalitis virus (flavivirus).

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