Literature DB >> 3008425

Partial N-terminal amino acid sequences of three nonstructural proteins of two flaviviruses.

C M Rice, R Aebersold, D B Teplow, J Pata, J R Bell, A V Vorndam, D W Trent, M W Brandriss, J J Schlesinger, J H Strauss.   

Abstract

Partial N-terminal amino acid sequences for the three largest nonstructural proteins of two flaviviruses, yellow fever virus and St. Louis encephalitis virus, have been obtained. The determined sequences of these proteins exhibit significant amino acid sequence homology, and allow the positioning of these three nonstructural proteins in the polyprotein sequence deduced from the nucleotide sequence of yellow fever virus (C. M. Rice, E. M. Lenches, S. R. Eddy, S. J. Shin, R. L. Sheets, and J. H. Strauss, 1985, Science 229, 726-733.) The deduced start points support the hypothesis that the N terminus of nonstructural glycoprotein NS1 results from cleavage by signalase, whereas the N termini of NS3 and NS5 result from cleavages following double basic residues that are flanked by amino acids with short side chains.

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Year:  1986        PMID: 3008425     DOI: 10.1016/0042-6822(86)90098-x

Source DB:  PubMed          Journal:  Virology        ISSN: 0042-6822            Impact factor:   3.616


  15 in total

1.  Both nonstructural proteins NS2B and NS3 are required for the proteolytic processing of dengue virus nonstructural proteins.

Authors:  B Falgout; M Pethel; Y M Zhang; C J Lai
Journal:  J Virol       Date:  1991-05       Impact factor: 5.103

2.  Proper processing of dengue virus nonstructural glycoprotein NS1 requires the N-terminal hydrophobic signal sequence and the downstream nonstructural protein NS2a.

Authors:  B Falgout; R Chanock; C J Lai
Journal:  J Virol       Date:  1989-05       Impact factor: 5.103

3.  Processing of the yellow fever virus nonstructural polyprotein: a catalytically active NS3 proteinase domain and NS2B are required for cleavages at dibasic sites.

Authors:  T J Chambers; A Grakoui; C M Rice
Journal:  J Virol       Date:  1991-11       Impact factor: 5.103

4.  In vitro processing of dengue virus type 2 nonstructural proteins NS2A, NS2B, and NS3.

Authors:  F Preugschat; C W Yao; J H Strauss
Journal:  J Virol       Date:  1990-09       Impact factor: 5.103

5.  Evidence that the N-terminal domain of nonstructural protein NS3 from yellow fever virus is a serine protease responsible for site-specific cleavages in the viral polyprotein.

Authors:  T J Chambers; R C Weir; A Grakoui; D W McCourt; J F Bazan; R J Fletterick; C M Rice
Journal:  Proc Natl Acad Sci U S A       Date:  1990-11       Impact factor: 11.205

6.  The envelope glycoprotein domain III of Dengue virus type 2 induced the expression of anticoagulant molecules in endothelial cells.

Authors:  Lien-Cheng Chen; Trai-Ming Yeh; Yi-Ying Lin; Yi-Fen Wang; Shu-Jem Su; Chang-Yu Chen; Kuan-Hua Lin; Miao-Chen Chou; Huey-Wen Shyu
Journal:  Mol Cell Biochem       Date:  2010-06-05       Impact factor: 3.396

Review 7.  Proteases involved in the processing of viral polyproteins. Brief review.

Authors:  J Wellink; A van Kammen
Journal:  Arch Virol       Date:  1988       Impact factor: 2.574

8.  Processing of yellow fever virus polyprotein: role of cellular proteases in maturation of the structural proteins.

Authors:  A Ruiz-Linares; A Cahour; P Després; M Girard; M Bouloy
Journal:  J Virol       Date:  1989-10       Impact factor: 5.103

9.  Cleavage of the dengue virus polyprotein at the NS3/NS4A and NS4B/NS5 junctions is mediated by viral protease NS2B-NS3, whereas NS4A/NS4B may be processed by a cellular protease.

Authors:  A Cahour; B Falgout; C J Lai
Journal:  J Virol       Date:  1992-03       Impact factor: 5.103

10.  High-level expression of the tick-borne encephalitis virus NS1 protein by using an adenovirus-based vector: protection elicited in a murine model.

Authors:  S C Jacobs; J R Stephenson; G W Wilkinson
Journal:  J Virol       Date:  1992-04       Impact factor: 5.103

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