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Author Ight, G. Spe ♦ Westaway, E. G.
Source CiteSeerX
Content type Text
File Format PDF
Subject Domain (in DDC) Computer science, information & general works ♦ Data processing & computer science
Subject Keyword Nine Protein ♦ Carboxy-terminal Analysis ♦ Intracellular Core Protein ♦ Flavivirus Kunjin ♦ Lysine Residue ♦ Intracellular Equivalent ♦ Common Carboxy Terminus Lys-arg ♦ Flavivirus Consensus Site ♦ Carboxy-terminal Lys ♦ Several Specie ♦ Nucleotide Sequence ♦ Anomalous Electrophoretic Migration ♦ Yellow Fever ♦ Virion Protein ♦ Carboxy Terminus ♦ Amino Acid Residue ♦ Inthe Viral Polyprotein ♦ Kunjin Virus ♦ Internal Lys-arg Site ♦ Long Open Reading Frame ♦ Kun Virus ♦ Gel System ♦ Apparent Internal Cleavage ♦ Previous N-terminal Amino Acid ♦ Putative Internal Cleavage Site ♦ Theoretical Amount ♦ Cleavage Site ♦ Dengue Fever ♦ Theoretical Mr
Abstract Nine proteins pecified by Kunjin virus were labelled with [3H]lysine and digested with carboxypeptidase B which specifically cleaves carboxy-terminal Lys or Arg. The theoretical amount of [3H]lysine was released from the non-structural (ns) proteins NS2A, NS2B, NS3 and NS4B, which have a common carboxy terminus Lys-Arg deduced from cleavage sites established inthe viral polyprotein by previous N-terminal amino acid analyses. This is a flavivirus consensus site, always followed by Gly, Ala or Ser. These results indicate that no truncations had occurred despite anomalous electrophoretic migrations of NS2A, NS2B and NS4B observed in some gel systems. No [3H]lysine was released from NS4A or NS5 which terminate in Ala and Leu, respectively, thus establishing that NS5 (observed M r 98000, theoretical Mr 103600) was not cleaved post-translationally at any internal Lys-Arg site. Unexpectedly, [3H]lysine residues were apparently released from P14(C), the intracellular equivalent of virion C protein which terminates in Ala (adjacent to he established N-terminus of prM). However, a putative internal cleavage site (Lys-Arg~,Gly) exists 18 residues upstream from the carboxy terminus of C, prior to the transmembrane spanning domain. Apparent internal cleavage in the cytosol at this site to produce P 14(C) would expose [3H]lysine residues to carboxypeptidase B, and account for the previously observed ifferences in size and composition between C and P14(C). Kunjin (KUN) virus is a member of the Flaviviridae, a family of arthropod-borne, small, enveloped, RNA viruses which cause yellow fever, dengue fever and other diseases in man. The nucleotide sequence is known for several species including KUN virus and the coding region comprises one long open reading frame of about 3400 amino acid residues, representing three structural nd seven non-structural (ns) proteins (Castle et al., 1986; Deubel et al., 1988; Hahn et
Educational Role Student ♦ Teacher
Age Range above 22 year
Educational Use Research
Education Level UG and PG ♦ Career/Technical Study
Publisher Date 1989-01-01