PROTEOLYTIC CLEAVAGE OF INFLUENZA-VIRUS HEMAGGLUTININS - PRIMARY STRUCTURE OF THE CONNECTING PEPTIDE BETWEEN HA1 AND HA2 DETERMINES PROTEOLYTIC CLEAVABILITY AND PATHOGENICITY OF AVIAN INFLUENZA-VIRUSES
PROTEOLYTIC CLEAVAGE OF INFLUENZA-VIRUS HEMAGGLUTININS - PRIMARY STRUCTURE OF THE CONNECTING PEPTIDE BETWEEN HA1 AND HA2 DETERMINES PROTEOLYTIC CLEAVABILITY AND PATHOGENICITY OF AVIAN INFLUENZA-VIRUSES
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DOI：
10.1016/0042-6822(81)90201-4
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发表时间：
1981-01-01
期刊：
影响因子：
3.7
通讯作者：
ROTT, R
中科院分区：
文献类型：
--
作者：
BOSCH, FX;GARTEN, W;ROTT, R
The structural basis for the different proteolytic cleavability of influenza virus hemagglutinin (HA) was investigated with a group of pathogenic and nonpathogenic avian influenza viruses belonging to the antigenic subtype H7 (Hav1). Infected cell [chick embryo] lysates or lystates of purified virus particles were subjected to 2-dimenshional gel electrophoresis. The 1st dimension, isoelectric focusing, was done under nonreducing conditions, the 2nd dimension, SDS-PAGE [sodium dodecyl sulfate-polyacrylamide gel electrophoresis], under reducing conditions. The amino acid sequence of the connecting peptide between HA1 and HA2 determines proteolytic cleavability by a trypsin-like cellular enzyme. Upon proteolytic cleavage of HA of pathogenic strains, peptides of differing positive charge were eliminated. These HA have significantly more basic connecting peptides than HA of nonpathogenic viruses. HA of nonpathogenic H7 strains appear to have a connecting peptide similar to the human influenza viruses, since treatment of these viruses with trypsin results in a similar small charge shift which probably corresponds to the elimination of 1 basic amino acid. The primary structure of the connecting peptide determines biological activation and therapy pathogenicity of these viruses.
