Molecular basis of proteolytic activation of Sendai virus infection and the defensive compounds for infection

Biological Chemistry
H KidoT Towatari

Abstract

It has been proposed that the pathogenicity of Sendai virus is primarily determined by a host cellular protease(s) that activates viral infectivity by proteolytic cleavage of envelope fusion glycoproteins. We isolated a trypsin-like serine protease, tryptase Clara, localized in and secreted from Clara cells of the bronchial epithelium of rats. The enzyme specifically cleaved the precursor of fusion glycoprotein F0 of Sendai virus at residue Arg116 in the consensus cleavage motif, Gln(Glu)-X-Arg, resulting in the presentation of the membrane fusion domain in the amino-terminus of the F1 subunit. Administration of an antibody against tryptase Clara in the airway significantly inhibited the activation of progeny virus and multiple cycles of viral replication, thus reducing the mortality rate. These findings indicate that tryptase Clara in the airway is a primary determinant of Sendai virus infection and that proteolytic activation occurs extracellularly. We identified two cellular inhibitory compounds against tryptase Clara in bronchial lavage. One was a mucus protease inhibitor, a major serine protease inhibitor of granulocyte elastase in the lining fluids of the human respiratory tract, and the other was a pulmonary surfactant w...Continue Reading

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Citations

Aug 31, 2000·Annual Review of Biochemistry·J J Skehel, D C Wiley
Jul 13, 2001·Pulmonary Pharmacology & Therapeutics·T M Cocks, J D Moffatt
Sep 6, 2017·Expert Opinion on Drug Discovery·Woo-Jin Shin, Baik Lin Seong

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