Skip to main page content
Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
, 387 (4), 467-75

Identification of Trypsin I as a Candidate for Influenza A Virus and Sendai Virus Envelope Glycoprotein Processing Protease in Rat Brain

Affiliations

Identification of Trypsin I as a Candidate for Influenza A Virus and Sendai Virus Envelope Glycoprotein Processing Protease in Rat Brain

Trong Quang Le et al. Biol Chem.

Erratum in

  • Biol Chem. 2006 Sep;387(9):1305

Abstract

Extracellular cleavage of virus envelope fusion glycoprotein hemagglutinin (HA0) by host trypsin-like proteases is a prerequisite for the infectivity and pathogenicity of human influenza A viruses and Sendai virus. The common epidemic influenza A viruses are pneumotropic, but occasionally cause encephalopathy or encephalitis, although the HA0 processing enzyme in the brain has not been identified. In searching for the brain processing proteases, we identified a processing enzyme in rat brain that was inducible by infection with these viruses. The purified enzyme exhibited an apparent molecular mass of approximately 22 kDa on SDS-PAGE and the N-terminal amino acid sequence was consistent with that of rat pancreatic trypsin I. Its substrate specificities and inhibition profiles were the same as those of pancreatic trypsin I. In situ hybridization and immunohistochemical studies on trypsin I distribution revealed heavy deposits in the brain capillaries, particularly in the allocortex, as well as in clustered neuronal cells of the hippocampus. The purified enzyme efficiently processed the HA0 of human influenza A virus and the fusion glycoprotein precursor of Sendai virus. Our results suggest that trypsin I in the brain potentiates virus multiplication in the pathogenesis and progression of influenza-associated encephalopathy or encephalitis.

Similar articles

See all similar articles

Cited by 13 PubMed Central articles

See all "Cited by" articles

Publication types

MeSH terms

LinkOut - more resources

Feedback