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PMID: 2174359 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

An endoprotease homologous to the blood clotting factor X as a determinant of viral tropism in chick embryo.

The EMBO journal ·Vol. 9 ·No. 12 ·1990-12-00 ·Pages 4189-95

Gotoh B, Ogasawara T, Toyoda T, Inocencio NM, Hamaguchi M, Nagai Y

Abstract

Host cell proteases responsible for activation of viral fusion glycoproteins are an important determinant for spread and tropism of various animal viruses. Exemplifying such proteases for the first time, we isolated an endoprotease from chick embryo, that activates para- and orthomyxovirus fusion glycoproteins by cleaving their precursor proteins at a specific, single arginine site. The protease is a calcium dependent serine protease consisting of two subunits, the 33 kd catalytic chain and the 23 kd chain possibly required for Ca2+ binding, and was found to be highly homologous, if not identical, to the blood clotting factor X(FX), a member of the prothrombin family. Its high efficiency and specificity in cleavage reactions was attributable to the properties characteristic of FX. Its role in vivo was strongly supported by cleavage inhibition in ovo highly selective for this virus group with a specific peptide inhibitor against FX.

MeSH Terms
Amino Acid Sequence Animals Chick Embryo Chickens Factor X/genetics,isolation & purification,metabolism Kinetics Macromolecular Substances Molecular Sequence Data Parainfluenza Virus 1, Human/physiology Sequence Homology, Nucleic Acid Serine Endopeptidases/genetics,isolation & purification,metabolism Viral Fusion Proteins/metabolism
Chemicals
Macromolecular Substances Viral Fusion Proteins Factor X Serine Endopeptidases virus activating protease
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Gotoh B
Research Institute for Disease Mechanism and Control, Nagoya University School of Medicine, Japan.
Ogasawara T
Toyoda T
Inocencio N M
Hamaguchi M
Nagai Y
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1990-12-00
Pages
4189-95
Language
English
Region
England
NLM ID
8208664
PMCID
PMC552195
Subset
IM
External Links
PubMed source PMC Full Text View journal details
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