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PMID: 6441705 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Inhibition of proteolytic cleavage of the hemagglutinin of influenza virus by the calcium-specific ionophore A23187.

The EMBO journal ·Vol. 3 ·No. 12 ·1984-12-01 ·Pages 2911-5

Klenk HD, Garten W, Rott R

Abstract

At calcium-specific ionophore A23187 concentrations of approximately 0.25 microM [which still allow assembly and release of fowl plague virus (FPV) particles] post-translational proteolytic cleavage of the viral hemagglutinin precursor HA into the fragments HA1 and HA2 is inhibited. The resulting virus particles with uncleaved hemagglutinin, that cannot be obtained under normal conditions, provide a suitable substrate for in vitro assays of the protease sensitivity of the FPV hemagglutinin. Proteolytic activation is accomplished with trypsin. Treatment with cathepsin B at low pH yields aberrant cleavage products suggesting that the cellular cleavage enzyme is not of lysosomal origin. A protease that cleaves the FPV hemagglutinin in the correct place can be detected in lysates of MDBK cells. This enzyme is calcium dependent and has a neutral pH optimum.

MeSH Terms
Animals Calcimycin/pharmacology Cattle Cell Line Cricetinae Hemagglutination Tests Humans Influenza A virus/drug effects,genetics Kidney Thermolysin/metabolism Viral Envelope Proteins/analysis Viral Matrix Proteins Viral Plaque Assay Virus Replication/drug effects
Chemicals
M-protein, influenza virus Viral Envelope Proteins Viral Matrix Proteins Calcimycin Thermolysin
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Klenk H D
Garten W
Rott R
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38 references, click to expand
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1984-12-01
Pages
2911-5
Language
English
Region
England
NLM ID
8208664
PMCID
PMC557788
Subset
IM
External Links
PubMed source PMC Full Text View journal details
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