Virucidal Activity and Viral Protein Modification by Myeloperoxidase: A Candidate for Defense Factor of Human Polymorphonuclear Leukocytes against Influenza Virus Infection

Influenza virus (IFV) was inactivated by treatment with degranulated fluid (DF) or myeloperoxidase (MPO) from human polymorphonuclear leukocytes in the presence of H20 2. Hemagglutinin and neuraminidase activities of the virus were also reduced by DF treatment. In addition, treatment with OF or MPO...

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Bibliographic Details
Published in:The Journal of infectious diseases 1991-07, Vol.164 (1), p.8-14
Main Authors: Yamamoto, Kiichi, Miyoshi-Koshio, Toshiko, Utsuki, Yoshio, Mizuno, Satoshi, Suzuki, Kazuo
Format: Article
Language:English
Subjects:
Biological and medical sciences
Cell Degranulation
Cells, Cultured
Densitometry
Electrophoresis, Polyacrylamide Gel
Enzymes
Fundamental and applied biological sciences. Psychology
Gels
Hemagglutinins, Viral - immunology
Humans
Infections
Influenza A virus - drug effects
Influenza A virus - immunology
Major Articles
Microbiology
Neuraminidase - immunology
Neutrophils
Neutrophils - enzymology
Neutrophils - immunology
Orthomyxoviridae
Peroxidase - pharmacology
Radioactive decay
Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains
Viral infections
Viral Matrix Proteins - drug effects
Viral Matrix Proteins - immunology
Viral proteins
Viral Proteins - drug effects
Viral Proteins - immunology
Virions
Virology
Viruses
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Description
Summary:Influenza virus (IFV) was inactivated by treatment with degranulated fluid (DF) or myeloperoxidase (MPO) from human polymorphonuclear leukocytes in the presence of H20 2. Hemagglutinin and neuraminidase activities of the virus were also reduced by DF treatment. In addition, treatment with OF or MPO in the presence of H20 2 resulted in delayed migration of viral proteins in SOS-PAGE, indicating extensively modified viral proteins. Parallel with this aberrant migration, the radioactivity of each protein band on SOS-PAGE using [35S]methioninelabeled IFV was greatly reduced. Moreover, some of the modified viral protein did not migrate. A small amount of acid-soluble degraded viral peptide was also generated. The modification of the proteins was exhibited in all major viral proteins, including the inner proteins in the envelope. These results suggest that inactivation of IFV and protein modification by OF is due to MPO present in OF.
ISSN:0022-1899
1537-6613
DOI:10.1093/infdis/164.1.8