title: Analysis of the mechanism of influenza B virus inactivation by guinea pig serum.
abstract: Normal guinea pig serum lacking detectable antiviral antibody inactivated influenza B virus via the classical complement pathway. This virus inactivation appeared to result from the steric hindrance of HA activity by the association with the virus of serum proteins presumed to be complement components. Trypsin digestion of the associated proteins fully restored the HA activity but not infectivity. It was found that the virus underwent minor disruption of the envelope and degradation of M1 protein and genomic RNA.
authors.affiliation: Laboratory of Virology, Nagoya University School of Medicine, Japan.
authors.forename: F
authors.initials: F
authors.lastname: Yamamoto Goshima
authors.forename: K
authors.initials: K
authors.lastname: Maeno
authors.forename: S
authors.initials: S
authors.lastname: Shibata
authors.forename: H
authors.initials: H
authors.lastname: Mano
authors.forename: T
authors.initials: T
authors.lastname: Suzuki
authors.forename: Y
authors.initials: Y
authors.lastname: Nishi
mesh_terms: D000818:Animals; D003167:Complement Activation; D006168:Guinea Pigs; D019267:Hemagglutinin Glycoproteins, Influenza Virus; D006389:Hemagglutinins, Viral / Q000276:immunology; D009981:Influenza B virus / Q000276:immunology* / Q000648:ultrastructure; D012367:RNA, Viral / Q000378:metabolism; D012260:Ribonucleases / Q000502:physiology; D014357:Trypsin; D014763:Viral Matrix Proteins / Q000276:immunology
chemical_list: D019267:Hemagglutinin Glycoproteins, Influenza Virus; D006389:Hemagglutinins, Viral; D012367:RNA, Viral; D014763:Viral Matrix Proteins; D012260:Ribonucleases; D014357:Trypsin