Antigenic alteration of influenza B virus associated with loss of a glycosylation site due to host-cell adaptation.
Effects of host-cell adaptation of the hemagglutinin (HA) protein were evaluated by the analyses of four pairs of recent influenza B field isolates, each pair consisting of an Madin Darby canine kidney (MDCK)- and an embryonated chicken egg-derived isolates from the same clinical specimen. Among the isolates examined, all of the MDCK-derived isolates retained glycosylation site at amino acid 197 on the HA1 molecule, whereas three egg-derived isolates lost it. Antigenic difference in the HA molecule between an MDCK- and an egg-derived isolates of three of these pairs was demonstrated to be associated with the glycosylation 197. Replication of the MDCK-derived isolates was suppressed in eggs, suggesting that the presence of the glycosylation 197 was disadvantageous to replication in eggs. Virus-binding affinity assay revealed that the loss of carbohydrate chain did not significantly alter the preferential recognition of sialic acid linkage. Immunogenicity and vaccine efficacy of an MDCK- and an egg-derived clones of B/Akita/27/2001, the former retained the glycosylation 197 and the latter lost it, were compared in a hamster model. When formalin-inactivated whole virion vaccines prepared from the paired isolates were administered into hamsters, no significant difference between them was observed in protective ability against challenges by the homologous and heterologous clones. Implication of the egg adaptation of influenza virus to antigenic surveillance of the field isolates as well as the selection of vaccine strains, and possibility of the involvement of the viral protein(s) other than the HA in the egg adaptation were discussed.
Department of Virology III, National Institute of Infectious Diseases, Tokyo, Japan. taksaito@nih.go.jp
Takehiko
T
Saito
Yoko
Y
Nakaya
Takashi
T
Suzuki
Reiko
R
Ito
Toshinori
T
Saito
Hiroyuki
H
Saito
Shinichi
S
Takao
Keiji
K
Sahara
Takato
T
Odagiri
Takeomi
T
Murata
Taichi
T
Usui
Yasuo
Y
Suzuki
Masato
M
Tashiro
D000818:Animals; D000914:Antibodies, Viral / Q000097:blood; D000940:Antigenic Variation; D000956:Antigens, Viral / Q000235:genetics / Q000276:immunology; D002460:Cell Line; D002478:Cells, Cultured; D002642:Chick Embryo; D006224:Cricetinae; D004285:Dogs; D006031:Glycosylation; D019267:Hemagglutinin Glycoproteins, Influenza Virus / Q000235:genetics / Q000276:immunology; D009981:Influenza B virus / Q000235:genetics / Q000254:growth & development*; D007252:Influenza Vaccines / Q000008:administration & dosage / Q000276:immunology; D008969:Molecular Sequence Data; D009976:Orthomyxoviridae Infections / Q000517:prevention & control; D017422:Sequence Analysis, DNA; D014776:Virus Cultivation
D000914:Antibodies, Viral; D000956:Antigens, Viral; D019267:Hemagglutinin Glycoproteins, Influenza Virus; D007252:Influenza Vaccines