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Analysis of the host-specific haemagglutination of influenza A(H1N1) viruses isolated in the 1995/6 season

Published online by Cambridge University Press:  01 December 1997

T. MORISHITA ,
E. NOBUSAWA ,
S. LUO ,
K. SATO ,
S. NAKAJIMA  and
K. NAKAJIMA
T. MORISHITA
Affiliation:
Department of Virology, Medical School, Nagoya City University, 1, Kawasumi, Mizuhochou, Mizuho-ku, Nagoya 467, Japan Department of Virology, Aichi Prefectural Institute of Public Health, Nagoya 462, Japan
E. NOBUSAWA
Affiliation:
Department of Virology, Medical School, Nagoya City University, 1, Kawasumi, Mizuhochou, Mizuho-ku, Nagoya 467, Japan
S. LUO
Affiliation:
Department of Virology, Medical School, Nagoya City University, 1, Kawasumi, Mizuhochou, Mizuho-ku, Nagoya 467, Japan
K. SATO
Affiliation:
Department of Virology, Medical School, Nagoya City University, 1, Kawasumi, Mizuhochou, Mizuho-ku, Nagoya 467, Japan Department of Virology, Aichi Prefectural Institute of Public Health, Nagoya 462, Japan
S. NAKAJIMA
Affiliation:
National Institute of Public Health, 4-6-1, Shirokanedai, Minato-ku, Tokyo 108, Japan
K. NAKAJIMA
Affiliation:
Department of Virology, Medical School, Nagoya City University, 1, Kawasumi, Mizuhochou, Mizuho-ku, Nagoya 467, Japan
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Abstract

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Two phenotypes of human influenza A(H1N1) virus are currently circulating in Japan. One (group 1) agglutinates both chicken and goose red blood cells (CRBC and GRBC), the other (group 2) agglutinates GRBC but not CRBC. In the 1995/6 season, group 2 viruses accounted for 70% of the H1N1 viruses isolated in MDCK cells. The 1995/6 viruses were located on two branches of the genetic tree. One branch contained both group 1 and group 2 viruses and the other branch contained only group 2 viruses. Group 2 viruses had aspartic acid at residue 225 in the haemagglutinin (HA) protein, the key amino acid residue for group 2 phenotype. The HA protein of group 1 viruses had a change from aspartic acid to asparagine at residue 225 and the expressed HA protein of these viruses adsorbed CRBC. Serial passage of group 2 viruses in MDCK cells or embryonated chicken eggs caused these viruses to gain the ability to agglutinate CRBC. MDCK-adapted viruses had the same amino acid sequences of HA polypeptide as the original ones, but egg-adapted viruses had changed amino acid sequences. The expressed HA protein from one egg-adapted virus that originally belonged to group 2 adsorbed CRBC.

Type
Research Article
Information
Epidemiology & Infection , Volume 119 , Issue 3 , December 1997 , pp. 327 - 334
Copyright
© 1997 Cambridge University Press