Variation of the Conserved Neutralizing Epitope in Influenza B Virus Victoria Group Isolates in Japan

Nakagawa, Naoko; Kubota, Ritsuko; Okuno, Yoshinobu

doi:10.1128/jcm.43.8.4212-4214.2005

Cited by 16 publications

(24 citation statements)

References 17 publications

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“…3b). In fact, field isolates with substitutions in this region, for instance, Asp164 1 3Glu or Asn165 1 3Lys, were found to have much weaker reactivity with human antibodies, which may impose a future epidemic threat (63). Thus, alterations of the pattern of insertion and deletion and amino acid substitutions in this region appear to be effective ways for influenza B virus to vary (56), in particular to survive a long period of time without antigenic shifts, as observed with influenza A virus (65).…”

Section: Resultsmentioning

confidence: 99%

Crystal Structure of Unliganded Influenza B Virus Hemagglutinin

Wang

Cheng

et al. 2008

J Virol

125

141

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Here we report the crystal structure of hemagglutinin (HA) from influenza B/Hong Kong/8/73 (B/HK) virus determined to 2.8 Å. At a sequence identity of ϳ25% to influenza A virus HAs, B/HK HA shares a similar overall structure and domain organization. More than two dozen amino acid substitutions on influenza B virus HAs have been identified to cause antigenicity alteration in site-specific mutants, monoclonal antibody escape mutants, or field isolates. Mapping these substitutions on the structure of B/HK HA reveals four major epitopes, the 120 loop, the 150 loop, the 160 loop, and the 190 helix, that are located close in space to form a large, continuous antigenic site. Moreover, a systematic comparison of known HA structures across the entire influenza virus family reveals evolutionarily conserved ionizable residues at all regions along the chain and subunit interfaces. These ionizable residues are likely the structural basis for the pH dependence and sensitivity to ionic strength of influenza HA and hemagglutinin-esterase fusion proteins.Influenza virus is a negative-stranded RNA virus belonging to the Orthomyxoviridae family. Three types of influenza viruses have been detected: A, B, and C. They all have a major surface glycoprotein, hemagglutinin (HA) for influenza A and B viruses and hemagglutinin-esterase fusion (HEF) protein for influenza C virus (2,20,85,98). Infections caused by influenza A and B viruses remain a major source of human morbidity and mortality worldwide (13, 90).Influenza B virus circulates exclusively in humans and seals (66), with no subtypes. The first isolated influenza B virus strain was B/Lee/40 (44). Currently, there are two major phylogenetic lineages found in circulation: B/Victoria/2/87 (B/VI) like and B/Yamagata/16/88 (B/YM) like (41,77,83). Despite the lack of subtypes, influenza B virus undergoes antigenic variation through genetic reassortment among cocirculating strains of different lineages and antigenic drift from cumulative mutations (17,48,49,56,70,83,101). Influenza B virus HAs have a mutational rate about five times slower than that observed for influenza A virus HAs (3,10,15,19,34,41,44,45,81,94,101). The antigenic structures of influenza B virus HAs have been studied by sequence analysis of both naturally occurring variants and antibody-selected escape variants (5,6,10,35,44,45,51,76,77,94,96), using the structure of influenza A H3 HA as a reference (100). However, given the rather low sequence identity between influenza A and B virus HAs, ϳ20% for HA 1 , which is the primary target for antigenic variation, it is hard to define accurately the antigenic sites in this fashion.We have recently reported two crystal structures of influenza B/Hong Kong/8/73 virus HA (referred to as B/HK HA herein) in complex with human and avian receptor analogs (95). Comparison of these structures with those of influenza A virus HAs provided a structural basis for the receptor-binding properties of influenza A and B virus HAs and suggested the role of residue 222 (H3 numbering) as a key an...

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Section: Resultsmentioning

confidence: 99%

Crystal Structure of Unliganded Influenza B Virus Hemagglutinin

Wang

Cheng

et al. 2008

J Virol

125

141

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“…There was one isolate, B/Kobe/28/2003, which did not react either to 10B8 or to 10D7. It showed another amino acid substitution at site B (N165K) (12) (Fig. 1).…”

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confidence: 99%

“…In the 1996/1997 season, there was a B/Victoria epidemic in Japan after almost 10 years' absence of the strain. Then, the next one was in the 2002/2003 season (8,11,12). The antigenicities of B/Victoria isolates in these seasons were distinct from those of the isolates in the mid-1980s.…”

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confidence: 99%

“…The first variants appeared in the 1996/1997 season with an extra oligosaccharide chain near the receptor binding region, and they became predominant in the 2002/2003 season (11). Then, the second variants appeared with variation in the conserved epitope of B/Victoria isolates, at the "tip" of the hemagglutinin (HA) molecule (12). The "tip" consists of the antigenic site of influenza AH3 virus HA, previously defined as site B.…”

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confidence: 99%

“…Escape mutants were induced by incubating virus with 9B2, by a modification of the method previously described (1,4,10). The nucleotide sequences of the escape mutants were analyzed as described previously (8)(9)(10)(11)(12).…”

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confidence: 99%

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Discovery of the Neutralizing Epitope Common to Influenza B Virus Victoria Group Isolates in Japan

Nakagawa¹,

Suzuoki²,

Kubota

et al. 2006

J Clin Microbiol

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Monoclonal antibody 9B2 possesses hemagglutination inhibition activity against all the 2002/2003 influenza B virus Victoria group isolates in Kobe, Japan, as well as representative strains isolated between 1987 and 1997. The 9B2 epitope localizes three-dimensionally in the vicinity of antigenic site A of the hemagglutinin molecule, and amino acid substitutions in this region affected the binding of 9B2.

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Diversifying selective pressure on influenza B virus hemagglutinin

Shen

Kirk

et al. 2008

Journal of Medical Virology

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Influenza B virus hemagglutinin (HA) is a major surface glycoprotein with frequent amino acid substitutions. However, the roles of antibody selection in the amino acid substitutions of HA were still poorly understood. In order to gain insights into this important issue, an analysis was conducted on a total of 271 HA 1 sequences of influenza B virus strains isolated during . In this analysis, phylogenetic analysis by maximum likelihood (PAML) package was used to detect the existence of positive selection and to identify positively selected sites on HA 1 . Strikingly, all the positively selected sites were located in the four major epitopes (120-loop, 150-loop, 160-loop, and 190-helix) of HA identified in previous studies, thus supporting a predominant role of antibody selection in HA evolution. Of particular significance is the involvement of the 120-loop in positive selection, which may become increasingly important in future field isolates. Despite the absence of different subtypes, influenza B virus HA continued to evolve into new sublineages, within which the four major epitopes were targeted selectively in positive selection. Thus, any newly emerging strains need to be placed in the context of their evolutionary history in order to understand and predict their epidemic potential.

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Variation of the Conserved Neutralizing Epitope in Influenza B Virus Victoria Group Isolates in Japan

Cited by 16 publications

References 17 publications

Crystal Structure of Unliganded Influenza B Virus Hemagglutinin

Crystal Structure of Unliganded Influenza B Virus Hemagglutinin

Discovery of the Neutralizing Epitope Common to Influenza B Virus Victoria Group Isolates in Japan

Diversifying selective pressure on influenza B virus hemagglutinin

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