J Bacteriol Virol.  2012 Dec;42(4):363-367. 10.4167/jbv.2012.42.4.363.

An Universal Approach to Getting Ahead for Influenza B Vaccines

• Kim JI
• Park MS

• KMID: 2168674
• DOI: http://doi.org/10.4167/jbv.2012.42.4.363

Abstract

Cross-reactive neutralizing antibodies against influenza A viruses have received attention for their potentials for prophylactic and therapeutic. These antibodies usually bind to relatively conserved stem domains of influenza hemagglutinin, one of surface glycoproteins responsible for viral binding to sialic acid-tagged cellular receptors and for membrane fusion to initiate a release process of viral genomes inside cells. Recently, a similar approach extended to influenza B viruses, which causing annual epidemics only in the human population, and some of human monoclonal antibodies exhibited promising efficacies against two antigenically diverged lineages of influenza B viruses. Moreover, one of these broadly neutralizing antibodies protected mice against both of influenza A and B challenges. Appropriate immunization may selectively enhance the efficacy of these antibodies, and this strategy may lead individuals to be prepared with broad immune responses against various influenza viruses.

Keyword

Hemagglutinin; Influenza B virus; Monoclonal antibody; Universal vaccine

MeSH Terms

Animals
Antibodies
Antibodies, Monoclonal
Antibodies, Neutralizing
Collodion
Genome, Viral
Hemagglutinins
Humans
Immunization
Influenza A virus
Influenza B virus
Influenza, Human
Membrane Fusion
Membrane Glycoproteins
Mice
Orthomyxoviridae
Vaccines
Antibodies
Antibodies, Monoclonal
Antibodies, Neutralizing
Collodion
Hemagglutinins
Membrane Glycoproteins
Vaccines

Figure

• 

  Figure 1 Phylogenetic analysis of influenza B HAs. 571 submitted HA sequences (collapsed from total 1,142 sequences available from National Center for Biotechnology Information) of influenza B viruses since 1940 were analyzed for their genetic distances. To compare phylogenetic lines between sequences, the neighbor-joining method was applied for a clustering algorithm. F84 distance was adopted for nucleotide distances for each coding sequence. The number in the parentheses represents the number of isolates.

• 

  Figure 2 Crystal structure of HA monomer and domains. 3D-crystalized structure of influenza B HA monomer was represented by PyMol software using B/Brisbane/60/2008 HA crystal structure 4FQM (PDB ID). RBS, receptor binding site; Magenta, HA1; Orange, HA2.

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