ArticleJournal of virology2004
Influenza B virus BM2 protein is a crucial component for incorporation of viral ribonucleoprotein complex into virions during virus assembly.
Article in Journal of virology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 54 citations in OpenAlex.
- Highly versatile small virus-encoded proteins in cellular membranes: A structural perspective on how proteins' inherent conformational plasticity couples with host membranes' properties to control cellular processes.Journal of structural biology: X · 2025Article
- Activation of the Influenza B M2 Proton Channel (BM2).Biochemistry · 2024Article
- Activation of the influenza B M2 proton channel (BM2).bioRxiv : the preprint server for biology · 2024Article
- The Potential of Cyclodextrins as Inhibitors for the BM2 Protein: An In Silico Investigation.Molecules (Basel, Switzerland) · 2024Article
- Review
- Functions of Viroporins in the Viral Life Cycle and Their Regulation of Host Cell Responses.Frontiers in immunology · 2022Review
- M2e-based universal influenza vaccines: a historical overview and new approaches to development.Journal of biomedical science · 2019Review
- The Development and Use of Reporter Influenza B Viruses.Viruses · 2019Review
- IgA tetramerization improves target breadth but not peak potency of functionality of anti-influenza virus broadly neutralizing antibody.PLoS pathogens · 2019Article
- Functional studies reveal the similarities and differences between AM2 and BM2 proton channels from influenza viruses.Biochimica et biophysica acta. Biomembranes · 2018Article
- Solid-State NMR Investigation of the Conformation, Proton Conduction, and Hydration of the Influenza B Virus M2 Transmembrane Proton Channel.Journal of the American Chemical Society · 2016Article
- NB protein does not affect influenza B virus replication in vitro and is not required for replication in or transmission between ferrets.The Journal of general virology · 2016Article
- Targeting the Channel Activity of Viroporins.Advances in protein chemistry and structural biology · 2016Review
- The effect of the cytoplasmic tail of influenza C virus CM2 protein on its biochemical properties and intracellular processing.Biochemistry and biophysics reports · 2015Article
- The BM2 protein of influenza B virus interacts with p53 and inhibits its transcriptional and apoptotic activities.Molecular and cellular biochemistry · 2015Article
- Influenza A matrix protein M1 multimerizes upon binding to lipid membranes.Biophysical journal · 2014Article
- Characterization of the nucleocytoplasmic shuttle of the matrix protein of influenza B virus.Journal of virology · 2014Article
- Universal influenza B virus genomic amplification facilitates sequencing, diagnostics, and reverse genetics.Journal of clinical microbiology · 2014Article
- The minimalist architectures of viroporins and their therapeutic implications.Biochimica et biophysica acta · 2014Review
- The cytoplasmic tail domain of influenza B virus hemagglutinin is important for its incorporation into virions but is not essential for virus replication in cell culture in the presence of compensatory mutations.Journal of virology · 2012Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Influenza B virus contains four integral membrane proteins in its envelope. Of these, BM2 has recently been found to have ion channel activity and is considered to be a functional counterpart to influenza A virus M2, but the role of BM2 in the life cycle of influenza B virus remains unclear. In an effort to explore its function, a number of BM2 mutant viruses were generated by using a reverse genetics technique. The BM2DeltaATG mutant virus synthesized BM2 at markedly lower levels but exhibited similar growth to wild-type (wt) virus. In contrast, the BM2 knockout virus, which did not produce BM2, did not grow substantially but was able to grow normally when BM2 was supplemented in trans by host cells expressing BM2. These results indicate that BM2 is a required component for the production of infectious viruses. In the one-step growth cycle, the BM2 knockout virus produced progeny viruses lacking viral ribonucleoprotein complex (vRNP). The inhibited incorporation of vRNP was regained by trans-supplementation of BM2. An immunofluorescence study of virus-infected cells revealed that distribution of hemagglutinin, nucleoprotein, and matrix (M1) protein of the BM2 knockout virus at the apical membrane did not differ from that of wt virus, whereas the sucrose gradient flotation assay revealed that the membrane association of M1 was greatly affected in the absence of BM2, resulting in a decrease of vRNP in membrane fractions. These results strongly suggest that BM2 functions to capture the M1-vRNP complex at the virion budding site during virus assembly.
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