ArticleJournal of virology2002
Homomultimerization of the coxsackievirus 2B protein in living cells visualized by fluorescence resonance energy transfer microscopy.
Article in Journal of virology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 53 citations in OpenAlex.
- Enterovirus 2B protein: From viroporin to membrane stress sensor, mechanistic principles of multi-pathway regulation.Virulence · 2027Review
- Review
- The Role of β Cell Stress and Neo-Epitopes in the Immunopathology of Type 1 Diabetes.Frontiers in endocrinology · 2020Review
- Inherent ER stress in pancreatic islet β cells causes self-recognition by autoreactive T cells in type 1 diabetes.Journal of autoimmunity · 2016Article
- T cell epitopes and post-translationally modified epitopes in type 1 diabetes.Current diabetes reports · 2015Review
- β cell ER stress and the implications for immunogenicity in type 1 diabetes.Frontiers in cell and developmental biology · 2015Review
- Topology and biological function of enterovirus non-structural protein 2B as a member of the viroporin family.Veterinary research · 2014Review
- Viral targets of acylguanidines.Drug discovery today · 2012Review
- Viroporins: structure and biological functions.Nature reviews. Microbiology · 2012Review
- Mechanism of function of viral channel proteins and implications for drug development.International review of cell and molecular biology · 2012Review
- Membrane integration of poliovirus 2B viroporin.Journal of virology · 2011Article
- Viral proteins function as ion channels.Biochimica et biophysica acta · 2011Review
- FLIM and emission spectral analysis of caspase-3 activation inside single living cell during anticancer drug-induced cell death.European biophysics journal : EBJ · 2009Article
- Viral channel-forming proteins.International review of cell and molecular biology · 2009Review
- Quantitative analysis of multi-protein interactions using FRET: application to the SUMO pathway.Protein science : a publication of the Protein Society · 2008Article
- Functional analysis of picornavirus 2B proteins: effects on calcium homeostasis and intracellular protein trafficking.Journal of virology · 2008Article
- Cytopathic mechanisms of HIV-1.Virology journal · 2007Review
- Article
- Interaction of metastasis-inducing S100A4 protein in vivo by fluorescence lifetime imaging microscopy.European biophysics journal : EBJ · 2005Article
- Oligomerization of HEXIM1 via 7SK snRNA and coiled-coil region directs the inhibition of P-TEFb.Nucleic acids research · 2005Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The 2B protein of enteroviruses is the viral membrane-active protein that is responsible for the modifications in host cell membrane permeability that take place in enterovirus-infected cells. The 2B protein shows structural similarities to the group of lytic polypeptides, polypeptides that permeate membranes either by forming multimeric membrane-integral pores or, alternatively, by lying parallel to the lipid bilayer and disturbing the curvature and symmetry of the membrane. Our aim is to gain more insight into the molecular architecture of the 2B protein in vivo. In this study, the possible existence of multimers of the coxsackie B3 virus 2B protein in single living cells was explored by fluorescence resonance energy transfer (FRET) microscopy. FRET between fusion proteins 2B-ECFP and 2B-EYFP (enhanced cyan and yellow fluorescent variants of green fluorescent protein) was monitored by using spectral imaging microscopy (SPIM) and fluorescence lifetime imaging microscopy (FLIM). Both techniques revealed the occurrence of intermolecular FRET between 2B-ECFP and 2B-EYFP, providing evidence for the formation of protein 2B homomultimers. Putative models for the mode of action of the membrane-active 2B protein and the formation of membrane-integral pores by 2B multimers are discussed.
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