Diverse binding modes, same goal: The receptor recognition mechanism of botulinum neurotoxin. Issue 2 (March 2015)

• Record Type: Journal Article
• Authors: Lam, Kwok-Ho; Yao, Guorui; Jin, Rongsheng
• Is Part Of: Progress in biophysics and molecular biology. Volume 117:Issue 2/3(2015)
• Page Start: 225
• Page End: 231
• Publication Date: 2015-03
• Subjects: Botulinum neurotoxin -- Botulism -- Synaptotagmin -- Synaptic vesicle glycoprotein 2 -- Protein complex -- Host-pathogen recognition; botulinum neurotoxin BoNT -- light chain LC -- heavy chain HC -- N-terminal domain of HC HN -- C-terminal domain of HC HC -- N-terminal subdomain of HC HCN -- C-terminal subdomain of HC HCC -- synaptotagmin Syt -- synaptic vesicle glycoprotein 2 SV2; Biophysics -- Periodicals; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular Biology -- Periodicals; Biophysique -- Périodiques; Biochimie -- Périodiques; 571.4
• DOI: 10.1016/j.pbiomolbio.2015.02.004
• Languages: English
• ISSNs: 0079-6107

Abstract

Abstract: Botulinum neurotoxins (BoNTs) are among the most deadly toxins known. They act rapidly in a highly specific manner to block neurotransmitter release by cleaving the soluble N-ethylmaleimide sensitive factor attachment protein receptor (SNARE) complex at neuromuscular junctions. The extreme toxicity of BoNTs relies predominantly on their neurotropism that is accomplished by recognition of two host receptors, a polysialo-ganglioside and in the majority of cases a synaptic vesicle protein, through their receptor-binding domains. Two proteins, synaptotagmin and synaptic vesicle glycoprotein 2, have been identified as the receptors for various serotypes of BoNTs. Here, we review recent breakthroughs in the structural studies of BoNT–protein receptor recognitions that highlight a range of diverse mechanisms by which BoNTs manipulate host neuronal proteins for highly specific uptake at neuromuscular junctions.