Heat-labile enterotoxin: beyond G(m1) binding.
| Data(s) |
01/06/2010
|
|---|---|
| Formato |
1445 - 1470 |
| Identificador |
http://www.ncbi.nlm.nih.gov/pubmed/22069646 toxins-02-01445 Toxins (Basel), 2010, 2 (6), pp. 1445 - 1470 http://hdl.handle.net/10161/10656 2072-6651 |
| Relação |
Toxins (Basel) 10.3390/toxins2061445 |
| Palavras-Chave | #ETEC #GM1 #blood antigen #heat-labile enterotoxin #lipopolysaccharide #Animals #Bacterial Toxins #Enterotoxins #Escherichia coli Proteins #G(M1) Ganglioside #Glycosides #Humans #Lipopolysaccharides #Protein Binding #Triterpenes |
| Tipo |
Journal Article |
| Cobertura |
Switzerland |
| Resumo |
Enterotoxigenic Escherichia coli (ETEC) is a significant source of morbidity and mortality worldwide. One major virulence factor released by ETEC is the heat-labile enterotoxin LT, which is structurally and functionally similar to cholera toxin. LT consists of five B subunits carrying a single catalytically active A subunit. LTB binds the monosialoganglioside G(M1), the toxin's host receptor, but interactions with A-type blood sugars and E. coli lipopolysaccharide have also been identified within the past decade. Here, we review the regulation, assembly, and binding properties of the LT B-subunit pentamer and discuss the possible roles of its numerous molecular interactions. |
| Idioma(s) |
ENG |
