Structure, stability, and receptor interaction of cholera toxin as studied by Fourier-transform infrared spectroscopy
- PMID: 2261465
- DOI: 10.1021/bi00487a017
Structure, stability, and receptor interaction of cholera toxin as studied by Fourier-transform infrared spectroscopy
Abstract
The structure and thermal stability of isolated B and A subunits of cholera toxin, as well as the interaction of the B subunit with a ganglioside GM1 receptor, were studied by Fourier-transform infrared spectroscopy. The B subunit of the toxin is highly folded; its secondary structure consists predominantly of beta-sheets. The temperature dependence of the infrared spectrum indicates that the B subunit undergoes thermal unfolding in the temperature range between approximately 66 and 78 degrees C. Binding to the ganglioside GM1 receptor or to its oligosaccharide moiety results in only marginal, if any, change in the secondary structure of the B subunit; however, the receptor-associated subunit does show a markedly increased thermal stability. The secondary structure of the enzymatically active A subunit is less ordered and much less stable than that of the B subunit. The relatively loose folding of the A subunit is likely to be of importance for the effective membrane translocation of this subunit.
Similar articles
-
Thermal stability and intersubunit interactions of cholera toxin in solution and in association with its cell-surface receptor ganglioside GM1.Biochemistry. 1988 Mar 22;27(6):2046-52. doi: 10.1021/bi00406a035. Biochemistry. 1988. PMID: 3378043
-
Crystal structure of cholera toxin B-pentamer bound to receptor GM1 pentasaccharide.Protein Sci. 1994 Feb;3(2):166-75. doi: 10.1002/pro.5560030202. Protein Sci. 1994. PMID: 8003954 Free PMC article.
-
Chemical and immunochemical studies on the receptor binding domain of cholera toxin B subunit.J Biol Chem. 1985 Oct 15;260(23):12528-34. J Biol Chem. 1985. PMID: 2413025
-
New insights into the structure-function relationships and therapeutic applications of cholera-like enterotoxins.Int J Med Microbiol. 2002 Feb;291(6-7):531-5. doi: 10.1078/1438-4221-00163. Int J Med Microbiol. 2002. PMID: 11890554 Review.
-
Cholera toxin.Biosci Rep. 1982 Mar;2(3):135-46. doi: 10.1007/BF01116376. Biosci Rep. 1982. PMID: 6121589 Review. No abstract available.
Cited by
-
Secondary Structures of MERS-CoV, SARS-CoV, and SARS-CoV-2 Spike Proteins Revealed by Infrared Vibrational Spectroscopy.Int J Mol Sci. 2023 May 31;24(11):9550. doi: 10.3390/ijms24119550. Int J Mol Sci. 2023. PMID: 37298500 Free PMC article.
-
The cholera toxin A1(3) subdomain is essential for interaction with ADP-ribosylation factor 6 and full toxic activity but is not required for translocation from the endoplasmic reticulum to the cytosol.Infect Immun. 2006 Apr;74(4):2259-67. doi: 10.1128/IAI.74.4.2259-2267.2006. Infect Immun. 2006. PMID: 16552056 Free PMC article.
-
FTIR reveals structural differences between native beta-sheet proteins and amyloid fibrils.Protein Sci. 2004 Dec;13(12):3314-21. doi: 10.1110/ps.041024904. Epub 2004 Nov 10. Protein Sci. 2004. PMID: 15537750 Free PMC article.
-
Enzymatic activity of Lecithin:retinol acyltransferase: a thermostable and highly active enzyme with a likely mode of interfacial activation.Biochim Biophys Acta. 2014 Jun;1844(6):1128-36. doi: 10.1016/j.bbapap.2014.02.022. Epub 2014 Mar 5. Biochim Biophys Acta. 2014. PMID: 24613493 Free PMC article.
-
A Conformational Shift in the Dissociated Cholera Toxin A1 Subunit Prevents Reassembly of the Cholera Holotoxin.Toxins (Basel). 2015 Jul 20;7(7):2674-84. doi: 10.3390/toxins7072674. Toxins (Basel). 2015. PMID: 26266549 Free PMC article.
MeSH terms
Substances
LinkOut - more resources
Other Literature Sources