Gene Symbol: VC1457
Description: cholera enterotoxin subunit A
Species: Vibrio cholerae O1 biovar El Tor str. N16961
- The arrangement of subunits in cholera toxinD M Gill
Biochemistry 15:1242-8. 1976..This binding increases the effective concentration of the toxin in the vicinity of the plasma membrane. Possible ways in which A1 then crosses the membrane are considered in the Discussion...
- Crystal structures of an intrinsically active cholera toxin mutant yield insight into the toxin activation mechanismClaire J O'Neal
Department of Chemistry and Biomolecular Structure Center, University of Washington, Seattle, Washington 98195, USA
Biochemistry 43:3772-82. 2004..On the basis of these six new views of the CT holotoxin, we propose a model for how the activational modifications experienced by wild-type CT are communicated to the active site...
- Gangliosides that associate with lipid rafts mediate transport of cholera and related toxins from the plasma membrane to endoplasmic reticulmYukako Fujinaga
GI Cell Biology, Children s Hospital and Harvard Medical School, Boston, Massachusetts 02115, USA
Mol Biol Cell 14:4783-93. 2003..Our results explain why LTIIb does not cause disease in humans and suggest that gangliosides with high affinity for lipid rafts may provide a general vehicle for the transport of toxins to the ER...
- The three-dimensional crystal structure of cholera toxinR G Zhang
Center for Mechanistic Biology and Biotechnology, Argonne National Laboratory, IL 60439, USA
J Mol Biol 251:563-73. 1995..These structures, along with those of related toxins from Shigella dysenteria and Bordetella pertussis, offer a first step towards the rational design of new vaccines and anti-microbial agents...
- Isolation and characterization of a precursor form of the 'A' subunit of cholera toxinL K Duffy
FEBS Lett 126:187-90. 1981
- Covalent structure of the gamma chain of the A subunit of cholera toxinL K Duffy
J Biol Chem 256:12252-6. 1981..The chemical similarity between the gamma chain regions of these two enterotoxins was thus considerably less than that of their beta chains which were shown to be 79% identical...
- Cholera toxin genes: nucleotide sequence, deletion analysis and vaccine developmentJ J Mekalanos
Nature 306:551-7. 1983..Incorporation of defined in vitro-generated ctx deletion mutations into Vibrio cholerae by in vivo genetic recombination produced strains which have practical value in cholera vaccine development...
- Nucleotide sequence analysis of the A2 and B subunits of Vibrio cholerae enterotoxinH Lockman
J Biol Chem 258:13722-6. 1983..cholerae and E. coli LT demonstrates two regions of highly conserved sequences: 12 and 22 uninterrupted amino acids are the same among the A2 and B subunits, respectively, from the three strains...
- Vibrio cholerae enterotoxin genes: nucleotide sequence analysis of DNA encoding ADP-ribosyltransferaseH A Lockman
J Bacteriol 159:1086-9. 1984..The primary structure of the A1 fragment from cholera enterotoxin is more related to that from a human enterotoxigenic Escherichia coli than to that from a porcine enterotoxigenic E. coli...
- Stimulation of intestinal adenyl cyclase by cholera toxinG W Sharp
Nature 229:266-9. 1971
- Nucleotide sequence analysis of the CT operon of the Vibrio cholerae classical strain 569BE Dams
RUCA Laboratory for Human Biochemistry, University of Antwerp, Belgium
Biochim Biophys Acta 1090:139-41. 1991..The results prove the exactness of the amino acid CT B sequence published by Takao et al. (1985, Eur. J. Biochem. 146, 503-508). A comparison is made with already reported CT genes...
- Subunit structure and N-terminal amino acid sequence of the three chains of cholera enterotoxinD G Klapper
Immunochemistry 13:605-11. 1976
- Primary structure of cholera toxin subunit A1: isolation, partial sequences and alignment of the BrCN fragmentsC Y Lai
FEBS Lett 100:85-9. 1979
- Structural basis for the activation of cholera toxin by human ARF6-GTPClaire J O'Neal
Department of Chemistry, University of Washington, Seattle, WA 98195, USA
Science 309:1093-6. 2005..The extensive toxin:ARF-GTP interface surface mimics ARF-GTP recognition of normal cellular protein partners, which suggests that the toxin has evolved to exploit promiscuous binding properties of ARFs...