Purification and characterization of a cytotonic protein expressed In vitro by the live cholera vaccine candidate CVD 103-HgR.
Cholera vaccines developed by the deletion of CTX genes from Vibrio cholerae induce a residual reactogenicity in up to 10% of vaccinees. A novel cytotonic agent named secreted CHO cell elongating protein (S-CEP) was purified from culture supernatants of CVD 103-HgR (Levine et al., Lancet ii:467-470, 1988). Five fractionation steps yielded electrophoretically pure S-CEP with an M(r) of 79,000. A partially purified preparation caused fluid accumulation in the sealed infant mouse model. The amino terminus bore a unique sequence with strong homology to a cytotonic toxin of El Tor V. cholerae.
Sathyamoorthy
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V
Division of Virulence Assessment, Center for Food Safety and Applied Nutrition, Food and Drug Administration, Washington, D.C. 20204, USA.
Hall
R H
RH
McCardell
B A
BA
Kothary
M H
MH
Ahn
S J
SJ
Ratnayake
S
S
D000595:Amino Acid Sequence; D000818:Animals; D001427:Bacterial Toxins / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism / Q000633:toxicity; D016466:CHO Cells; D022121:Cholera Vaccines; D006224:Cricetinae; D051379:Mice; D008969:Molecular Sequence Data; D014734:Vibrio cholerae / Q000254:growth & development / Q000378:metabolism* / Q000472:pathogenicity*
D001427:Bacterial Toxins; D022121:Cholera Vaccines