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Infection and Immunity, October 2000, p. 6062-6065, Vol. 68, No. 10
0019-9567/00/$04.00+0

Purification and Characterization of a Cytotonic Protein Expressed In Vitro by the Live Cholera Vaccine Candidate CVD 103-HgR

Venugopal Sathyamoorthy, Robert H. Hall,* Barbara A. McCardell, Mahendra H. Kothary, Susie J. Ahn, and Shashikala Ratnayake

Division of Virulence Assessment, Center for Food Safety and Applied Nutrition, Food and Drug Administration, Washington, D.C. 20204

Received 1 May 2000/Returned for modification 16 June 2000/Accepted 27 July 2000

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 Mr 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.

* Corresponding author. Mailing address: Food and Drug Administration, CFSAN/DVA/HFS 327, Washington, DC 20204. Phone: (202) 205-4918. Fax: (202) 205-4939. E-mail: rhh{at}cfsan.fda.gov.

Infection and Immunity, October 2000, p. 6062-6065, Vol. 68, No. 10
0019-9567/00/$04.00+0




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