Purification and characterization of a cytotonic protein expressed In vitro by the live cholera vaccine candidate CVD 103-HgR

对霍乱活疫苗候选株 CVD 103-HgR 在体外表达的细胞张力蛋白进行纯化和表征

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Abstract

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.

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