Immunogenicity of a fusion protein linking the beta subunit carboxyl terminal peptide (CTP) of human chorionic gonadotropin to the B subunit of Escherichia coli heat-labile enterotoxin (LTB)

Human chorionic gonadotropin (hCG) is currently under investigation as an antigenic target in both anti-cancer and anti-fertility vaccines. Formulations studied to date show promise in clinical trials for both applications yet are expensive to produce and require frequent administration in order to...

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Bibliographic Details
Published inVaccine Vol. 14; no. 16; pp. 1560 - 1568
Main Authors Rock, Edwin P., Reich, Karl A., Lyu, Dennis M., Hovi, Marianne, Hardy, Jonathan, Schoolnik, Gary K., Stocker, Bruce A.D., Stevens, Vernon
Format Journal Article
LanguageEnglish
Published Oxford Elsevier Ltd 01.11.1996
Elsevier
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Summary:Human chorionic gonadotropin (hCG) is currently under investigation as an antigenic target in both anti-cancer and anti-fertility vaccines. Formulations studied to date show promise in clinical trials for both applications yet are expensive to produce and require frequent administration in order to maintain an effective antibody titer. We have engineered a fusion protein consisting of Escherichia coli heat-labile enterotoxin subunit B (LTB) genetically linked at its C terminus via a nine amino acid linker to the 37 amino acid carboxyl terminal peptide (CTP) of the hCG beta chain. This LTB-CTP fusion protein is stably expressed in bacteria and forms pentamers of full-length protein subunits. Purified LTB-CTP protein induces hCG-specific antibodies in mice without additional adjuvants.
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ISSN:0264-410X
1873-2518
DOI:10.1016/S0264-410X(96)00046-1