The use of maleimidocaproyloxysuccinimide to prepare malarial peptide carrier immunogens. Immunogenicity of the linking region.

Journal of Immunological Methods
G JonesA Saul

Abstract

Malarial peptides synthesized with an added N terminal cysteine were conjugated to purified diphtheria toxoid (DT) protein using the bifunctional reagent maleimidocaproyloxysuccinimide (MCS). The molar ratio of peptide to carrier was determined by subtractive sulphydryl titration and confirmed by sodium dodecyl sulphate (SDS) electrophoresis. For enzyme-linked immunoabsorbent (ELISA) analysis of sera from animals immunized with the DT conjugates, peptides were conjugated to bovine serum albumin (BSA) using MCS as well as a glutaraldehyde based coupling procedure. Western blotting analysis shows that both DT and BSA adducts were recognized by monoclonal antibodies (Mabs) directed against the peptide epitopes in the native sequences. Animals immunized with the DT-peptide conjugates produced antibodies to the coupling reagent (MCS) as well as diphtheria toxoid and peptide specific antibodies. This MCS specificity could be largely abolished by pre-incubation of sera with a soluble MCS homologue, a thiosuccinimidocaproylamide (TSC).

References

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Jul 1, 1988·Proceedings of the National Academy of Sciences of the United States of America·J A SmytheR F Anders
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Citations

Jul 1, 1990·Biologicals : Journal of the International Association of Biological Standardization·S PlaueM H Van Regenmortel
Sep 1, 1996·The Journal of Pharmacy and Pharmacology·A M JehanliM al-Shami
Jan 1, 1997·Molecular and Cellular Neurosciences·S Kröger
Oct 27, 2012·Journal of Immunological Methods·Daming ZhuAllan Saul
May 1, 1996·Environmental Management·T L McAllisterE D Brill

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