Cationization of protein antigens

Autor: J G Michael, Amadeo J. Pesce, Muckerheide A
Rok vydání: 1990
Předmět:
Zdroj: Cellular Immunology. 127:67-77
ISSN: 0008-8749
DOI: 10.1016/0008-8749(90)90115-8
Popis: Preparations of bovine serum albumin (BSA) were cationized by substituting anionic side chain carboxyl groups with polycationic aminoethylamide groups. Different degrees of substitution were obtained by varying the reaction time. Mice immunized with partially cationized proteins produced early increased levels of antibody over those made by mice immunized with nBSA, followed by a period of decreased response before returning to a second period of enhanced and prolonged antibody synthesis. In contrast, fully substituted BSA gave rise to a significantly enhanced response which was delayed in its onset. Differences in isotype or in antibody specificity during the early and late periods of enhanced responsiveness could not be demonstrated. Cell transfer experiments showed that T cells harvested from mice immunized with the less cationized cBSA preparations could, in contrast to T cells from mice immunized with the fully cationized preparations, suppress antibody responses to both nBSA and cBSA in normal mice. These data are consistent with the possibility that the partially cationized proteins, in contrast to the fully cationized antigen, yield a unique pattern of responsiveness due to retention of determinants necessary for the induction of Ts while exhibiting the enhanced immunogenicity characteristic of cationized molecules.
Databáze: OpenAIRE