Abstract
The problem of delineating the portion of mycobacterial cell wall that is essential for the activity of Freund’s complete adjuvant (FCA) has made noteworthy progress over the last five years [see reviews 48, 12]. The native mycobacterial disaccharide-tetrapeptide [1], monomeric subunits of other peptidoglycans [24, 35, 57], and a N-acetyl-muramyl-linked tripeptide [24] were successively found to be fully active in enhancing antibody response as well as in inducing the development of delayed hypersensitivity when administered with an antigen in a water-in-oil emulsion. A synthetic N-acetylmuramyl-dipeptide, analogue of part of the streptococcal peptidoglycan subunit, was thereafter shown to be the minimal structure essential for eliciting in guinea pigs the adjuvant effects ascribed to mycobacterial cell walls in FCA [24, 35]. Starting from this muramyl-dipeptide (N-acetylmuramyl-L-alanyl-D-isoglutamine) various analogues, stereoisomers, and derivatives were prepared in several laboratories [39, 40, 41, 42, 44, 50, 54] with the aim of selecting effective compounds and of establishing correlations between chemical structure and adjuvant activity.
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