Characterization and localization of the enzymatic deacylation of lipoteichoic acid in group A streptococci.

Open Access
Publisher Website
Google Scholar
Abstract
Protoplasts of a group A streptococcal strain contained enzymatic activity capable of converting lipoteichoic acid (LTA) to deacylated lipoteichoic acid (dLTA). The enzyme(s) appears to be located mainly in the membrane, although activity was also found in the cytoplasm. Determination of cleavage sites within the LTA molecule was approached by comparing the chemical composition of LTA and native dLTA. Native dLTA, as distinguished from chemically deacylated LTA, was isolated from buffer in which liver streptococci were resuspended and incubated. The chemical data suggest that the enzyme(s) was lipolytic in nature; that is, the conversion of LTA to dLTA was the result of cleavage of the ester linkages between the fatty acids and the remainder of the LTA molecule.