An Unusual Type of Bacterial Cell‐Wall in a Mutant of Bacillus subtilis 168

This is the authors' abstract. We don't add key points for this paper.

It was previously shown that in the cell walls of the Cbl‐1 mutant of Bacillus subtilis 168 wt, teichoic acid was replaced by a protein of high molecular weight which accounted for about 50% of the cell wall material. The structure of this unusual bacterial cell wall was further investigated. The autolysin associated with the cell walls of the mutant was characterized as a muramidase and thus differed from that of the parent strain. Furthermore, a proteolytic activity was detected in these cell walls. Several procedures were examined for the isolation and purification of the Cbl‐1 cell wall protein and peptidoglycan. The protein was readily isolated by treating the cell walls with 6 M lithium chloride and it was shown to consist of two non‐covalently associated chains which could be separeted by either dodecylsulfate or urea. Treatment of the cell walls with 2% sodium dodecylsulfate yielded an insoluble protein‐free fraction presenting the characteristic composition of a peptidoglycan and the well‐known morphology of rod‐shaped ghosts. As in the case of the cell walls of B. subtilis 168 wt, this fraction contained galactosamine and an excess of glucosamine.