Structure of the Cell Wall of Bacillus Species C.I.P. 76‐111

Publisher Website
Google Scholar
Abstract
An unusual type of bacterial cell wall was encountered in a Bacillus strain referred to as Bacillus sp. C.I.P. 76-111. The major constituent of this cell wall is a high-MW anionic protein non-covalently associated to a peptidoglycan-polysacchride complex. The cell wall appeared as a multilayered structure when sections of whole cells or of isolated cell walls fixed with glutaraldehyde and postfixed with osmium tetroxide were examined by EM. The correlation between the observed morphological features and the biochemical data suggested that a thin central electron-dense layer identifiable with the peptidoglycan-polysaccharide complex is located between 2 similar thick layers of protein. Negative staining of isolated cell walls revealed that the outer protein layer has a regular surface array of subunits with hexagonal symmetry. Several structure properties of the cell wall peptidoglycan were investigated and they resembled those of other bacilli. Further characterization of the autolytic system showed that an N-acetylmuramyl-L-alanine amidase and a glycosidase, presumably a N-acetylmuramidase, were associated with the peptidoglycan-polysaccharide complex. This strain is devoid of membrane teichoic acid.

This publication has 44 references indexed in Scilit: