Periplasmic lysozime inhibitior pliC and its role in antilysozime activity of enterobacteria

Two families of specific inhibitors of type C lysozyme (Ivy and PliC) secreted from the periplasmic space are known in enterobacteria. Microbial capacity for distant lysozyme inactivation (antilysozyme activity) is most pronounced in the strains and species carrying homologues of the pliC gene. The pliC homologue localized in a ～200-kb megaplasmid of Klebsiella pneumoniae was shown to differ significantly in the amino acid composition of the coded polypeptide. Similar to the Salmonella enterica pliC homologue, it possesses a detachable signal part and contains identical functionally critical amino acids of the active center of the inhibitor. Antilysozyme activity of the pliC-positive K. pneumoniae strains was observed at the level corresponding to the highest values found in pliC-positive S. enterica. High level of the antilysozyme activity in K. pneumoniae strains containing the plasmid pliC homologue was found in all studied strains, unlike S. enterica strains carrying the known chromosomal pliC homologue.     

Lysozyme activity of pneumococci]

Examination of 329 pneumococcal strains showed that 41.2 per cent of the cultures had lysozyme activity. The frequency of the lysozyme feature depended on the method used. The lysozyme active strains were more frequently isolated from patients than from healthy persons and characterized by antibiotic resistance. The lysozyme feature correlated with the pneumococcal virulence with respect to albino mice, capacity for capsule formaiton and resistance to phagocytosis.     

The antilysozyme activity of meningococci

The antilysozyme activity of 184 meningococcal strains was studied. Such activity was found in all strains within the range 1-25 micrograms/ml, which was due to the heterogeneity of bacterial population. Strains varying in the total level of their lysozyme activity differed in the population structure by this sign. Preparations inhibiting antilysozyme activity could be differentiated according to the character of their action by the method of the population analysis. In the process of phagocytosis the selection of clones with a high level of antilysozyme activity was found to occur. The antilysozyme factor, heat resistant protein with a molecular weight of 10,000-30,000 D, was sensitive to trypsin.     

Growth-phase associated changes in the reproductive capacity, intracellular polyamines, and antilysozyme activity inEscherichia coli batch culture

Growth-phase associated changes in and relationships between the specific growth rate (μ) characterizing the reproductive capacity of the cells, the contents of intracellular biogenic polyamines (BPA), such as putrescine (P), cadaverine (C), and spermidine (S), and antilysozyme activity (ALA) were studied in 37 strains ofEscherichia coli grown in batch culture on solid medium. A decrease in μ upon the transition of the culture to the stationary growth phase was accompanied by a decrease in the pool of free BPA, mainly P and C, and by the appearance of ALA. The interrelations between the parameters studied were described as a complex of direct and negative correlations; the combination of low initial P and C contents, reduced P/S and C/S ratios, and a high level of ALA was designated as afactor of slight inhibition ofE. coli reproduction. It is argued that BPA and ALA are integrated in a system controlling both the metabolism and stability of peptidoglycan inE. coli.