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PubMed2006

Muralytic activity of Micrococcus luteus Rpf and its relationship to physiological activity in promoting bacterial growth and resuscitation.

The culturability of several actinobacteria is controlled by resuscitation-promoting factors (Rpfs). These are proteins containing a c. 70-residue domain that adopts a lysozyme-like fold. The invariant catalytic glutamate residue found in lysozyme and various bacterial lytic transglycosylases is also conserved in the Rpf proteins. Rpf from Micrococcus luteus, the founder member of this protein family, is indeed a muralytic enzyme, as revealed by its activity in zymograms containing M. luteus cell walls and its ability to (i) cause lysis of Escherichia coli when expressed and secreted into the periplasm; (ii) release fluorescent material from fluorescamine-labelled cell walls of M. luteus; and (iii) hydrolyse the artificial lysozyme substrate, 4-methylumbelliferyl-beta-D-N,N',N''-triacetylchitotrioside. Rpf activity was reduced but not completely abolished when the invariant glutamate residue was altered. Moreover, none of the other acidic residues in the Rpf domain was absolutely required for muralytic activity. Replacement of one or both of the cysteine residues that probably form a disulphide bridge within Rpf impaired but did not completely abolish muralytic activity. The muralytic activities of the Rpf mutants were correlated with their abilities to stimulate bacterial culturability and resuscitation, consistent with the view that the biological activity of Rpf results directly or indirectly from its ability to cleave bonds in bacterial peptidoglycan.

Animals↗
PubMed2006

Characterization of the Staphylococcus aureus CidR regulon: elucidation of a novel role for acetoin metabolism in cell death and lysis.

The Staphylococcus aureus cid and lrg operons encode a novel regulatory system that affects murein hydrolase activity, stationary-phase survival and antibiotic tolerance. Expression of the lrgAB operon is positively regulated by a two-component regulatory system encoded by the lytSR operon located immediately upstream to lrgAB. By comparison, the cidABC operon lies downstream from the cidR gene, encoding a protein homologous to the LysR-type family of transcriptional regulators. Transcription analysis of a cidR mutant revealed that CidR enhances cidABC expression in the presence of acetic acid generated by the metabolism of excess glucose. Microarray studies identified additional CidR-regulated operons including the IrgAB and alsSD encoding proteins involved in acetoin production. Surprisingly, Northern blot analyses revealed that cidABC and lrgAB transcription was uninducible in an alsSD mutant grown in the presence of excess glucose, suggesting that the CidR-mediated upregulation of cidABC and lrgAB transcription is dependent on the presence of intact alsSD genes. Zymographic and quantitative analyses of murein hydrolase activity also revealed that disruption of the alsSD genes results in significantly decreased extracellular murein hydrolase activity compared with that of the parental strain, UAMS-1. Furthermore, the alsSD mutant displayed decreased stationary-phase survival relative to UAMS-1, both in the presence and absence of glucose. The results of this study define the CidR regulon and demonstrate that the generation of acetoin is linked to the control of cell death and lysis in S. aureus.

Acetoin↗
PubMed1981

The use of lysostaphin in in vitro assays of phagocyte function: adherence to and penetration into granulocytes.

The usefulness of lysostaphin for the removal of cell-adherent and extracellular bacteria in assays performed to measure the intracellular killing of Staphylococcus aureus by granulocytes was investigated. The results showed that the adherence of lysostaphin to the granulocyte surface is effectuated by a temperature-independent process and that bound lysostaphin is still microbicidal. Lysostaphin also penetrates into the granulocytes by a temperature-dependent process and kills ingested S. aureus intracellularly. Therefore, despite reports to the contrary in the literature, lysostaphin is not a reliable agent for the removal of only extracellular S. aureus and should no longer be used in assays to determine the rate of intracellular killing by granulocytes.

Bacteriolysis↗
PubMed1994

Effect of proteolytic enzymes on the lysis and growth of oral bacteria.

Previous studies have shown increased levels of proteolytic enzymes in affected periodontal sites. The aim of the present investigation was to evaluate the effect of proteolytic environments on the lysis and growth of selected oral bacteria associated with either healthy or diseased periodontal sites. The effect of trypsin, chymotrypsin and proteinase K on cell lysis was determined following incubation with bacteria, whereas the effect of the same proteolytic enzymes on bacterial growth was tested using a disc-plate technique. Overall, gram-positive bacteria appeared to be more resistant to lysis than gram-negative bacteria. The most susceptible bacteria were Actinomyces spp., Eubacterium saburreum, Prevotella intermedia, Capnocytophaga ochracea, Fusobacterium nucleatum, Prevotella loescheii, Treponema denticola and Actinobacillus actinomycetemcomitans. The disc-plate procedure indicated that the growth of Actinomyces spp., E. saburreum, C. ochracea, P. intermedia, P. loescheii, Porphyromonas gingivalis and T. denticola were the most affected, more particularly by chymotrypsin and proteinase K. Interestingly, the growth of F. nucleatum was rather stimulated by proteolytic enzymes. The observations reported in this investigation indicate that specific and general proteolytic activities have the ability to lyse some oral bacterial species and to interfere with their growth. It is suggested that such effects could represent new mechanisms by which the bacterial ecology of subgingival sites may be affected.

Actinomyces↗
PubMed1977

Structure and synthesis of a lipid-containing bacteriophage. An endolysin activity associated with bacteriophage PM2.

Endolysin was induced in Pseudomonas BAL-31 infected with bacteriophage PM2 and was also associated with the purified virion. This enzyme required divalent cations for its activity, Ca2+ being the most effective cation. Endolysin activity in the virion increased up to three-fold upon disruption and the activity could be localized in the viral nucleocapsid. Thus the enzyme is localized within the virion. After purification of the structural proteins of bacteriophage PM2, only the nucleocapsid protein (III) had endolysin activity.

Bacteriolysis↗
PubMed1985

Second lytic target of beta-lactam compounds that have a terminal D-amino acid residue.

A new biochemical mechanism of lysing bacterial cells by treatment with certain beta-lactam compounds that possess a terminal D-amino acid moiety in their side chain was demonstrated. The two functions of the molecule, the beta-lactam and terminal D-amino acid moiety, are both involved in the activity of lysing gram-negative bacteria, which is characterized by very rapid lysis of the cells in the first few hours after their contact with the compound. This mechanism was proved by studies on one such compound, named MT-141, which contains a terminal D-cysteine moiety with free amino and carboxyl groups in the 7 beta-side chain of the 7 alpha-methoxy-cephalosporin skeleton. This compound bound to the cell-wall peptidoglycan of Escherichia coli through the D-amino group of its terminal D-amino acid moiety and this seemed to cause rapid cell lysis. Both activities, of binding to peptidoglycan and of causing rapid cell lysis, were inhibited by certain D-amino acids, but not by L-amino acids. Mutants were isolated that had simultaneously gained decreased sensitivity to this kind of beta-lactam compound and supersensitivity to globomycin, an inhibitor of formation of lipoproteins which function in linking the peptidoglycan to the outer membrane. These results suggest that binding of the terminal D-amino acid moiety of the beta-lactam compound to peptidoglycan somehow influences formation of the linkage between the outer membrane and the peptidoglycan and consequently enhances the cell lytic activity of the beta-lactam portion of the molecule.

Amino Acid Sequence↗
PubMed1986

Searching for autolysin functions. Characterization of a pneumococcal mutant deleted in the lytA gene.

The first mutant of Streptococcus pneumoniae showing a complete deletion in the lytA gene coding for the N-acetylmuramyl-L-alanine amidase has been isolated and characterized. This amidase was previously the only autolysin detected in this species. This mutant shows a normal growth rate and can be transformed using either chromosomal or plasmid DNA. The most remarkable biological consequences of the absence of the amidase are the formation of small chains (six to eight cells) and the absence of lysis in the stationary phase of growth. In addition, this mutant exhibits a tolerant response against the beta-lactam antibiotics.

Amidohydrolases↗
PubMed1991

Comparative studies on bacteriolytic properties of Staphylococcus chromogenes and Staphylococcus hyicus.

Staphylococcus chromogenes and Staphylococcus hyicus showed bacteriolytic activities towards a Micrococcus luteus reference strain. This was demonstrated on tryptone soya agar containing M. luteus cells. Both bacteriolytic enzymes could be isolated by ionic exchange chromatography and subsequent gel filtration. The isolated bacteriolysin of S. chromogenes lysed the M. luteus reference culture, was heat inactivated by 95 degrees C and precipitated specifically with antiserum produced against the bacteriolysin of S. hyicus.

Animals↗
PubMed2006

Contribution of virus-induced lysis and protozoan grazing to benthic bacterial mortality estimated simultaneously in microcosms.

In contrast to the water column, the fate of bacterial production in freshwater sediments is still a matter of debate. Thus, the importance of virus-induced lysis and protozoan grazing of bacteria was investigated for the first time simultaneously in a silty sediment layer of a mesotrophic oxbow lake. Microcosms were installed in the laboratory in order to study the dynamics of these processes over 15 days. All microbial and physicochemical parameters showed acceptable resemblance to field data observed during a concomitant in situ study, and similar conclusions can be drawn with respect to the quantitative impact of viruses and protozoa on the bacterial compartment. Viral decay rates ranged from undetectable to 0.078 h(-1) (average, 0.033 h(-1)), and the control of bacterial production from below the detection limit to 36% (average, 12%). The contribution of virus-induced lysis of bacteria to the dissolved organic matter pool as well as to benthic bacterial nutrition was low. Ingestion rates of protozoan grazers ranged from undetectable to 24.7 bacteria per heterotrophic nanoflagellate (HNF) per hour (average, 4.8 bacteria HNF(-1) h(-1)) and from undetectable to 73.3 bacteria per ciliate per hour (average, 11.2 bacteria ciliate(-1) h(-1)). Heterotrophic nanoflagellate and ciliates together cropped up to 5% (average, 1%) of bacterial production. The viral impact on bacteria prevailed over protozoan grazing by a factor of 2.5-19.9 (average, 9.5). In sum, these factors together removed up to 36% (average, 12%) of bacterial production. The high number of correlations between viral and protozoan parameters is discussed in view of a possible relationship between virus removal and the presence of protozoan grazers.

Animals↗