Lysozyme binding by a polyglycerol phosphate polymer of the oral bacterium Streptococcus mutans BHT

Iacono, Vincent J.; Mackay, Bruce; Grossbard, B.L.; DiRienzo, Sharon; Pollock, Jerry J.

doi:10.1016/0003-9969(82)90165-0

Cited by 7 publications

(8 citation statements)

References 35 publications

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“…The fact that some of the pathogens in our tests were killed but not lysed by the coho egg lysozyme supports the conclusion of Iacono et al (1980) that the mechanisms underlying the bactericidal and lytic properties of the enzyme are not always the same. Hydrolysis of peptidoglycan by lysozyme is one explanation for the enzyme's antibacterial activity; however, bactericidal effects of some forms of lysozyme may depend on activities of these enzymes unrelated to an ability to hydrolyse the peptidoglycan.…”

Section: Resultssupporting

confidence: 81%

“…Hydrolysis of peptidoglycan by lysozyme is one explanation for the enzyme's antibacterial activity; however, bactericidal effects of some forms of lysozyme may depend on activities of these enzymes unrelated to an ability to hydrolyse the peptidoglycan. Lysozyme has been shown to bind to the lipopolysaccharide of Pseudomonas aeruginosa (Day et al 1978) and other cell structures like the cytoplasmic membrane (Iacono et al 1980). Binding of lysozyme to the tested Gramnegative fish pathogens might therefore result in damage to the outer cell membrane, thus permitting additional lysozyme to reach and injure deeper-lying structures like the cytoplasmic membrane.…”

Section: Resultsmentioning

confidence: 99%

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In vitro evidence for the antibacterial role of lysozyme in salmonid eggs

Yousif¹,

Albright²,

Evelyn³

1994

Dis. Aquat. Org.

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ABSTRACT-The yolk material of coho salmon Oncorhynchus lusutch eggs contains at least 1 naturally occurring antibactenal factor -lysozyme. The antibacterial properties of this lysozyme were studied with selected bacterial flsh pathogens. It was found to be rapidly bactericidal to Aeromonas hydrophila, Aeromonas salmonic~da, and Carnobacterium piscicola at a concentration of 700 pg ml-l, a concentration approximately one-third of that found in the yolk of most salmonid eggs. However, the lysis that ~t caused with the test bacterium Micrococcus lysodeikticus did not occur with the foregoing fish pathogens. The kidney disease bacterium Renibacterium salmoninarum was not killed when incubated with as much as 1900 pg ml-' of the enzyme for 90 min. The data presented indicate that the antibacterial role of lysozyme should not be equated merely with its ability to lyse microorganisms, and that lysozyme has a role in preventing the mother to progeny (vertical) transmission of some bacterial fish pathogens. Its failure to kill R. salmoninarum helps to explain why this organism is readily vertically transmitted.

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Section: Resultssupporting

confidence: 81%

Section: Resultsmentioning

confidence: 99%

In vitro evidence for the antibacterial role of lysozyme in salmonid eggs

Yousif¹,

Albright²,

Evelyn³

1994

Dis. Aquat. Org.

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“…23 In particular, lysozyme is aggressive against the cell membrane of Gram-positive bacteria and this is mainly associated with its anti-bacterial function. 44,45 The antibacterial function of lysozyme could, in the light of present results, be indeed related to the actual destabilization of the lipid membrane. Overall, the effect of hemoglobin, BSA and lysozyme on the structure of the lipid bilayers does not seem to be related to their structure but rather to their colloidal properties, mainly in terms of their surface charge density distribution.…”

Section: Discussionmentioning

confidence: 53%

Non-specific interactions between soluble proteins and lipids induce irreversible changes in the properties of lipid bilayers

et al. 2013

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Soluble proteins in the extracellular matrix experience a crowded environment. However, most of the biophysical studies performed to date have focused on protein concentrations within the dilute regime (well below the mM range). Here, we systematically studied the interaction of model cell membrane systems (giant unilamellar vesicles and supported lipid bilayers) with soluble globular proteins, bovine serum albumin, hemoglobin and lysozyme at physiologically relevant concentrations. To mimic the extracellular environment more closely, we also used fetal bovine serum as a good representative of a biomimetic protein mixture. We found that regardless of the protein used (and thus of their biological function), the interactions between a model cell membrane and these proteins are determined by their physico-chemical characteristics, mainly their dipolar character (or charged patches). In this paper we discuss the specificity and reversibility of these interactions and their potential implications on the living cells. In particular, we report initial evidence for an additional role of glycolipids in cell membranes: that of reducing the effects of non-specific adsorption of soluble proteins on the cell membrane.

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“…The findings in this study cannot be generalized for all serotypes of S. mutans. Strains of serotype e atid f have been reported to be tesistant to growth-inhibition and ly.sis by HEWL, whereas serotypes c and d revealed partial susceptibility (9). Whether these differences in susceptibility also are valid for salivary ly.sozyme is not clear.…”

Section: Discussionmentioning

confidence: 99%

“…Addition of HKWL alone did tiot catise cell lysis (7,8). It has therelbre been suggested that the enzyme may cause damage of S. mutans BHT by mechanisms other than its mttratnidase activity (9).…”

mentioning

confidence: 99%

Lysis of Streptococcus mutans BHT by salivary lysozyme

Twetman

Under

Modéer

1983

European J Oral Sciences

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– The aim of this work was to study the bacteriolytic ability of human salivary lysozyme (HSL) on Streptococcus mutans BHT. The cells were grown in a synthetic medium containing 3H‐thymidine to monitor DNA release after incubation with either HSL, purified by ion exchange chromatography, or hen egg white lysozyme (HEWL). The experiments demonstrated that HSL as well as HEWL could liberate DNA from cells. The lysis was dependent on enzyme concentration as well as incubation‐time. Approximately 80% of the 3H‐thymidine was released at final concentrattons of 4.5μg/mland incubation‐times exceeding 16hr. Additional treatment of the suspensions with DNase increased the levels of released radioisotopes. The lytic ability of HSL and HEWL was similar at low concentrations. HSL inactivated with goat antiserum to human lysozyme decreased the liberation of DNA by about 70%. This study suggests that HSL can lyse S. mutans BHT without presence of inorganic ions.

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Lysozyme binding by a polyglycerol phosphate polymer of the oral bacterium Streptococcus mutans BHT

Cited by 7 publications

References 35 publications

In vitro evidence for the antibacterial role of lysozyme in salmonid eggs

In vitro evidence for the antibacterial role of lysozyme in salmonid eggs

Non-specific interactions between soluble proteins and lipids induce irreversible changes in the properties of lipid bilayers

Lysis of Streptococcus mutans BHT by salivary lysozyme

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