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9 výsledky
Effects of cecropin-XJ on growth and adherence of oral cariogenic bacteria in vitro.
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BACKGROUND
Cecropin-XJ belongs to cecropin-B, which is the most potent antibacterial peptide found naturally. The aim of this study was to investigate the effects of cecropin-XJ on growth and adherence of oral cariogenic bacteria.
METHODS
Four oral cariogenic bacteria (Streptococcus mutans,
Insight Into the Effects of Nisin and Cecropin on the Oral Microbial Community of Rats by High-Throughput Sequencing
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The oral microbiome has major impacts on oral health and disease. Antimicrobial peptides (AMPs), such as nisin and cecropin, have been widely used as food preservatives or feed additives, and are thus inevitably ingested by consumers through their oral cavity. However, as broad-spectrum
In vitro susceptibility of the Streptococcus milleri group to antimicrobial peptides.
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OBJECTIVE
To determine the susceptibility of strains of the Streptococcus milleri group (SMG) to commercially available antimicrobial peptides.
METHODS
Thirty strains of SMG from a range of sources were assessed for their susceptibility to 10 antimicrobial peptides of either human, animal or insect
Polydnaviruses of hymenopteran endoparasitoids knock out the host insect immune response.
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The insect immune system reacts against invading microorganisms and parasites with the recruitment of haemocytes and with humoral response. Cellular immune reactions involve phagocytosis, nodule formation and encapsulation by different types of haemocytes whereas insect cell-free antibacterial
Antimicrobial peptides protect coho salmon from Vibrio anguillarum infections.
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Fish losses from infectious diseases are a significant problem in aquaculture worldwide. Therefore, we investigated the ability of cationic antimicrobial peptides to protect against infection caused by the fish pathogen Vibrio anguillarum. To identify effective peptides for fish, the MICs of certain
Phosphatidylcholine in membrane of Escherichia coli changes bacterial antigenicity.
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This study reports that Escherichia coli phosphatidylcholine-positive (PC+) strain Top10/ptac66 (PC+ PE+), in which borrelial PC synthase (PCS) directly condenses exogenous choline with CDP-diacylglycerol (CDP-DAG) to form PC, displayed not only stronger resistance to antimicrobial peptides cecropin
[Anti-infective defence strategies and methods of escape from entomologic pathogens under immunologic control of insects].
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Insect immunity comprises a complex of several distinct systems, both haemocytic and humoral in nature, that cooperate together in a more or less coordinated way to provide protection of the body cavity from invading microorganisms. Insects can respond to infections by a selective synthesis of
[Man's own antibiotics--an innate immune system].
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In 1981, Steiner and co-workers of Stockholm described a newly discovered type of potent antibacterial peptides which lack cysteine, so called cecropins, which are spiral-formed molecules of 30-40 amino acids found to kill bacteria within a few minutes by disintegration of the bacterial cell wall,
The antibacterial peptide pyrrhocoricin inhibits the ATPase actions of DnaK and prevents chaperone-assisted protein folding.
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Recently, we documented that the short, proline-rich antibacterial peptides pyrrhocoricin, drosocin, and apidaecin interact with the bacterial heat shock protein DnaK, and peptide binding to DnaK can be correlated with antimicrobial activity. In the current report we studied the mechanism of action
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