Cationic Bactericidal Peptides

Hancock, Robert E. W.; Falla, Timothy J.; Brown, Melissa H.

doi:10.1016/s0065-2911(08)60145-9

Cited by 266 publications

(228 citation statements)

References 202 publications

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“…Benton et al (1963) determined the inhibition rate on the spores of Bacillus subtilis from the venom of A. mellifera. Similarly Hancock et al (1995) reported that Melittin in the venom of A. mellifera had wide spectrum of biological effects including antimicrobial activity. The toxicity of A. cerana venom has been reported to be twice as high has that of Apis mellifera (Benton and Morse, 1968).…”

Section: Resultsmentioning

confidence: 97%

Antimicrobial activity of crude venom extracts in honeybees (Apis cerana, Apis dorsata, Apis florea) tested against selected pathogens

Surendra¹,

Jayaram²,

Reddy³

2011

Afr. J. Microbiol. Res.

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Antimicrobial activity of crude venom extracts from different honeybee species was tested against selected pathogens. Toxicity of bee venom is known to man since ages, which varies from mild inflammations to death. Bee venom is synthesized in the venom glands of worker bees and queen and is stored in the venom sac. In the present study the toxic potentialities of honeybee venom pertaining to different honeybee species Apis cerana, Apis dorsata and Apis florea was carried out in vitro on selected species of bacteria and fungi. The selected bacteria and fungal species were Pseudomonas aeruginosa, Klebsiella pneumoniae, Escherichia coli, Xanthomonas subtilis, Proteus vulgaris, Salmonella typhimurium and Candida albicans. They were collected from St. John Medical College, Bangalore. The antimicrobial activity of different species of Apis bee venom (ABV) was studied by Disc Diffusion Assay. Minimal inhibitory concentration (MIC) was determined using Broth dilution method at lowest dilution (0.5 mg/ml). Bacterial growth was assessed by the measurement of inhibitory zone. The order of susceptibility of the pathogens against the ABV recorded was: A. cerana > Apis dorsata> Apis florea. The results showed that, ABV has significant antimicrobial effects and could be a potential alternative antibiotic.

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Section: Resultsmentioning

confidence: 97%

Antimicrobial activity of crude venom extracts in honeybees (Apis cerana, Apis dorsata, Apis florea) tested against selected pathogens

Surendra¹,

Jayaram²,

Reddy³

2011

Afr. J. Microbiol. Res.

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“…Defensin-like structures such as the defensins themselves and the lantibiotics show voltage-dependent formation of channels in artificial and biological membranes [17]. This voltage-dependence is shared by other bacteriocidins including colicins [13,20,27].…”

Section: Voltage-dependence Of the Lactacin-f-induced Membrane Conducmentioning

confidence: 99%

Bacterial membrane injuries induced by lactacin F and nisin

et al. 2002

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The combined action of nisin and lactacin F, two bacteriocins produced by lactic acid bacteria, is additive. In this report, the basis of this effect is examined. Channels formed by lactacin F were studied by experiments using planar lipid bilayers, and bactericidal effects were analyzed by flow cytometry. Lactacin F produced pores with a conductance of 1 ns in black lipid bilayers in 1 mM KCl at 10 mV at 20°C. Pore formation was strongly dependent on voltage. Although lactacin F formed pores at very low potential (10 mV), the dependence was exponential above 40 mV. The injuries induced by nisin and lactacin F in the membranes of Lactobacillus helveticus produced different flow cytometric profiles. Probably, when both bacteriocins are present, each acts separately; their cooperation may be due to an increase in the number of single membrane injuries.

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“…1) (17)(18)(19)(20). The latter are resistant to polymyxin, a cationic lipopeptide antibiotic (17)(18)(19), and to some of the cationic antimicrobial peptides of the innate immune system (21,22). The covalent appendages that confer polymyxin resistance ( Fig.…”

mentioning

confidence: 99%

Oxidative Decarboxylation of UDP-Glucuronic Acid in Extracts of Polymyxin-resistant Escherichia coli

Breazeale¹,

Ribeiro²,

Raetz³

2002

Journal of Biological Chemistry

102

148

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Addition of the 4-amino-4-deoxy-L-arabinose (L-Ara4NPmrI (renamed ArnA) was overexpressed using a T7 construct, and shown by itself to catalyze the unprecedented oxidative decarboxylation of UDP-glucuronic acid to form uridine 5-(␤-L-threo-pentapyranosyl-4؆-ulose diphosphate). A 6-mg sample of the latter was purified, and its structure was validated by NMR studies as the hydrate of the 4؆ ketone. ArnA resembles UDP-galactose epimerase, dTDP-glucose-4,6-dehydratase, and UDP-xylose synthase in oxidizing the C-4؆ position of its substrate, but differs in that it releases the NADH product.

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Cationic Bactericidal Peptides

Cited by 266 publications

References 202 publications

Antimicrobial activity of crude venom extracts in honeybees (Apis cerana, Apis dorsata, Apis florea) tested against selected pathogens

Antimicrobial activity of crude venom extracts in honeybees (Apis cerana, Apis dorsata, Apis florea) tested against selected pathogens

Bacterial membrane injuries induced by lactacin F and nisin

Oxidative Decarboxylation of UDP-Glucuronic Acid in Extracts of Polymyxin-resistant Escherichia coli

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