Macedocin, a Food-Grade Lantibiotic Produced by
            <i>Streptococcus macedonicus</i>
            ACA-DC 198

Georgalaki, Marina; Berghe, Erika Van den; Kritikos, Dimitrios; Devreese, Bart; Beeumen, Jozef Van; Kalantzopoulos, George; Vuyst, Luc De; Tsakalidou, Effie

doi:10.1128/aem.68.12.5891-5903.2002

Cited by 96 publications

(85 citation statements)

References 65 publications

(71 reference statements)

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“…Similar wide range pH activity was reported in other bacteria such as Cornobacterium piscicola C5526 and Streptococcus macedonicus ACA-DC 198 (Georgalaki et al, 2002).…”

Section: Bacteriocin Productionsupporting

confidence: 57%

Antimicrobial Activity and Characterization of Bacteriocin of Acetobacter tropicalis S3O1: A Novel Methionine Producing Bacteria Isolated from Sago Industrial Waste

Arunkumar¹,

Sundharam²

2017

Int.J.Curr.Microbiol.App.Sci

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“…Similar wide range pH activity was reported in other bacteria such as Cornobacterium piscicola C5526 and Streptococcus macedonicus ACA-DC 198 (Georgalaki et al, 2002).…”

Section: Bacteriocin Productionsupporting

confidence: 57%

Antimicrobial Activity and Characterization of Bacteriocin of Acetobacter tropicalis S3O1: A Novel Methionine Producing Bacteria Isolated from Sago Industrial Waste

Arunkumar¹,

Sundharam²

2017

Int.J.Curr.Microbiol.App.Sci

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“…In this medium, we repeatedly found a growth delay of S. aureus, which was not found in nutrient-rich media like brain heart infusion. This could be due to the autoinhibition, which has been described for other Gram-positive bacteria (30,31).…”

Section: Antibacterial Activity Of All-38 and Ll-37mentioning

confidence: 99%

Processing of Seminal Plasma hCAP-18 to ALL-38 by Gastricsin

Sorensen

Gram²,

Johnsen

et al. 2003

Journal of Biological Chemistry

139

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The human cathelicidin, hCAP-18, is expressed both in neutrophils and in epithelial cells. hCAP-18 is processed to the antimicrobial peptide LL-37 by proteinase 3 in neutrophils. hCAP-18 is highly expressed in the epididymis with a subsequent high concentration in seminal plasma where the protein is present in its unprocessed and antimicrobially inactive form. We report here that hCAP-18 in seminal plasma is processed to generate a 38-amino acid antimicrobial peptide ALL-38 by the prostate-derived protease gastricsin when incubated at a pH corresponding to the vaginal pH. In accordance with this, seminal plasma derived hCAP-18 was found in its processed form in the vagina following sexual intercourse. The antimicrobial activity of ALL-38 against a variety of microorganisms tested is equal to that of LL-37. This enzymatic activation of a proantimicrobial substance in seminal plasma following exposure to the vaginal milieu represents a novel mechanism to prevent infection following sexual intercourse.Antimicrobial peptides are important effector molecules of the innate immune system from insects to humans (1, 2). The peptides are active against a broad spectrum of Gram-positive and Gram-negative bacteria as well as some fungi and enveloped viruses. These peptides may play a role in the regulation of the normal microflora (3). In mammals, the antimicrobial peptides are of major importance for the antimicrobial efficacy of professional phagocytes such as neutrophils and macrophages, but the peptides are also expressed in epithelial cells (4). In mammals, there are two large families of antimicrobial peptides, defensins and cathelicidins. Defensins are divided into the ␣-defensins found in neutrophils, macrophages, and Paneth cells in the small intestine, and the ␤-defensins, which are found widespread in epithelial cells. Cathelicidins are found mainly in neutrophils (5). Members of this protein family share a highly conserved N terminus of 12 kDa, named cathelin after a protein isolated from porcine neutrophils (6).Antimicrobial peptides are synthesized as preproproteins and (with the exception of defensins in neutrophils) stored as inactive proproteins (7). In order to become biologically active, the peptides must be liberated from the proproteins by proteolytic cleavage.The proteolytic generation of antimicrobial peptides is very important for the clearance of bacteria at sites of infection. In mice, ␣-defensins from Paneth cells in the small intestine are generated by matrilysin-mediated cleavage of prodefensins, and matrilysin knock-out mice have increased susceptibility to intestinal infections (8). Inhibition of activation of the porcine neutrophil cathelicidins by elastase impairs clearance of bacteria from wounds in vivo (9).The only human cathelicidin, hCAP-18, is a major protein of the specific granules of human neutrophils (10). It is processed to the antimicrobial peptide LL-37 by extracellular cleavage by proteinase 3 from azurophil granules following exocytosis (11). LL-37 has broad spectrum antimicro...

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“…Biochemical characterization: Qualitative tests for Protease (Georgalaki et al, 2002, Mubarik et al, 2010 (Sarkar et al, 2008;AlQuadan et al, 2009). Protease was quantified by using spectrophotometric method as reported by (Malathu et al, 2008;Mubarik et al, 2010).…”

Section: Morphological Characterizationmentioning

confidence: 99%

Condoms-As Sources of Extracellular Enzyme Producing Microbes

Mishra¹

2010

American Journal of Microbiology

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Problem statement: Condoms are widely used birth control measures which are made of natural latex or synthetic materials like polyurethane or polyisoprene as matrix with lubricants added to make them ready to use commodities. Absence of sterilization method along with presence of lubricant like petroleum jelly (that are applied on the outer surface), prompted the investigators to look for microbes from the surface of male condoms. Approach: The culture based method was used for the study. This study reports the isolation and preliminary characterization of microbes from unused new condoms of ten different brands available in the chemist's shop in Kolkata, India. Results: The microbial count varies between 0-3×10 10 in samples obtained from different batches. Thirty four microbial isolates were selected for their colony and cell morphology as well as biochemical characterization. Ten among them were picked up for antibiotic sensitivity testing, quorum sensing behaviour and swimming and swarming behavior while six of them were characterized at the molecular level (16S rDNA). Most of the isolates were lipase producing. 10Gray of 60 Co gamma ray was found to be effective to decontaminate the condoms. Conclusion/Recommendations: The growth due to contamination might be supported by the lubricant. Hence it is time to consider seriously the need to maintain aseptic conditions during manufacturing.

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Macedocin, a Food-Grade Lantibiotic Produced by Streptococcus macedonicus ACA-DC 198

Cited by 96 publications

References 65 publications

Antimicrobial Activity and Characterization of Bacteriocin of Acetobacter tropicalis S3O1: A Novel Methionine Producing Bacteria Isolated from Sago Industrial Waste

Antimicrobial Activity and Characterization of Bacteriocin of Acetobacter tropicalis S3O1: A Novel Methionine Producing Bacteria Isolated from Sago Industrial Waste

Processing of Seminal Plasma hCAP-18 to ALL-38 by Gastricsin

Condoms-As Sources of Extracellular Enzyme Producing Microbes

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