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Bacteriocins
Bacteriocins are proteinaceous or peptide, peptidic toxins produced by bacteria to inhibit the growth of similar or closely related bacterial strain(s). They are similar to yeast and paramecium killing factors, and are structurally, functionally, and ecologically diverse. Applications of bacteriocins are being tested to assess their application as narrow-spectrum antibiotics. Bacteriocins were first discovered by André Gratia in 1925. He was involved in the process of searching for ways to kill bacteria, which also resulted in the development of antibiotics and the discovery of bacteriophage, all within a span of a few years. He called his first discovery a ''colicine'' because it killed ''Escherichia coli, E. coli.'' Classification Bacteriocins are categorized in several ways, including producing strain, common resistance mechanisms, and mechanism of killing. There are several large categories of bacteriocin which are only phenomenologically related. These include the ba ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Class II Bacteriocins
Class II bacteriocins are a class of small peptides that inhibit the growth of various bacteria. Many Gram-positive bacteria produce ribosomally synthesized antimicrobial peptides, termed bacteriocins. Bacteriocins for which disulfide bonds are the only modification to the peptide are Class II bacteriocins. Class IIa One important and well studied class of bacteriocins is the class IIa or pediocin-like bacteriocins produced by lactic acid bacteria. All class IIa bacteriocins are produced by food-associated strains, isolated from a variety of food products of industrial and natural origins, including meat products, dairy products and vegetables. Class IIa bacteriocins are all cationic, display anti-''Listeria'' activity, and kill target cells by permeabilizing the cell membrane. Class IIa bacteriocins contain between 37 and 48 residues. Based on their primary structures, the peptide chains of class IIa bacteriocins may be divided roughly into two regions: a hydrophilic, cationi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ribosomally Synthesized And Post-translationally Modified Peptides
Ribosomally synthesized and post-translationally modified peptides (RiPPs), also known as ribosomal natural products, are a diverse class of natural products of ribosomal origin. Consisting of more than 20 sub-classes, RiPPs are produced by a variety of organisms, including prokaryotes, eukaryotes, and archaea, and they possess a wide range of biological functions. As a consequence of the falling cost of genome sequencing and the accompanying rise in available genomic data, scientific interest in RiPPs has increased in the last few decades. Because the chemical structures of RiPPs are more closely predictable from genomic data than are other natural products (e.g. alkaloids, terpenoids), their presence in sequenced organisms can, in theory, be identified rapidly. This makes RiPPs an attractive target of modern natural product discovery efforts. Definition RiPPs consist of any peptides (i.e. molecular weight below 10 kDa) that are ribosomally-produced and undergo some degree ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Lantibiotic
Lantibiotics are a class of polycyclic peptide antibiotics that contain the characteristic thioether amino acids lanthionine or methyllanthionine, as well as the unsaturated amino acids dehydroalanine, and 2-aminoisobutyric acid. They belong to ribosomally synthesized and post-translationally modified peptides. Lanthionine is composed of two alanine residues that are crosslinked on their β-carbon atoms by a thioether (monosulfide) linkage. Lantibiotics are produced by a large number of Gram-positive bacteria such as ''Streptococcus'' and ''Streptomyces'' to attack other Gram-positive bacteria, and as such, they are considered a member of the bacteriocins. Bacteriocins are classified according to their extent of posttranslational modification. The lantibiotics are a class of more extensively modified bacteriocins, also called Class I bacteriocins. (Bacteriocins for which disulfide bonds are the only modification to the peptide are Class II bacteriocins.) Lantibiotics are well ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Lantibiotics
Lantibiotics are a class of polycyclic peptide antibiotics that contain the characteristic thioether amino acids lanthionine or methyllanthionine, as well as the unsaturated amino acids dehydroalanine, and 2-aminoisobutyric acid. They belong to ribosomally synthesized and post-translationally modified peptides. Lanthionine is composed of two alanine residues that are crosslinked on their β-carbon atoms by a thioether (monosulfide) linkage. Lantibiotics are produced by a large number of Gram-positive bacteria such as '' Streptococcus'' and ''Streptomyces'' to attack other Gram-positive bacteria, and as such, they are considered a member of the bacteriocins. Bacteriocins are classified according to their extent of posttranslational modification. The lantibiotics are a class of more extensively modified bacteriocins, also called Class I bacteriocins. (Bacteriocins for which disulfide bonds are the only modification to the peptide are Class II bacteriocins.) Lantibiotics a ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Colicins
A colicin is a type of bacteriocin produced by and toxic to some strains of ''Escherichia coli''. Colicins are released into the environment to reduce competition from other bacterial strains. Colicins bind to outer membrane receptors, using them to translocate to the cytoplasm or cytoplasmic membrane, where they exert their cytotoxic effect, including depolarisation of the cytoplasmic membrane, DNase activity, RNase activity, or inhibition of murein synthesis. Structure Channel-forming colicins (colicins A, B, E1, Ia, Ib, and N) are transmembrane proteins that depolarize the cytoplasmic membrane, leading to dissipation of cellular energy. These colicins contain at least three domains: an N-terminal translocation domain responsible for movement across the outer membrane and periplasmic space; a central domain responsible for receptor recognition; and a C-terminal cytotoxic domain responsible for channel formation in the cytoplasmic membrane. One domain regulates the target an ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Colicins
A colicin is a type of bacteriocin produced by and toxic to some strains of ''Escherichia coli''. Colicins are released into the environment to reduce competition from other bacterial strains. Colicins bind to outer membrane receptors, using them to translocate to the cytoplasm or cytoplasmic membrane, where they exert their cytotoxic effect, including depolarisation of the cytoplasmic membrane, DNase activity, RNase activity, or inhibition of murein synthesis. Structure Channel-forming colicins (colicins A, B, E1, Ia, Ib, and N) are transmembrane proteins that depolarize the cytoplasmic membrane, leading to dissipation of cellular energy. These colicins contain at least three domains: an N-terminal translocation domain responsible for movement across the outer membrane and periplasmic space; a central domain responsible for receptor recognition; and a C-terminal cytotoxic domain responsible for channel formation in the cytoplasmic membrane. One domain regulates the target an ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Food Preservation
Food preservation includes processes that make food more resistant to microorganism growth and slow the oxidation of fats. This slows down the decomposition and rancidification process. Food preservation may also include processes that inhibit visual deterioration, such as the enzymatic browning reaction in apples after they are cut during food preparation. By preserving food, food waste can be reduced, which is an important way to decrease production costs and increase the efficiency of food systems, improve food security and nutrition and contribute towards environmental sustainability. For instance, it can reduce the environmental impact of food production. Many processes designed to preserve food involve more than one food preservation method. Preserving fruit by turning it into jam, for example, involves boiling (to reduce the fruit's moisture content and to kill bacteria, etc.), sugaring (to prevent their re-growth) and sealing within an airtight jar (to prevent re ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Microcin
Microcins are very small bacteriocins, composed of relatively few amino acids. For this reason, they are distinct from their larger protein cousins. The classic example is microcin V, of ''Escherichia coli''. Subtilosin A is another bacteriocin from ''Bacillus subtilis''. The peptide has a cyclized backbone and forms three cross-links between the sulphurs of Cys13, Cys7 and Cys4 and the alpha-positions of Phe22, Thr28 and Phe31. Microcins produced by commensal ''E. coli'' strains target and eliminate enteric pathogens such as ''Salmonella enterica'' by mimicking the siderophore Siderophores (Greek: "iron carrier") are small, high-affinity iron- chelating compounds that are secreted by microorganisms such as bacteria and fungi. They help the organism accumulate iron. Although a widening range of siderophore functions is n ...s the pathogens use for iron scavenging. Microcins also help commensal strains of ''E. coli'' outcompete pathogenic strains. BACTIBASE database is an op ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Microcin V
Microcins are very small bacteriocins, composed of relatively few amino acids. For this reason, they are distinct from their larger protein cousins. The classic example is microcin V, of ''Escherichia coli''. Subtilosin A is another bacteriocin from ''Bacillus subtilis''. The peptide has a cyclized backbone and forms three cross-links between the sulphurs of Cys13, Cys7 and Cys4 and the alpha-positions of Phe22, Thr28 and Phe31. Microcins produced by commensal ''E. coli'' strains target and eliminate enteric pathogens such as ''Salmonella enterica'' by mimicking the siderophore Siderophores (Greek: "iron carrier") are small, high-affinity iron-chelating compounds that are secreted by microorganisms such as bacteria and fungi. They help the organism accumulate iron. Although a widening range of siderophore functions is no ...s the pathogens use for iron scavenging. Microcins also help commensal strains of ''E. coli'' outcompete pathogenic strains. BACTIBASE database is an op ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Microcins
Microcins are very small bacteriocins, composed of relatively few amino acids. For this reason, they are distinct from their larger protein cousins. The classic example is microcin V, of ''Escherichia coli''. Subtilosin A is another bacteriocin from ''Bacillus subtilis''. The peptide has a cyclized backbone and forms three cross-links between the sulphurs of Cys13, Cys7 and Cys4 and the alpha-positions of Phe22, Thr28 and Phe31. Microcins produced by commensal ''E. coli'' strains target and eliminate enteric pathogens such as ''Salmonella enterica'' by mimicking the siderophore Siderophores (Greek: "iron carrier") are small, high-affinity iron- chelating compounds that are secreted by microorganisms such as bacteria and fungi. They help the organism accumulate iron. Although a widening range of siderophore functions is n ...s the pathogens use for iron scavenging. Microcins also help commensal strains of ''E. coli'' outcompete pathogenic strains. BACTIBASE database is an op ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Pyocin
Pyocins are bacteriocins produced by bacteria belonging to the ''Pseudomonas'' genus. François Jacob François Jacob (17 June 1920 – 19 April 2013) was a French biologist who, together with Jacques Monod, originated the idea that control of enzyme levels in all cells occurs through regulation of transcription. He shared the 1965 Nobel Prize i ... described the first pyocin in 1954. Pyocins can be divided into three distinct classes: S-type, R-type, and F-type pyocins. S-type pyocins are colicin-like bacteriocins as R-type and F-type pyocins belong to tailocins. S-type pyocins S-type (soluble) pyocins are binary protein complexes that compose of a cytotoxic protein and an immunity protein that protects the producing strain from cytotoxic effects. The amino-terminal domain of the protein takes part in receptor binding as the carboxy-terminal domain is responsible for cytotoxic effect. Most S-type pyocins act by degrading DNA and RNA but some exhibit their cytotoxicity by form ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Nisin
Nisin is a polycyclic antibacterial peptide produced by the bacterium '' Lactococcus lactis'' that is used as a food preservative. It has 34 amino acid residues, including the uncommon amino acids lanthionine (Lan), methyllanthionine (MeLan), didehydroalanine (Dha), and didehydroaminobutyric acid (Dhb). These unusual amino acids are introduced by posttranslational modification of the precursor peptide. In these reactions a ribosomally synthesized 57-mer is converted to the final peptide. The unsaturated amino acids originate from serine and threonine, and the enzyme-catalysed addition of cysteine residues to the didehydro amino acids result in the multiple (5) thioether bridges. Subtilin and epidermin are related to nisin. All are members of a class of molecules known as lantibiotics. In the food industry, nisin is obtained from the culturing of ''L. lactis'' on natural substrates, such as milk or dextrose, and it is not chemically synthesized. It was originally isolated ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
