{"id":44190,"date":"2024-05-25T03:33:14","date_gmt":"2024-05-24T21:48:14","guid":{"rendered":"https:\/\/microbenotes.com\/?p=44190"},"modified":"2024-05-25T03:33:16","modified_gmt":"2024-05-24T21:48:16","slug":"bacteriocins-lantibiotics","status":"publish","type":"post","link":"https:\/\/microbenotes.com\/bacteriocins-lantibiotics\/","title":{"rendered":"Bacteriocins and Lantibiotics: Class, Functions, Examples"},"content":{"rendered":"\n<p><strong>Bacteriocins, small cationic molecules of about 30\u201360 <a href=\"https:\/\/microbenotes.com\/amino-acids-properties-structure-classification-and-functions\/\" data-type=\"post\" data-id=\"1030\">amino acids<\/a>, are proteinaceous compounds produced by lactic acid bacteria (LAB) having a bactericidal mode of action that can kill closely related bacteria.<\/strong><\/p>\n\n\n\n<ul>\n<li>In 1928, the prototype LAB bacteriocin, nisin, was first developed.<\/li>\n\n\n\n<li>Bacteriocins form amphiphilic helices and become stable at 100 \u00b0C for 10 min. They vary in the spectrum of activity, molecular weight (MW), origin of genetics, mode of action, and biochemical properties.<\/li>\n\n\n\n<li>LAB acts as a natural bio-preservative. It shows antimicrobial activities that can produce various metabolites, including lactic acid, hydrogen peroxide, and bacteriocins.\u00a0<\/li>\n\n\n\n<li>It has been used in food industries for fermenting food, such as for flavor and texture, and inhibiting the growth of spoilage and pathogenic microorganisms.\u00a0<\/li>\n\n\n\n<li>By the expression of a specific immunity protein encoded in the bacteriocin operon, LAB strains producing bacteriocin prevent themselves from <a href=\"https:\/\/microbenotes.com\/differences-between-exotoxins-and-endotoxins\/\" data-type=\"post\" data-id=\"40812\">toxins<\/a> produced by bacteriocin.<\/li>\n<\/ul>\n\n\n\n<div id=\"ez-toc-container\" class=\"ez-toc-v2_0_66_1 counter-hierarchy ez-toc-counter ez-toc-custom ez-toc-container-direction\">\n<div class=\"ez-toc-title-container\">\n<p class=\"ez-toc-title \" >Table of Contents<\/p>\n<span class=\"ez-toc-title-toggle\"><a href=\"#\" class=\"ez-toc-pull-right ez-toc-btn ez-toc-btn-xs ez-toc-btn-default ez-toc-toggle\" aria-label=\"Toggle Table of Content\"><span class=\"ez-toc-js-icon-con\"><span class=\"\"><span class=\"eztoc-hide\" style=\"display:none;\">Toggle<\/span><span class=\"ez-toc-icon-toggle-span\"><svg style=\"fill: #0a0a0a;color:#0a0a0a\" xmlns=\"http:\/\/www.w3.org\/2000\/svg\" class=\"list-377408\" width=\"20px\" height=\"20px\" viewBox=\"0 0 24 24\" fill=\"none\"><path d=\"M6 6H4v2h2V6zm14 0H8v2h12V6zM4 11h2v2H4v-2zm16 0H8v2h12v-2zM4 16h2v2H4v-2zm16 0H8v2h12v-2z\" fill=\"currentColor\"><\/path><\/svg><svg style=\"fill: #0a0a0a;color:#0a0a0a\" class=\"arrow-unsorted-368013\" xmlns=\"http:\/\/www.w3.org\/2000\/svg\" width=\"10px\" height=\"10px\" viewBox=\"0 0 24 24\" version=\"1.2\" baseProfile=\"tiny\"><path d=\"M18.2 9.3l-6.2-6.3-6.2 6.3c-.2.2-.3.4-.3.7s.1.5.3.7c.2.2.4.3.7.3h11c.3 0 .5-.1.7-.3.2-.2.3-.5.3-.7s-.1-.5-.3-.7zM5.8 14.7l6.2 6.3 6.2-6.3c.2-.2.3-.5.3-.7s-.1-.5-.3-.7c-.2-.2-.4-.3-.7-.3h-11c-.3 0-.5.1-.7.3-.2.2-.3.5-.3.7s.1.5.3.7z\"\/><\/svg><\/span><\/span><\/span><\/a><\/span><\/div>\n<nav><ul class='ez-toc-list ez-toc-list-level-1 ' ><li class='ez-toc-page-1 ez-toc-heading-level-2'><a class=\"ez-toc-link ez-toc-heading-1\" href=\"https:\/\/microbenotes.com\/bacteriocins-lantibiotics\/#class-of-lab-bacteriocins\" title=\"Class of LAB Bacteriocins\">Class of LAB Bacteriocins<\/a><ul class='ez-toc-list-level-3' ><li class='ez-toc-heading-level-3'><a class=\"ez-toc-link ez-toc-heading-2\" href=\"https:\/\/microbenotes.com\/bacteriocins-lantibiotics\/#class-i-bacteriocins\" title=\"Class I bacteriocins\">Class I bacteriocins<\/a><\/li><li class='ez-toc-page-1 ez-toc-heading-level-3'><a class=\"ez-toc-link ez-toc-heading-3\" href=\"https:\/\/microbenotes.com\/bacteriocins-lantibiotics\/#class-ii-bacteriocins\" title=\"Class II bacteriocins\">Class II bacteriocins<\/a><\/li><li class='ez-toc-page-1 ez-toc-heading-level-3'><a class=\"ez-toc-link ez-toc-heading-4\" href=\"https:\/\/microbenotes.com\/bacteriocins-lantibiotics\/#class-iii-bacteriocins\" title=\"Class III bacteriocins\">Class III bacteriocins<\/a><\/li><li class='ez-toc-page-1 ez-toc-heading-level-3'><a class=\"ez-toc-link ez-toc-heading-5\" href=\"https:\/\/microbenotes.com\/bacteriocins-lantibiotics\/#class-iv-bacteriocins\" title=\"Class IV bacteriocins\">Class IV bacteriocins<\/a><\/li><\/ul><\/li><li class='ez-toc-page-1 ez-toc-heading-level-2'><a class=\"ez-toc-link ez-toc-heading-6\" href=\"https:\/\/microbenotes.com\/bacteriocins-lantibiotics\/#what-are-lantibiotics\" title=\"What are Lantibiotics?\">What are Lantibiotics?<\/a><\/li><li class='ez-toc-page-1 ez-toc-heading-level-2'><a class=\"ez-toc-link ez-toc-heading-7\" href=\"https:\/\/microbenotes.com\/bacteriocins-lantibiotics\/#structural-aspects-of-lantibiotics\" title=\"Structural Aspects of Lantibiotics\">Structural Aspects of Lantibiotics<\/a><ul class='ez-toc-list-level-3' ><li class='ez-toc-heading-level-3'><a class=\"ez-toc-link ez-toc-heading-8\" href=\"https:\/\/microbenotes.com\/bacteriocins-lantibiotics\/#type-a-lantibiotics\" title=\"Type-A lantibiotics\">Type-A lantibiotics<\/a><\/li><li class='ez-toc-page-1 ez-toc-heading-level-3'><a class=\"ez-toc-link ez-toc-heading-9\" href=\"https:\/\/microbenotes.com\/bacteriocins-lantibiotics\/#type-b-lantibiotics\" title=\"Type-B lantibiotics\">Type-B lantibiotics<\/a><\/li><\/ul><\/li><li class='ez-toc-page-1 ez-toc-heading-level-2'><a class=\"ez-toc-link ez-toc-heading-10\" href=\"https:\/\/microbenotes.com\/bacteriocins-lantibiotics\/#mode-of-action-of-lantibiotics\" title=\"Mode of action of Lantibiotics\">Mode of action of Lantibiotics<\/a><\/li><li class='ez-toc-page-1 ez-toc-heading-level-2'><a class=\"ez-toc-link ez-toc-heading-11\" href=\"https:\/\/microbenotes.com\/bacteriocins-lantibiotics\/#class-of-lantibiotics\" title=\"Class of Lantibiotics\">Class of Lantibiotics<\/a><\/li><li class='ez-toc-page-1 ez-toc-heading-level-2'><a class=\"ez-toc-link ez-toc-heading-12\" href=\"https:\/\/microbenotes.com\/bacteriocins-lantibiotics\/#examples-of-lantibiotics\" title=\"Examples of Lantibiotics\">Examples of Lantibiotics<\/a><\/li><li class='ez-toc-page-1 ez-toc-heading-level-2'><a class=\"ez-toc-link ez-toc-heading-13\" href=\"https:\/\/microbenotes.com\/bacteriocins-lantibiotics\/#applications-of-lantibiotics\" title=\"Applications of Lantibiotics\">Applications of Lantibiotics<\/a><\/li><li class='ez-toc-page-1 ez-toc-heading-level-2'><a class=\"ez-toc-link ez-toc-heading-14\" href=\"https:\/\/microbenotes.com\/bacteriocins-lantibiotics\/#references\" title=\"References\">References<\/a><\/li><\/ul><\/nav><\/div>\n<h2 class=\"wp-block-heading\"><span class=\"ez-toc-section\" id=\"class-of-lab-bacteriocins\"><\/span><strong>Class of LAB Bacteriocins<\/strong><span class=\"ez-toc-section-end\"><\/span><\/h2>\n\n\n\n<p>According to Klaenhammer in 1993, based on their primary structures, molecular weights, post-translational modifications, and genetic characteristics, LAB bacteriocins are classified into four classes. <\/p>\n\n\n\n<figure class=\"wp-block-image size-full\"><img loading=\"lazy\" decoding=\"async\" width=\"1500\" height=\"1538\" src=\"https:\/\/microbenotes.com\/wp-content\/uploads\/2024\/05\/Class-of-Bacteriocins.jpeg\" alt=\"Class of Bacteriocins\" class=\"wp-image-44202\" srcset=\"https:\/\/microbenotes.com\/wp-content\/uploads\/2024\/05\/Class-of-Bacteriocins.jpeg 1500w, https:\/\/microbenotes.com\/wp-content\/uploads\/2024\/05\/Class-of-Bacteriocins-293x300.jpeg 293w, https:\/\/microbenotes.com\/wp-content\/uploads\/2024\/05\/Class-of-Bacteriocins-999x1024.jpeg 999w, https:\/\/microbenotes.com\/wp-content\/uploads\/2024\/05\/Class-of-Bacteriocins-768x787.jpeg 768w, https:\/\/microbenotes.com\/wp-content\/uploads\/2024\/05\/Class-of-Bacteriocins-1498x1536.jpeg 1498w\" sizes=\"(max-width: 1500px) 100vw, 1500px\" \/><figcaption class=\"wp-element-caption\">Image Source: Karpi\u0144ski, T., &amp; Szkaradkiewicz, A. (2016). Bacteriocins. In <em>Elsevier eBooks<\/em> (pp. 312\u2013319). https:\/\/doi.org\/10.1016\/b978-0-12-384947-2.00053-2.<\/figcaption><\/figure>\n\n\n\n<p><strong>They are:<\/strong><\/p>\n\n\n\n<ol>\n<li>Class I bacteriocins<\/li>\n\n\n\n<li>Class II bacteriocins\u00a0<\/li>\n\n\n\n<li>Class III bacteriocins\u00a0<\/li>\n\n\n\n<li>Class IV bacteriocins<\/li>\n<\/ol>\n\n\n\n<h3 class=\"wp-block-heading\"><span class=\"ez-toc-section\" id=\"class-i-bacteriocins\"><\/span><strong>Class I bacteriocins<\/strong><span class=\"ez-toc-section-end\"><\/span><\/h3>\n\n\n\n<ol><\/ol>\n\n\n\n<ul>\n<li><strong>Class I bacteriocins are called lantibiotics. <\/strong>They are small (&lt;5 kDa) peptides containing unique amino acids such as lanthionine (Lan) and \u03b2-methyllanthionine (MeLan).\u00a0<\/li>\n\n\n\n<li>It consists of some dehydrated amino acids.<\/li>\n\n\n\n<li>Examples are nisin, lacticin, and mersacidin. Cytolysin and lacticin are the two-component lantibiotics.\u00a0<em>Enterococcus faecalis<\/em>\u00a0produces cytolysin and\u00a0<em>Lactobacillus lactis subsp. lactis<\/em>\u00a0produces lacticin 3147.\u00a0<em>Staphylococcus aureus <\/em>produces<em>\u00a0<\/em>staphylococcin C55\u00a0<\/li>\n<\/ul>\n\n\n\n<h3 class=\"wp-block-heading\"><span class=\"ez-toc-section\" id=\"class-ii-bacteriocins\"><\/span><strong>Class II bacteriocins<\/strong><span class=\"ez-toc-section-end\"><\/span><\/h3>\n\n\n\n<ol start=\"2\"><\/ol>\n\n\n\n<ul>\n<li>Class II bacteriocins are small (&lt;10 kDa), heat-stable, non-modified, cationic, hydrophobic, and non-Lan-containing membrane-active peptides.\u00a0<\/li>\n\n\n\n<li>This class is classified into Class IIa, Class IIb, and Class IIc.\u00a0<\/li>\n<\/ul>\n\n\n\n<p><strong>Class IIa<\/strong><\/p>\n\n\n\n<ol><\/ol>\n\n\n\n<ul>\n<li>Class IIa contains a double\u2013glycine leader peptide and pediocin-like\u00a0<em>Listeria<\/em>\u00a0active peptides with the N-terminal consensus sequence YGNGV (Subclass IIa).\u00a0<\/li>\n\n\n\n<li>Examples are pediocin PA1, sakicin A, enterocin A and leucocin A. It is now more inclined toward food preservation, with pediocin PA1 and leucocin.<\/li>\n\n\n\n<li>Source: Class IIa bacteriocins isolated from fermented meat, fermented vegetables, dairy products, smoked salmon, and the human gastrointestinal tract. Examples are\u00a0<em>Leuconostoc gelidum.<\/em><\/li>\n<\/ul>\n\n\n\n<p><strong>Class IIb<\/strong><\/p>\n\n\n\n<ol start=\"2\"><\/ol>\n\n\n\n<ul>\n<li>Amphiphilic and hydrophobic regions are present in Class IIb bacteriocins, which are cationic.\u00a0<\/li>\n\n\n\n<li>It consists of synergies of two complementary peptides. Examples are lactococcin G, lacticin F, plantaricin A, and\u00a0\u00a0enterocin X. The class IIb components are produced by\u00a0<em>Enterococcus faecium.<\/em><\/li>\n<\/ul>\n\n\n\n<p><strong>Class IIc<\/strong><\/p>\n\n\n\n<ol start=\"3\"><\/ol>\n\n\n\n<ul>\n<li>Class IIc, the\u00a0<em>sec<\/em>-dependent secreted bacteriocins, affects membrane permeability and cell wall formation.<\/li>\n\n\n\n<li>Examples are acidocin B, entereocin P, and reuterin 6. The class IIc components producing species are\u00a0<em>Lactobacillus acidophilus.<\/em><\/li>\n<\/ul>\n\n\n\n<h3 class=\"wp-block-heading\"><span class=\"ez-toc-section\" id=\"class-iii-bacteriocins\"><\/span><strong>Class III bacteriocins<\/strong><span class=\"ez-toc-section-end\"><\/span><\/h3>\n\n\n\n<ol start=\"3\"><\/ol>\n\n\n\n<ul>\n<li>Members of Class III are large molecular mass peptides (>30 kDa) and are heat-labile proteins. Examples are lysostaphin, enterolysin A, and helveticin J.\u00a0<\/li>\n\n\n\n<li>The class III component-producing species is\u00a0<em>Lactobacillus helveticus, which produces helveticin J.<\/em><\/li>\n<\/ul>\n\n\n\n<h3 class=\"wp-block-heading\"><span class=\"ez-toc-section\" id=\"class-iv-bacteriocins\"><\/span><strong>Class IV bacteriocins<\/strong><span class=\"ez-toc-section-end\"><\/span><\/h3>\n\n\n\n<ol start=\"4\"><\/ol>\n\n\n\n<ul>\n<li>Class IV bacteriocins are complex types of bacteriocins that require large complexes of proteins with other macromolecules and non-proteinaceous moieties for activity.\u00a0<\/li>\n\n\n\n<li>This class has not been studied much yet at the biochemical level.<\/li>\n<\/ul>\n\n\n\n<h2 class=\"wp-block-heading\"><span class=\"ez-toc-section\" id=\"what-are-lantibiotics\"><\/span><strong>What are Lantibiotics?<\/strong><span class=\"ez-toc-section-end\"><\/span><\/h2>\n\n\n\n<p><strong>Lantibiotics, a type of bacteriocin, are synthesized ribosomally and post-translationally modified linear peptides. It has antimicrobial activity due to the presence of meso-lanthionine and 3-methyl-lanthionine.<\/strong><\/p>\n\n\n\n<figure class=\"wp-block-image size-full\"><img loading=\"lazy\" decoding=\"async\" width=\"1500\" height=\"786\" src=\"https:\/\/microbenotes.com\/wp-content\/uploads\/2024\/05\/Lantibiotics.jpeg\" alt=\"Lantibiotics\" class=\"wp-image-44195\" srcset=\"https:\/\/microbenotes.com\/wp-content\/uploads\/2024\/05\/Lantibiotics.jpeg 1500w, https:\/\/microbenotes.com\/wp-content\/uploads\/2024\/05\/Lantibiotics-300x157.jpeg 300w, https:\/\/microbenotes.com\/wp-content\/uploads\/2024\/05\/Lantibiotics-1024x537.jpeg 1024w, https:\/\/microbenotes.com\/wp-content\/uploads\/2024\/05\/Lantibiotics-768x402.jpeg 768w\" sizes=\"(max-width: 1500px) 100vw, 1500px\" \/><figcaption class=\"wp-element-caption\">Image Source: Davidson, V. L. (2010). Protein-Derived cofactors. In <em>Elsevier eBooks<\/em> (pp. 675\u2013710). https:\/\/doi.org\/10.1016\/b978-008045382-8.00143-x.<\/figcaption><\/figure>\n\n\n\n<ul>\n<li>Lantibiotics, lanthionine (lan)-containing antibiotic peptides, were first described in 1988.<\/li>\n\n\n\n<li>It consists of two alanine residues that connect at their -carbons by a thioether bridge. Moreover, they are incorporated within cyclic peptides.<\/li>\n\n\n\n<li>Lantibiotics, peptide-derived antimicrobial agents, are composed of unique amino acids, such as lanthionine (lan) and methyllanthionine (melan), so-called (lan)-containing antibiotics.<\/li>\n\n\n\n<li>It also contains dehydrated amino acids, D-amino acids, \u03b1-keto amides, and\u00a0<em>S<\/em>-aminovinylcysteine.<\/li>\n\n\n\n<li>Lantibiotics produced by lactic acid bacteria are generally recognized as safe (GRAS), which is not harmful to human health. It has been in use for food safety and clinical applications.\u00a0<\/li>\n\n\n\n<li>Gram-positive bacteria including the lactic acid bacteria (LAB), <em>Bacillus, Enterococcus, Micrococcus, Streptococcus, Staphylococcus,<\/em> and <em>Actinomycetes<\/em> produce lantibiotics that target other bacterial species during defense strategies.<\/li>\n\n\n\n<li>Before producing mature functional lantipeptide, it undergoes extensive post-translational modifications.<\/li>\n\n\n\n<li>Most lanthionine-containing RiPPs are lantibiotics that lack antimicrobial activity, referred to as lantipeptides.\u00a0<\/li>\n\n\n\n<li>Lantibiotics are active against various food spoilage organisms, such as\u00a0<em><a href=\"https:\/\/microbenotes.com\/biochemical-test-of-listeria-monocytogenes\/\" data-type=\"post\" data-id=\"1602\">Listeria monocytogenes<\/a><\/em>\u00a0and\u00a0<em><a href=\"https:\/\/microbenotes.com\/botulism-food-poisoning\/\" data-type=\"post\" data-id=\"35988\">Clostridium botulinum<\/a>. In addition<\/em>, It explicits promising activity against resistant\u00a0<em><a href=\"https:\/\/microbenotes.com\/staphylococcus-aureus\/\" data-type=\"post\" data-id=\"32229\">Staphylococcus aureus<\/a><\/em>\u00a0and enterococcal infections.<\/li>\n<\/ul>\n\n\n\n<figure class=\"wp-block-image size-full\"><img loading=\"lazy\" decoding=\"async\" width=\"1500\" height=\"1553\" src=\"https:\/\/microbenotes.com\/wp-content\/uploads\/2024\/05\/Posttranslational-modifications-that-have-been-reported-to-date-for-the-lantibiotic-family.jpeg\" alt=\"Posttranslational modifications that have been reported to date for the lantibiotic family\" class=\"wp-image-44198\" srcset=\"https:\/\/microbenotes.com\/wp-content\/uploads\/2024\/05\/Posttranslational-modifications-that-have-been-reported-to-date-for-the-lantibiotic-family.jpeg 1500w, https:\/\/microbenotes.com\/wp-content\/uploads\/2024\/05\/Posttranslational-modifications-that-have-been-reported-to-date-for-the-lantibiotic-family-290x300.jpeg 290w, https:\/\/microbenotes.com\/wp-content\/uploads\/2024\/05\/Posttranslational-modifications-that-have-been-reported-to-date-for-the-lantibiotic-family-989x1024.jpeg 989w, https:\/\/microbenotes.com\/wp-content\/uploads\/2024\/05\/Posttranslational-modifications-that-have-been-reported-to-date-for-the-lantibiotic-family-768x795.jpeg 768w, https:\/\/microbenotes.com\/wp-content\/uploads\/2024\/05\/Posttranslational-modifications-that-have-been-reported-to-date-for-the-lantibiotic-family-1484x1536.jpeg 1484w\" sizes=\"(max-width: 1500px) 100vw, 1500px\" \/><figcaption class=\"wp-element-caption\">Image Source: Cooper, L. E., Li, B., &amp; Van Der Donk, W. A. (2010). Biosynthesis and mode of action of lantibiotics. In <em>Elsevier eBooks<\/em> (pp. 217\u2013256). https:\/\/doi.org\/10.1016\/b978-008045382-8.00116-7.<\/figcaption><\/figure>\n\n\n\n<h2 class=\"wp-block-heading\"><span class=\"ez-toc-section\" id=\"structural-aspects-of-lantibiotics\"><\/span><strong>Structural Aspects of <strong>Lantibiotics<\/strong><\/strong><span class=\"ez-toc-section-end\"><\/span><\/h2>\n\n\n\n<p>Based on their structural and functional features, type-A and type-B peptides are a group of antibiotics.<\/p>\n\n\n\n<h3 class=\"wp-block-heading\"><span class=\"ez-toc-section\" id=\"type-a-lantibiotics\"><\/span><strong>Type-A lantibiotics<\/strong><span class=\"ez-toc-section-end\"><\/span><\/h3>\n\n\n\n<ol><\/ol>\n\n\n\n<ul>\n<li>Type-A lantibiotics are elongated and cationic peptides up to 34 residues in length. It shows similarities in the arrangement of their Lan bridges.\u00a0<\/li>\n\n\n\n<li>This peptide acts primarily in the membrane integrity of target organisms disrupts that includes nisin (the most-studied lantibiotic produced by <em>Lactococcus lactis<\/em>), subtilin, and epidermin.\u00a0<\/li>\n<\/ul>\n\n\n\n<h3 class=\"wp-block-heading\"><span class=\"ez-toc-section\" id=\"type-b-lantibiotics\"><\/span><strong>Type-B lantibiotics<\/strong><span class=\"ez-toc-section-end\"><\/span><\/h3>\n\n\n\n<ol start=\"2\"><\/ol>\n\n\n\n<ul>\n<li>Type-B lantibiotics are globular and have peptides up to 19 residues in length.\u00a0<\/li>\n\n\n\n<li>These peptides act by disrupting the enzyme function, such as inhibiting the cell wall biosynthesis.\u00a0<\/li>\n\n\n\n<li>The duramycins produced by\u00a0<em>Streptomyces<\/em>\u00a0species, and mersacidin produced by\u00a0<em>Bacillus<\/em>\u00a0species that are active against several Gram-positive bacteria include- <a href=\"https:\/\/microbenotes.com\/methicillin-resistant-staphylococcus-aureus-mrsa\/\" data-type=\"post\" data-id=\"1673\">methicillin-resistant\u00a0<em>S. aureus<\/em><\/a><em>\u00a0<\/em>and actagardine, which are examples of type-B antibiotics.\u00a0<\/li>\n<\/ul>\n\n\n\n<h2 class=\"wp-block-heading\"><span class=\"ez-toc-section\" id=\"mode-of-action-of-lantibiotics\"><\/span><strong>Mode of action of <strong>Lantibiotics<\/strong><\/strong><span class=\"ez-toc-section-end\"><\/span><\/h2>\n\n\n\n<ul>\n<li>Lantibiotics have various modes of action to destroy bacteria. The inhibition of bacterial growth occurs by peptides&#8217; ability to attach to lipid II and interfere with the bacterial cell wall&#8217;s production.<\/li>\n\n\n\n<li>In the <a href=\"https:\/\/microbenotes.com\/cell-membrane\/\" data-type=\"post\" data-id=\"40797\">cell membrane<\/a>, It can form pores, which results in the loss of cellular contents and cell death.\u00a0<\/li>\n\n\n\n<li>As a result of this dual mode of action, bacteria find it far more challenging to build functional resistance against lantibiotic peptides.\u00a0<\/li>\n\n\n\n<li>When used independently, two-component lantibiotics may only have one of these modes of action (binding to lipid II).\u00a0<\/li>\n\n\n\n<li>But when used in combination, they may have both modes of action (lipid II binding and pore creation).<\/li>\n<\/ul>\n\n\n\n<h2 class=\"wp-block-heading\"><span class=\"ez-toc-section\" id=\"class-of-lantibiotics\"><\/span><strong>Class of Lantibiotics<\/strong><span class=\"ez-toc-section-end\"><\/span><\/h2>\n\n\n\n<p>Based on their biosynthetic pathways, Lantibiotics are divided into four classes.<\/p>\n\n\n\n<ol>\n<li><strong>Class I lantibiotics<\/strong><\/li>\n<\/ol>\n\n\n\n<p>The two various enzymes, LanB (dehydratase) and LanC (cyclase) modify Class I lantibiotics.<\/p>\n\n\n\n<ol start=\"2\">\n<li><strong>Class II lantibiotics<\/strong><\/li>\n<\/ol>\n\n\n\n<p>A single LanM enzyme with dehydratase and cyclase activity modifies Class II lantibiotics.<\/p>\n\n\n\n<ol start=\"3\">\n<li><strong>Class III and Class IV lantibiotics<\/strong><\/li>\n<\/ol>\n\n\n\n<p>A single enzyme- LanKC- modifies class III, whereas LanL modifies class IV. In addition, Class III possesses anti-allodynic\/antinociceptive activity, antiviral activity, or morphogenetic activities.<\/p>\n\n\n\n<figure class=\"wp-block-image size-full\"><img loading=\"lazy\" decoding=\"async\" width=\"1500\" height=\"1672\" src=\"https:\/\/microbenotes.com\/wp-content\/uploads\/2024\/05\/Representative-examples-of-the-three-classes-of-lantibiotics.jpeg\" alt=\"Representative examples of the three classes of lantibiotics\" class=\"wp-image-44199\" srcset=\"https:\/\/microbenotes.com\/wp-content\/uploads\/2024\/05\/Representative-examples-of-the-three-classes-of-lantibiotics.jpeg 1500w, https:\/\/microbenotes.com\/wp-content\/uploads\/2024\/05\/Representative-examples-of-the-three-classes-of-lantibiotics-269x300.jpeg 269w, https:\/\/microbenotes.com\/wp-content\/uploads\/2024\/05\/Representative-examples-of-the-three-classes-of-lantibiotics-919x1024.jpeg 919w, https:\/\/microbenotes.com\/wp-content\/uploads\/2024\/05\/Representative-examples-of-the-three-classes-of-lantibiotics-768x856.jpeg 768w, https:\/\/microbenotes.com\/wp-content\/uploads\/2024\/05\/Representative-examples-of-the-three-classes-of-lantibiotics-1378x1536.jpeg 1378w\" sizes=\"(max-width: 1500px) 100vw, 1500px\" \/><figcaption class=\"wp-element-caption\">Image Source: Cooper, L. E., Li, B., &amp; Van Der Donk, W. A. (2010). Biosynthesis and mode of action of lantibiotics. In <em>Elsevier eBooks<\/em> (pp. 217\u2013256). https:\/\/doi.org\/10.1016\/b978-008045382-8.00116-7.<\/figcaption><\/figure>\n\n\n\n<h2 class=\"wp-block-heading\"><span class=\"ez-toc-section\" id=\"examples-of-lantibiotics\"><\/span><strong>Examples of Lantibiotics<\/strong><span class=\"ez-toc-section-end\"><\/span><\/h2>\n\n\n\n<figure class=\"wp-block-table\"><table><tbody><tr><td><strong>Lantibiotics<\/strong><\/td><td><strong>Producing Strains<\/strong><\/td><\/tr><tr><td>Type-A Lantibiotics<\/td><td><\/td><\/tr><tr><td>Type-A(I)- Nisin A<\/td><td><em>L. lactis<\/em>&nbsp;NIZOR5, 6F3, NCFB894, ATCC11454<\/td><\/tr><tr><td>Nisin Z<\/td><td><em>L. lactis<\/em>&nbsp;N8, NIZO22186<\/td><\/tr><tr><td>Subtilin<\/td><td><em><a href=\"https:\/\/microbenotes.com\/bacillus-subtilis\/\" data-type=\"post\" data-id=\"38717\">B. subtilis<\/a><\/em>\u00a0ATCC6633<\/td><\/tr><tr><td>Epidermin<\/td><td><em>Staphylococcus epidermidis<\/em>&nbsp;Tu3298<\/td><\/tr><tr><td>Gallidermin<\/td><td><em>Staphylococcus gallinarum<\/em>&nbsp;Tu3928<\/td><\/tr><tr><td>Mutacin B-Ny266<\/td><td><em><a href=\"https:\/\/microbenotes.com\/streptococcus-mutans\/\" data-type=\"post\" data-id=\"32528\">S. mutans<\/a><\/em><\/td><\/tr><tr><td>Mutacin 1140<\/td><td><em>S. mutans<\/em>&nbsp;JH1000<\/td><\/tr><tr><td>Pep5<\/td><td><em><a href=\"https:\/\/microbenotes.com\/staphylococcus-epidermidis\/\" data-type=\"post\" data-id=\"30829\">S. epidermidis<\/a><\/em>\u00a05<\/td><\/tr><tr><td>Epicidin 280<\/td><td><em>S. epidermidis<\/em>&nbsp;BN280<\/td><\/tr><tr><td>Epilancin K7<\/td><td><em>S. epidermidis<\/em>&nbsp;K7<\/td><\/tr><tr><td><strong>Type-A (II)<\/strong><br>&#8211; Lacticin 481<br>&#8211; Cytolysin<\/td><td><br><em>L. lactis<\/em>&nbsp;CNRZ481, ADRIA85LO30<br><em>E. faecalis<\/em>&nbsp;DS16<\/td><\/tr><tr><td>Lacticin 3147<\/td><td><em>L. lactis<\/em>&nbsp;DPC3147<\/td><\/tr><tr><td>Staphylococcin C55<\/td><td><em>S. aureus<\/em>&nbsp;C55<\/td><\/tr><tr><td>Salvaricin A<\/td><td><em>Streptococcus salvarius<\/em>&nbsp;20P3<\/td><\/tr><tr><td>Lactocin S<\/td><td><em>L. sake<\/em>&nbsp;L45<\/td><\/tr><tr><td>Streptococcin A-FF2<\/td><td><em>Streptococcus pyogenes<\/em>&nbsp;FF22<\/td><\/tr><tr><td>Sublancin 168<\/td><td><em>B. subtilis<\/em>&nbsp;168<\/td><\/tr><tr><td>Carnocin U149<\/td><td><em>C. pisicola<\/em><\/td><\/tr><tr><td>Variacin 8<\/td><td><em>Micrococcus varians<\/em>&nbsp;MCV8<\/td><\/tr><tr><td>Cypemycin<\/td><td><em>Streptomyces<\/em>&nbsp;ssp.<\/td><\/tr><tr><td><strong>Type-B antibiotics<\/strong><br>&#8211; Cinnamycin<br>&#8211; Duramycin B<\/td><td><br><em>Streptomyces cinnamoneus<\/em><br><em>Streptoverticillium<\/em>&nbsp;ssp.<\/td><\/tr><tr><td>Duramycin C<\/td><td><em>Streptomyces griseoluteus<\/em><\/td><\/tr><tr><td>Ancovenin<\/td><td><em>Streptomyces<\/em>&nbsp;ssp.<\/td><\/tr><tr><td>Mersacidin<\/td><td><em>B. subtilis<\/em>&nbsp;HIL Y-85, 54728<\/td><\/tr><tr><td>Actagardine<\/td><td><em>Actinoplanes<\/em><\/td><\/tr><\/tbody><\/table><figcaption class=\"wp-element-caption\">Source: Olivia M, Paul R, and Colin H. (2001).<\/figcaption><\/figure>\n\n\n\n<figure class=\"wp-block-image size-full\"><img loading=\"lazy\" decoding=\"async\" width=\"1500\" height=\"2032\" src=\"https:\/\/microbenotes.com\/wp-content\/uploads\/2024\/05\/Structures-of-the-37-lantibiotics-constructed-by-homology-modelling-in-ribbon-representation.jpeg\" alt=\"Structures of the 37 lantibiotics constructed by homology modelling in ribbon representation\" class=\"wp-image-44196\" srcset=\"https:\/\/microbenotes.com\/wp-content\/uploads\/2024\/05\/Structures-of-the-37-lantibiotics-constructed-by-homology-modelling-in-ribbon-representation.jpeg 1500w, https:\/\/microbenotes.com\/wp-content\/uploads\/2024\/05\/Structures-of-the-37-lantibiotics-constructed-by-homology-modelling-in-ribbon-representation-221x300.jpeg 221w, https:\/\/microbenotes.com\/wp-content\/uploads\/2024\/05\/Structures-of-the-37-lantibiotics-constructed-by-homology-modelling-in-ribbon-representation-756x1024.jpeg 756w, https:\/\/microbenotes.com\/wp-content\/uploads\/2024\/05\/Structures-of-the-37-lantibiotics-constructed-by-homology-modelling-in-ribbon-representation-768x1040.jpeg 768w, https:\/\/microbenotes.com\/wp-content\/uploads\/2024\/05\/Structures-of-the-37-lantibiotics-constructed-by-homology-modelling-in-ribbon-representation-1134x1536.jpeg 1134w\" sizes=\"(max-width: 1500px) 100vw, 1500px\" \/><figcaption class=\"wp-element-caption\">Image Source: Chakraborty, H.J., Gangopadhyay, A. &amp; Datta, A. Prediction and characterisation of lantibiotic structures with molecular modelling and molecular dynamics simulations.\u00a0<em>Sci Rep<\/em>\u00a0<strong>9<\/strong>, 7169 (2019). https:\/\/doi.org\/10.1038\/s41598-019-42963-8.<\/figcaption><\/figure>\n\n\n\n<h2 class=\"wp-block-heading\"><span class=\"ez-toc-section\" id=\"applications-of-lantibiotics\"><\/span><strong>Applications of <strong>Lantibiotics<\/strong><\/strong><span class=\"ez-toc-section-end\"><\/span><\/h2>\n\n\n\n<ol>\n<li>Lantibiotics are at the center of attraction in <a href=\"https:\/\/microbenotes.com\/chemical-preservatives-food-preservation-types-examples\/\" data-type=\"post\" data-id=\"39562\">food preservation<\/a> and safety. Examples: Nisin has been used extensively as a preservative against foodborne pathogens.<\/li>\n\n\n\n<li>It can be used in the field of human and animal therapeutics.<\/li>\n\n\n\n<li>It has been used in various potential medical applications and some in clinical trials.<\/li>\n\n\n\n<li>It helps to improve their\u00a0<em>in vivo<\/em>\u00a0efficacy under various conditions, such as stroke and diabetic nephropathy.<\/li>\n<\/ol>\n\n\n\n<h2 class=\"wp-block-heading\"><span class=\"ez-toc-section\" id=\"references\"><\/span><strong>References<\/strong><span class=\"ez-toc-section-end\"><\/span><\/h2>\n\n\n\n<ol>\n<li>Olivia McAuliffe, R. Paul Ross, Colin Hill, <a href=\"https:\/\/academic.oup.com\/femsre\/article\/25\/3\/285\/624045\" target=\"_blank\" data-type=\"link\" data-id=\"https:\/\/academic.oup.com\/femsre\/article\/25\/3\/285\/624045\" rel=\"noreferrer noopener\">Lantibiotics: structure, biosynthesis and mode of action<\/a>,\u00a0<em>FEMS Microbiology Reviews<\/em>, Volume 25, Issue 3, May 2001, Pages 285\u2013308,\u00a0https:\/\/doi.org\/10.1111\/j.1574-6976.2001.tb00579.x<\/li>\n\n\n\n<li>Field, D., Cotter, P. D., Hill, C., &amp; Ross, R. P. (2015). Bioengineering Lantibiotics for Therapeutic Success.\u00a0<em>Frontiers in microbiology<\/em>,\u00a0<em>6<\/em>, 1363. https:\/\/doi.org\/10.3389\/fmicb.2015.01363<\/li>\n\n\n\n<li>Ross, A., Vederas, J. Fundamental functionality: recent developments in understanding the structure\u2013activity relationships of lantibiotic peptides.\u00a0<em>J Antibiot<\/em>\u00a0<strong>64<\/strong>, 27\u201334 (2011). https:\/\/doi.org\/10.1038\/ja.2010.136<\/li>\n\n\n\n<li>Mokoena M. P. (2017). Lactic Acid Bacteria and Their Bacteriocins: Classification, Biosynthesis and Applications against Uropathogens: A Mini-Review.\u00a0<em>Molecules (Basel, Switzerland)<\/em>,\u00a0<em>22<\/em>(8), 1255. https:\/\/doi.org\/10.3390\/molecules22081255<\/li>\n\n\n\n<li>Olivia McAuliffe, R. Paul Ross, Colin Hill, Lantibiotics: structure, biosynthesis and mode of action,\u00a0<em>FEMS Microbiology Reviews<\/em>, Volume 25, Issue 3, May 2001, Pages 285\u2013308,\u00a0https:\/\/doi.org\/10.1111\/j.1574-6976.2001.tb00579.x<\/li>\n\n\n\n<li>van Staden, A. D. P., van Zyl, W. F., Trindade, M., Dicks, L. M. T., &amp; Smith, C. (2021). Therapeutic Application of Lantibiotics and Other Lanthipeptides: Old and New Findings.\u00a0<em>Applied and environmental microbiology<\/em>,\u00a0<em>87<\/em>(14), e0018621. https:\/\/doi.org\/10.1128\/AEM.00186-21<\/li>\n\n\n\n<li>Chakraborty, H.J., Gangopadhyay, A. &amp; Datta, A. Prediction and characterisation of lantibiotic structures with molecular modelling and molecular dynamics simulations.\u00a0<em>Sci Rep<\/em>\u00a0<strong>9<\/strong>, 7169 (2019). https:\/\/doi.org\/10.1038\/s41598-019-42963-8<\/li>\n<\/ol>\n","protected":false},"excerpt":{"rendered":"<p>Bacteriocins, small cationic molecules of about 30\u201360 amino acids, are proteinaceous compounds produced by lactic acid bacteria (LAB) having a bactericidal mode of action that can kill closely related bacteria. &#8230; <a title=\"Bacteriocins and Lantibiotics: Class, Functions, Examples\" class=\"read-more\" href=\"https:\/\/microbenotes.com\/bacteriocins-lantibiotics\/\" aria-label=\"Read more about Bacteriocins and Lantibiotics: Class, Functions, Examples\">Read more<\/a><\/p>\n","protected":false},"author":39,"featured_media":44195,"comment_status":"open","ping_status":"closed","sticky":false,"template":"","format":"standard","meta":{"footnotes":""},"categories":[1553],"tags":[],"custom":{"td_video":"","featured_image":"https:\/\/microbenotes.com\/wp-content\/uploads\/2024\/05\/Lantibiotics.jpeg","author":{"name":"Prativa Shrestha","avatar":"https:\/\/secure.gravatar.com\/avatar\/5651d3e55f18303d307f06538f08d923?s=96&d=mm&r=g"},"categories":[{"term_id":1553,"name":"Biochemistry","slug":"biochemistry","term_group":0,"term_taxonomy_id":1553,"taxonomy":"category","description":"<strong>Biochemistry is a branch of science that deals with the structure, composition, and metabolism of biomolecules found in different living organisms.<\/strong>\r\n<ul>\r\n \t<li>Biochemistry is also termed \u2018biological chemistry\u2019 as it deals with the chemistry of life that utilizes techniques from analytical, inorganic, and organic chemistry.<\/li>\r\n \t<li>Metabolic processes in living beings are composed of catabolic and anabolic processes. Both of these processes involve metabolic reactions involving biochemical compounds.<\/li>\r\n \t<li>Biochemistry is also used in techniques that help to understand the interactions, metabolism, and functions of biomolecules.<\/li>\r\n \t<li>Important biomolecules like proteins, carbohydrates, fats, nucleic acid, vitamins, etc. are essential structural and physiological components of living organisms.<\/li>\r\n \t<li>The study of the biochemical composition of living beings is important as it helps to understand the molecular mechanisms of various biochemical phenomena like respiration, photosynthesis, fermentation, etc.<\/li>\r\n \t<li>The findings of these studies, in turn, can be applied in industries, nutrition, medicine, and agriculture for different purposes.<\/li>\r\n \t<li>The rate of biochemical reactions, enzymes, and the concentration of substrates and products give essential information about the organism.<\/li>\r\n \t<li>Biochemical reactions form the basis of biochemical testing that is used for the identification and differentiation of microorganisms into different groups.<\/li>\r\n \t<li>Results of studies involving different biochemical tests can be applied for the production of pharmaceutical products that selectively inhibit certain metabolic processes.<\/li>\r\n \t<li>Techniques in biochemistry have been increasingly combined with techniques from other fields like agriculture, genetic, molecular biology, and biophysics.<\/li>\r\n \t<li>Biochemistry also allows the understanding of nutritional requirements for different living organisms.<\/li>\r\n \t<li>Biochemical compounds have been increasingly used even for the diagnosis of different diseases like diabetes.<\/li>\r\n \t<li>The determination of the genetic composition of living beings is also a part of biochemistry which helps in genetic studies and diagnosis of genetic diseases.<\/li>\r\n \t<li>Biochemical analysis of different biomolecules assists in the study relating to the origin and evolution of living beings.<\/li>\r\n \t<li>An understanding of different biochemical processes helps to understand the complexity of different groups of living beings and their relationship with one another.<\/li>\r\n<\/ul>","parent":0,"count":160,"filter":"raw","cat_ID":1553,"category_count":160,"category_description":"<strong>Biochemistry is a branch of science that deals with the structure, composition, and metabolism of biomolecules found in different living organisms.<\/strong>\r\n<ul>\r\n \t<li>Biochemistry is also termed \u2018biological chemistry\u2019 as it deals with the chemistry of life that utilizes techniques from analytical, inorganic, and organic chemistry.<\/li>\r\n \t<li>Metabolic processes in living beings are composed of catabolic and anabolic processes. Both of these processes involve metabolic reactions involving biochemical compounds.<\/li>\r\n \t<li>Biochemistry is also used in techniques that help to understand the interactions, metabolism, and functions of biomolecules.<\/li>\r\n \t<li>Important biomolecules like proteins, carbohydrates, fats, nucleic acid, vitamins, etc. are essential structural and physiological components of living organisms.<\/li>\r\n \t<li>The study of the biochemical composition of living beings is important as it helps to understand the molecular mechanisms of various biochemical phenomena like respiration, photosynthesis, fermentation, etc.<\/li>\r\n \t<li>The findings of these studies, in turn, can be applied in industries, nutrition, medicine, and agriculture for different purposes.<\/li>\r\n \t<li>The rate of biochemical reactions, enzymes, and the concentration of substrates and products give essential information about the organism.<\/li>\r\n \t<li>Biochemical reactions form the basis of biochemical testing that is used for the identification and differentiation of microorganisms into different groups.<\/li>\r\n \t<li>Results of studies involving different biochemical tests can be applied for the production of pharmaceutical products that selectively inhibit certain metabolic processes.<\/li>\r\n \t<li>Techniques in biochemistry have been increasingly combined with techniques from other fields like agriculture, genetic, molecular biology, and biophysics.<\/li>\r\n \t<li>Biochemistry also allows the understanding of nutritional requirements for different living organisms.<\/li>\r\n \t<li>Biochemical compounds have been increasingly used even for the diagnosis of different diseases like diabetes.<\/li>\r\n \t<li>The determination of the genetic composition of living beings is also a part of biochemistry which helps in genetic studies and diagnosis of genetic diseases.<\/li>\r\n \t<li>Biochemical analysis of different biomolecules assists in the study relating to the origin and evolution of living beings.<\/li>\r\n \t<li>An understanding of different biochemical processes helps to understand the complexity of different groups of living beings and their relationship with one another.<\/li>\r\n<\/ul>","cat_name":"Biochemistry","category_nicename":"biochemistry","category_parent":0}]},"_links":{"self":[{"href":"https:\/\/microbenotes.com\/wp-json\/wp\/v2\/posts\/44190"}],"collection":[{"href":"https:\/\/microbenotes.com\/wp-json\/wp\/v2\/posts"}],"about":[{"href":"https:\/\/microbenotes.com\/wp-json\/wp\/v2\/types\/post"}],"author":[{"embeddable":true,"href":"https:\/\/microbenotes.com\/wp-json\/wp\/v2\/users\/39"}],"replies":[{"embeddable":true,"href":"https:\/\/microbenotes.com\/wp-json\/wp\/v2\/comments?post=44190"}],"version-history":[{"count":3,"href":"https:\/\/microbenotes.com\/wp-json\/wp\/v2\/posts\/44190\/revisions"}],"predecessor-version":[{"id":44205,"href":"https:\/\/microbenotes.com\/wp-json\/wp\/v2\/posts\/44190\/revisions\/44205"}],"wp:featuredmedia":[{"embeddable":true,"href":"https:\/\/microbenotes.com\/wp-json\/wp\/v2\/media\/44195"}],"wp:attachment":[{"href":"https:\/\/microbenotes.com\/wp-json\/wp\/v2\/media?parent=44190"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/microbenotes.com\/wp-json\/wp\/v2\/categories?post=44190"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/microbenotes.com\/wp-json\/wp\/v2\/tags?post=44190"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}