Chicken cathelicidin-2-derived peptides with enhanced immunomodulatory and antibacterial activities against biological warfare agents
Abstract Host defence peptides (HDPs) are considered to be excellent candidates for the development of novel therapeutic agents. Recently, it was demonstrated that the peptide C1-15, an N -terminal segment of chicken HDP cathelicidin-2, exhibits potent antibacterial activity while lacking cytotoxici...
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| Veröffentlicht in: | International journal of antimicrobial agents 2010-09, Vol.36 (3), p.271-274 |
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| creator | Molhoek, E. Margo van Dijk, Albert Veldhuizen, Edwin J.A Dijk-Knijnenburg, Helma Mars-Groenendijk, Roos H Boele, Linda C.L Kaman-van Zanten, Wendy E Haagsman, Henk P Bikker, Floris J |
| description | Abstract Host defence peptides (HDPs) are considered to be excellent candidates for the development of novel therapeutic agents. Recently, it was demonstrated that the peptide C1-15, an N -terminal segment of chicken HDP cathelicidin-2, exhibits potent antibacterial activity while lacking cytotoxicity towards eukaryotic cells. In the present study, we report that C1-15 is active against bacteria such as Bacillus anthracis and Yersinia pestis that may potentially be used by bioterrorists. Substitution of single and multiple phenylalanine (Phe) residues to tryptophan (Trp) in C1-15 resulted in variants with improved antibacterial activity against B. anthracis and Y. pestis as well as decreased salt sensitivity. In addition, these peptides exhibited enhanced neutralisation of lipopolysaccharide (LPS)-induced release of pro-inflammatory cytokines in human peripheral blood mononuclear cells (PBMCs). The antibacterial and LPS-neutralising activities of these C1-15-derived peptides are exerted at concentrations far below the concentrations that are toxic to human PBMCs. Taken together, we show that Phe → Trp substitutions in C1-15 variants enhances the antibacterial and LPS-neutralising activities against pathogenic bacteria, including those that may potentially be used as biological warfare agents. |
| doi_str_mv | 10.1016/j.ijantimicag.2010.06.001 |
| format | Article |
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Margo ; van Dijk, Albert ; Veldhuizen, Edwin J.A ; Dijk-Knijnenburg, Helma ; Mars-Groenendijk, Roos H ; Boele, Linda C.L ; Kaman-van Zanten, Wendy E ; Haagsman, Henk P ; Bikker, Floris J</creator><creatorcontrib>Molhoek, E. Margo ; van Dijk, Albert ; Veldhuizen, Edwin J.A ; Dijk-Knijnenburg, Helma ; Mars-Groenendijk, Roos H ; Boele, Linda C.L ; Kaman-van Zanten, Wendy E ; Haagsman, Henk P ; Bikker, Floris J</creatorcontrib><description>Abstract Host defence peptides (HDPs) are considered to be excellent candidates for the development of novel therapeutic agents. Recently, it was demonstrated that the peptide C1-15, an N -terminal segment of chicken HDP cathelicidin-2, exhibits potent antibacterial activity while lacking cytotoxicity towards eukaryotic cells. In the present study, we report that C1-15 is active against bacteria such as Bacillus anthracis and Yersinia pestis that may potentially be used by bioterrorists. Substitution of single and multiple phenylalanine (Phe) residues to tryptophan (Trp) in C1-15 resulted in variants with improved antibacterial activity against B. anthracis and Y. pestis as well as decreased salt sensitivity. In addition, these peptides exhibited enhanced neutralisation of lipopolysaccharide (LPS)-induced release of pro-inflammatory cytokines in human peripheral blood mononuclear cells (PBMCs). The antibacterial and LPS-neutralising activities of these C1-15-derived peptides are exerted at concentrations far below the concentrations that are toxic to human PBMCs. Taken together, we show that Phe → Trp substitutions in C1-15 variants enhances the antibacterial and LPS-neutralising activities against pathogenic bacteria, including those that may potentially be used as biological warfare agents.</description><identifier>ISSN: 0924-8579</identifier><identifier>EISSN: 1872-7913</identifier><identifier>DOI: 10.1016/j.ijantimicag.2010.06.001</identifier><identifier>PMID: 20630709</identifier><language>eng</language><publisher>Amsterdam: Elsevier B.V</publisher><subject>Amino Acid Substitution - genetics ; Animals ; Anti-Bacterial Agents - pharmacology ; Anti-Bacterial Agents - toxicity ; Antibacterial activity ; Antibiotics. Antiinfectious agents. Antiparasitic agents ; Antimicrobial Cationic Peptides - genetics ; Antimicrobial Cationic Peptides - pharmacology ; Antimicrobial Cationic Peptides - toxicity ; Bacillus anthracis ; Bacillus anthracis - drug effects ; Biological and medical sciences ; Biological Warfare Agents ; Cathelicidin ; Chickens ; Colony Count, Microbial ; Cytokines - secretion ; Cytotoxicity ; Host defence peptide ; Humans ; Immunologic Factors - genetics ; Immunologic Factors - pharmacology ; Immunologic Factors - toxicity ; Immunomodulatory activity ; Infectious Disease ; Leukocytes, Mononuclear - drug effects ; Leukocytes, Mononuclear - immunology ; Lipopolysaccharides - antagonists & inhibitors ; Medical sciences ; Methicillin-Resistant Staphylococcus aureus - drug effects ; Microbial Viability - drug effects ; Pharmacology. Drug treatments ; Vibrio cholerae - drug effects ; Yersinia pestis - drug effects</subject><ispartof>International journal of antimicrobial agents, 2010-09, Vol.36 (3), p.271-274</ispartof><rights>Elsevier B.V. and the International Society of Chemotherapy</rights><rights>2010 Elsevier B.V. and the International Society of Chemotherapy</rights><rights>2015 INIST-CNRS</rights><rights>Copyright (c) 2010 Elsevier B.V. and the International Society of Chemotherapy. All rights reserved.</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c578t-84353d64558ea29b9fb037c09561dd1f18a3857d8ee08cc6110123cec3fd56473</citedby><cites>FETCH-LOGICAL-c578t-84353d64558ea29b9fb037c09561dd1f18a3857d8ee08cc6110123cec3fd56473</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0924857910002384$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,314,776,780,881,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=23071929$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20630709$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-00608992$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Molhoek, E. Margo</creatorcontrib><creatorcontrib>van Dijk, Albert</creatorcontrib><creatorcontrib>Veldhuizen, Edwin J.A</creatorcontrib><creatorcontrib>Dijk-Knijnenburg, Helma</creatorcontrib><creatorcontrib>Mars-Groenendijk, Roos H</creatorcontrib><creatorcontrib>Boele, Linda C.L</creatorcontrib><creatorcontrib>Kaman-van Zanten, Wendy E</creatorcontrib><creatorcontrib>Haagsman, Henk P</creatorcontrib><creatorcontrib>Bikker, Floris J</creatorcontrib><title>Chicken cathelicidin-2-derived peptides with enhanced immunomodulatory and antibacterial activities against biological warfare agents</title><title>International journal of antimicrobial agents</title><addtitle>Int J Antimicrob Agents</addtitle><description>Abstract Host defence peptides (HDPs) are considered to be excellent candidates for the development of novel therapeutic agents. Recently, it was demonstrated that the peptide C1-15, an N -terminal segment of chicken HDP cathelicidin-2, exhibits potent antibacterial activity while lacking cytotoxicity towards eukaryotic cells. In the present study, we report that C1-15 is active against bacteria such as Bacillus anthracis and Yersinia pestis that may potentially be used by bioterrorists. Substitution of single and multiple phenylalanine (Phe) residues to tryptophan (Trp) in C1-15 resulted in variants with improved antibacterial activity against B. anthracis and Y. pestis as well as decreased salt sensitivity. In addition, these peptides exhibited enhanced neutralisation of lipopolysaccharide (LPS)-induced release of pro-inflammatory cytokines in human peripheral blood mononuclear cells (PBMCs). The antibacterial and LPS-neutralising activities of these C1-15-derived peptides are exerted at concentrations far below the concentrations that are toxic to human PBMCs. Taken together, we show that Phe → Trp substitutions in C1-15 variants enhances the antibacterial and LPS-neutralising activities against pathogenic bacteria, including those that may potentially be used as biological warfare agents.</description><subject>Amino Acid Substitution - genetics</subject><subject>Animals</subject><subject>Anti-Bacterial Agents - pharmacology</subject><subject>Anti-Bacterial Agents - toxicity</subject><subject>Antibacterial activity</subject><subject>Antibiotics. Antiinfectious agents. Antiparasitic agents</subject><subject>Antimicrobial Cationic Peptides - genetics</subject><subject>Antimicrobial Cationic Peptides - pharmacology</subject><subject>Antimicrobial Cationic Peptides - toxicity</subject><subject>Bacillus anthracis</subject><subject>Bacillus anthracis - drug effects</subject><subject>Biological and medical sciences</subject><subject>Biological Warfare Agents</subject><subject>Cathelicidin</subject><subject>Chickens</subject><subject>Colony Count, Microbial</subject><subject>Cytokines - secretion</subject><subject>Cytotoxicity</subject><subject>Host defence peptide</subject><subject>Humans</subject><subject>Immunologic Factors - genetics</subject><subject>Immunologic Factors - pharmacology</subject><subject>Immunologic Factors - toxicity</subject><subject>Immunomodulatory activity</subject><subject>Infectious Disease</subject><subject>Leukocytes, Mononuclear - drug effects</subject><subject>Leukocytes, Mononuclear - immunology</subject><subject>Lipopolysaccharides - antagonists & inhibitors</subject><subject>Medical sciences</subject><subject>Methicillin-Resistant Staphylococcus aureus - drug effects</subject><subject>Microbial Viability - drug effects</subject><subject>Pharmacology. Drug treatments</subject><subject>Vibrio cholerae - drug effects</subject><subject>Yersinia pestis - drug effects</subject><issn>0924-8579</issn><issn>1872-7913</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNks2O0zAQgCMEYsvCK6BwQIhDytjOny9IqwpYpEocgLPl2pN2uolTbKerPgDvjaOWBXHiZGvyzU_mc5a9YrBkwOp3-yXttYs0kNHbJYcUh3oJwB5lC9Y2vGgkE4-zBUheFm3VyKvsWQj7BFSirJ5mVxxqAQ3IRfZztSNzhy43Ou6wJ0OWXMELi56OaPMDHiJZDPk9xV2ObqedSWEahsmNw2inXsfRn3LtbD6PtNEmplTd5-lCR4qUcvVWkwsx39DYj9s0dJ_fa99pj-kTuhieZ0863Qd8cTmvs-8fP3xb3RbrL58-r27WhamaNhZtKSph67KqWtRcbmS3AdEYkFXNrGUda7VIv2tbRGiNqVnaFhcGjehsVZeNuM7enuvudK8OngbtT2rUpG5v1mqOAdTQSsmPLLFvzuzBjz8mDFENFAz2vXY4TkE1VZlqilYkUp5J48cQPHYPpRmoWZjaq7-EqVmYgjo1m7u8vHSZNgPah8zfhhLw-gLokBbX-SSAwh8uUUzymVudOUz7OxJ6FQzhLIs8mqjsSP81zvt_qpie3GzsDk8Y9uPkXRKkmApcgfo6v7D5gTEA4CL5-QWfSNCb</recordid><startdate>20100901</startdate><enddate>20100901</enddate><creator>Molhoek, E. 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Margo ; van Dijk, Albert ; Veldhuizen, Edwin J.A ; Dijk-Knijnenburg, Helma ; Mars-Groenendijk, Roos H ; Boele, Linda C.L ; Kaman-van Zanten, Wendy E ; Haagsman, Henk P ; Bikker, Floris J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c578t-84353d64558ea29b9fb037c09561dd1f18a3857d8ee08cc6110123cec3fd56473</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Amino Acid Substitution - genetics</topic><topic>Animals</topic><topic>Anti-Bacterial Agents - pharmacology</topic><topic>Anti-Bacterial Agents - toxicity</topic><topic>Antibacterial activity</topic><topic>Antibiotics. Antiinfectious agents. Antiparasitic agents</topic><topic>Antimicrobial Cationic Peptides - genetics</topic><topic>Antimicrobial Cationic Peptides - pharmacology</topic><topic>Antimicrobial Cationic Peptides - toxicity</topic><topic>Bacillus anthracis</topic><topic>Bacillus anthracis - drug effects</topic><topic>Biological and medical sciences</topic><topic>Biological Warfare Agents</topic><topic>Cathelicidin</topic><topic>Chickens</topic><topic>Colony Count, Microbial</topic><topic>Cytokines - secretion</topic><topic>Cytotoxicity</topic><topic>Host defence peptide</topic><topic>Humans</topic><topic>Immunologic Factors - genetics</topic><topic>Immunologic Factors - pharmacology</topic><topic>Immunologic Factors - toxicity</topic><topic>Immunomodulatory activity</topic><topic>Infectious Disease</topic><topic>Leukocytes, Mononuclear - drug effects</topic><topic>Leukocytes, Mononuclear - immunology</topic><topic>Lipopolysaccharides - antagonists & inhibitors</topic><topic>Medical sciences</topic><topic>Methicillin-Resistant Staphylococcus aureus - drug effects</topic><topic>Microbial Viability - drug effects</topic><topic>Pharmacology. 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Margo</au><au>van Dijk, Albert</au><au>Veldhuizen, Edwin J.A</au><au>Dijk-Knijnenburg, Helma</au><au>Mars-Groenendijk, Roos H</au><au>Boele, Linda C.L</au><au>Kaman-van Zanten, Wendy E</au><au>Haagsman, Henk P</au><au>Bikker, Floris J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Chicken cathelicidin-2-derived peptides with enhanced immunomodulatory and antibacterial activities against biological warfare agents</atitle><jtitle>International journal of antimicrobial agents</jtitle><addtitle>Int J Antimicrob Agents</addtitle><date>2010-09-01</date><risdate>2010</risdate><volume>36</volume><issue>3</issue><spage>271</spage><epage>274</epage><pages>271-274</pages><issn>0924-8579</issn><eissn>1872-7913</eissn><abstract>Abstract Host defence peptides (HDPs) are considered to be excellent candidates for the development of novel therapeutic agents. Recently, it was demonstrated that the peptide C1-15, an N -terminal segment of chicken HDP cathelicidin-2, exhibits potent antibacterial activity while lacking cytotoxicity towards eukaryotic cells. In the present study, we report that C1-15 is active against bacteria such as Bacillus anthracis and Yersinia pestis that may potentially be used by bioterrorists. Substitution of single and multiple phenylalanine (Phe) residues to tryptophan (Trp) in C1-15 resulted in variants with improved antibacterial activity against B. anthracis and Y. pestis as well as decreased salt sensitivity. In addition, these peptides exhibited enhanced neutralisation of lipopolysaccharide (LPS)-induced release of pro-inflammatory cytokines in human peripheral blood mononuclear cells (PBMCs). The antibacterial and LPS-neutralising activities of these C1-15-derived peptides are exerted at concentrations far below the concentrations that are toxic to human PBMCs. Taken together, we show that Phe → Trp substitutions in C1-15 variants enhances the antibacterial and LPS-neutralising activities against pathogenic bacteria, including those that may potentially be used as biological warfare agents.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><pmid>20630709</pmid><doi>10.1016/j.ijantimicag.2010.06.001</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Substitution - genetics Animals Anti-Bacterial Agents - pharmacology Anti-Bacterial Agents - toxicity Antibacterial activity Antibiotics. Antiinfectious agents. Antiparasitic agents Antimicrobial Cationic Peptides - genetics Antimicrobial Cationic Peptides - pharmacology Antimicrobial Cationic Peptides - toxicity Bacillus anthracis Bacillus anthracis - drug effects Biological and medical sciences Biological Warfare Agents Cathelicidin Chickens Colony Count, Microbial Cytokines - secretion Cytotoxicity Host defence peptide Humans Immunologic Factors - genetics Immunologic Factors - pharmacology Immunologic Factors - toxicity Immunomodulatory activity Infectious Disease Leukocytes, Mononuclear - drug effects Leukocytes, Mononuclear - immunology Lipopolysaccharides - antagonists & inhibitors Medical sciences Methicillin-Resistant Staphylococcus aureus - drug effects Microbial Viability - drug effects Pharmacology. Drug treatments Vibrio cholerae - drug effects Yersinia pestis - drug effects |
| title | Chicken cathelicidin-2-derived peptides with enhanced immunomodulatory and antibacterial activities against biological warfare agents |
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