Expression and activity of a novel cathelicidin from domestic cats
Cathelicidins are small cationic antimicrobial peptides found in many species including primates, mammals, marsupials, birds and even more primitive vertebrates, such as the hagfish. Some animals encode multiple cathelicidins in their genome, whereas others have only one. This report identifies and...
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description | Cathelicidins are small cationic antimicrobial peptides found in many species including primates, mammals, marsupials, birds and even more primitive vertebrates, such as the hagfish. Some animals encode multiple cathelicidins in their genome, whereas others have only one. This report identifies and characterizes feline cathelicidin (feCath) as the sole cathelicidin in domestic cats (Felis catus). Expression of feCath is predominantly found in the bone marrow, with lower levels of expression in the gastrointestinal tract and skin. By immunocytochemistry, feCath localizes to the cytoplasm of neutrophils in feline peripheral blood. Structurally, the mature feCath sequence is most similar to a subgroup of cathelicidins that form linear α-helices. feCath possesses antimicrobial activity against E. coli D31, Salmonella enterica serovar Typhimurium (IR715), Listeria monocytogenes and Staphylococcus pseudintermedius (clinical isolate) similar to that of the human ortholog, LL-37. In contrast, feCath lacks the DNA binding activity seen with LL-37. Given its similarity in sequence, structure, tissue expression, and antimicrobial activity, the cathelicidin encoded by cats, feCath, belongs to the subgroup of linear cathelicidins found not only in humans, but also non-human primates, dogs, mice, and rats. |
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Some animals encode multiple cathelicidins in their genome, whereas others have only one. This report identifies and characterizes feline cathelicidin (feCath) as the sole cathelicidin in domestic cats (Felis catus). Expression of feCath is predominantly found in the bone marrow, with lower levels of expression in the gastrointestinal tract and skin. By immunocytochemistry, feCath localizes to the cytoplasm of neutrophils in feline peripheral blood. Structurally, the mature feCath sequence is most similar to a subgroup of cathelicidins that form linear α-helices. feCath possesses antimicrobial activity against E. coli D31, Salmonella enterica serovar Typhimurium (IR715), Listeria monocytogenes and Staphylococcus pseudintermedius (clinical isolate) similar to that of the human ortholog, LL-37. In contrast, feCath lacks the DNA binding activity seen with LL-37. Given its similarity in sequence, structure, tissue expression, and antimicrobial activity, the cathelicidin encoded by cats, feCath, belongs to the subgroup of linear cathelicidins found not only in humans, but also non-human primates, dogs, mice, and rats.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0018756</identifier><identifier>PMID: 21533281</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Amino Acid Sequence ; Amino acids ; Animals ; Anti-Infective Agents - metabolism ; Antibiotics ; Antiinfectives and antibacterials ; Antimicrobial activity ; Antimicrobial agents ; Antimicrobial Cationic Peptides - genetics ; Antimicrobial Cationic Peptides - metabolism ; Antimicrobial peptides ; Base Sequence ; Biology ; Birds ; Bone marrow ; Cathelicidins ; Cationic antimicrobial peptides ; Cats ; Circular Dichroism ; Cytoplasm ; Deoxyribonucleic acid ; DNA ; DNA Primers ; DNA, Complementary ; Domestic animals ; E coli ; Gastrointestinal system ; Gastrointestinal tract ; Genes ; Genomes ; Genomics ; Granulocytes ; Helices ; Immunocytochemistry ; Immunohistochemistry ; Immunology ; Leukocytes (neutrophilic) ; Listeria ; Listeria monocytogenes ; Molecular Sequence Data ; Neutrophils ; Nucleotide sequence ; Peptides ; Peripheral blood ; Polymerase Chain Reaction ; Primates ; Rats ; Salmonella ; Sequence Homology, Amino Acid ; Sheep ; Skin ; Vertebrates ; Veterinary colleges ; Veterinary medicine ; Veterinary Science</subject><ispartof>PloS one, 2011-04, Vol.6 (4), p.e18756-e18756</ispartof><rights>COPYRIGHT 2011 Public Library of Science</rights><rights>2011 Leonard et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>Leonard et al. 2011</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c691t-7383b395dfe0fd2e0fa57e112dccbacb45233b05abde1b51ccb62e3c3fed1f673</citedby><cites>FETCH-LOGICAL-c691t-7383b395dfe0fd2e0fa57e112dccbacb45233b05abde1b51ccb62e3c3fed1f673</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3075274/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3075274/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,2102,2928,23866,27924,27925,53791,53793,79600,79601</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21533281$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Uversky, Vladimir N.</contributor><creatorcontrib>Leonard, Brian C</creatorcontrib><creatorcontrib>Chu, Hiutung</creatorcontrib><creatorcontrib>Johns, Jennifer L</creatorcontrib><creatorcontrib>Gallo, Richard L</creatorcontrib><creatorcontrib>Moore, Peter F</creatorcontrib><creatorcontrib>Marks, Stanley L</creatorcontrib><creatorcontrib>Bevins, Charles L</creatorcontrib><title>Expression and activity of a novel cathelicidin from domestic cats</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>Cathelicidins are small cationic antimicrobial peptides found in many species including primates, mammals, marsupials, birds and even more primitive vertebrates, such as the hagfish. Some animals encode multiple cathelicidins in their genome, whereas others have only one. This report identifies and characterizes feline cathelicidin (feCath) as the sole cathelicidin in domestic cats (Felis catus). Expression of feCath is predominantly found in the bone marrow, with lower levels of expression in the gastrointestinal tract and skin. By immunocytochemistry, feCath localizes to the cytoplasm of neutrophils in feline peripheral blood. Structurally, the mature feCath sequence is most similar to a subgroup of cathelicidins that form linear α-helices. feCath possesses antimicrobial activity against E. coli D31, Salmonella enterica serovar Typhimurium (IR715), Listeria monocytogenes and Staphylococcus pseudintermedius (clinical isolate) similar to that of the human ortholog, LL-37. In contrast, feCath lacks the DNA binding activity seen with LL-37. 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peptides found in many species including primates, mammals, marsupials, birds and even more primitive vertebrates, such as the hagfish. Some animals encode multiple cathelicidins in their genome, whereas others have only one. This report identifies and characterizes feline cathelicidin (feCath) as the sole cathelicidin in domestic cats (Felis catus). Expression of feCath is predominantly found in the bone marrow, with lower levels of expression in the gastrointestinal tract and skin. By immunocytochemistry, feCath localizes to the cytoplasm of neutrophils in feline peripheral blood. Structurally, the mature feCath sequence is most similar to a subgroup of cathelicidins that form linear α-helices. feCath possesses antimicrobial activity against E. coli D31, Salmonella enterica serovar Typhimurium (IR715), Listeria monocytogenes and Staphylococcus pseudintermedius (clinical isolate) similar to that of the human ortholog, LL-37. In contrast, feCath lacks the DNA binding activity seen with LL-37. Given its similarity in sequence, structure, tissue expression, and antimicrobial activity, the cathelicidin encoded by cats, feCath, belongs to the subgroup of linear cathelicidins found not only in humans, but also non-human primates, dogs, mice, and rats.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>21533281</pmid><doi>10.1371/journal.pone.0018756</doi><tpages>e18756</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amino Acid Sequence Amino acids Animals Anti-Infective Agents - metabolism Antibiotics Antiinfectives and antibacterials Antimicrobial activity Antimicrobial agents Antimicrobial Cationic Peptides - genetics Antimicrobial Cationic Peptides - metabolism Antimicrobial peptides Base Sequence Biology Birds Bone marrow Cathelicidins Cationic antimicrobial peptides Cats Circular Dichroism Cytoplasm Deoxyribonucleic acid DNA DNA Primers DNA, Complementary Domestic animals E coli Gastrointestinal system Gastrointestinal tract Genes Genomes Genomics Granulocytes Helices Immunocytochemistry Immunohistochemistry Immunology Leukocytes (neutrophilic) Listeria Listeria monocytogenes Molecular Sequence Data Neutrophils Nucleotide sequence Peptides Peripheral blood Polymerase Chain Reaction Primates Rats Salmonella Sequence Homology, Amino Acid Sheep Skin Vertebrates Veterinary colleges Veterinary medicine Veterinary Science |
title | Expression and activity of a novel cathelicidin from domestic cats |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-02T14%3A36%3A09IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_plos_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Expression%20and%20activity%20of%20a%20novel%20cathelicidin%20from%20domestic%20cats&rft.jtitle=PloS%20one&rft.au=Leonard,%20Brian%20C&rft.date=2011-04-12&rft.volume=6&rft.issue=4&rft.spage=e18756&rft.epage=e18756&rft.pages=e18756-e18756&rft.issn=1932-6203&rft.eissn=1932-6203&rft_id=info:doi/10.1371/journal.pone.0018756&rft_dat=%3Cgale_plos_%3EA476898214%3C/gale_plos_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1296293229&rft_id=info:pmid/21533281&rft_galeid=A476898214&rft_doaj_id=oai_doaj_org_article_c598cbf3539148d1b1e3437e8cf187e4&rfr_iscdi=true |