Current status of defensins and their role in innate and adaptive immunity
Abstract Naturally occurring antimicrobial cationic polypeptides play a major role in innate and adaptive immunity. These polypeptides are found to be either linear and unstructured or structured through disulfide bonds. Among the structured antimicrobial polypeptides, defensins comprise a family of...
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Veröffentlicht in: | FEMS microbiology letters 2002-01, Vol.206 (1), p.9-18 |
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description | Abstract
Naturally occurring antimicrobial cationic polypeptides play a major role in innate and adaptive immunity. These polypeptides are found to be either linear and unstructured or structured through disulfide bonds. Among the structured antimicrobial polypeptides, defensins comprise a family of cysteine-rich cationic polypeptides that contribute significantly to host defense against the invasion of microorganisms in animals, humans, insects and plants. Their wide-spread occurrence in various tissues of these diverse organisms, and their importance in innate and adaptive immunity have led to their identification, isolation and characterization. A large volume of literature is available on defensins’ occurrence, structural characterization, gene expression and regulation under normal and pathological conditions. Much has also been published regarding their antimicrobial, antiviral and chemoattractive properties, and their molecular and cellular interactions. In this review, we describe the current status of our knowledge of defensins with respect to their molecular, cellular and structural biology, their role in host defense, future research paradigms and the possibility of their utilization as a new class of non-toxic antimicrobial agents and immuno-modulators. |
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Naturally occurring antimicrobial cationic polypeptides play a major role in innate and adaptive immunity. These polypeptides are found to be either linear and unstructured or structured through disulfide bonds. Among the structured antimicrobial polypeptides, defensins comprise a family of cysteine-rich cationic polypeptides that contribute significantly to host defense against the invasion of microorganisms in animals, humans, insects and plants. Their wide-spread occurrence in various tissues of these diverse organisms, and their importance in innate and adaptive immunity have led to their identification, isolation and characterization. A large volume of literature is available on defensins’ occurrence, structural characterization, gene expression and regulation under normal and pathological conditions. Much has also been published regarding their antimicrobial, antiviral and chemoattractive properties, and their molecular and cellular interactions. In this review, we describe the current status of our knowledge of defensins with respect to their molecular, cellular and structural biology, their role in host defense, future research paradigms and the possibility of their utilization as a new class of non-toxic antimicrobial agents and immuno-modulators.</description><identifier>ISSN: 0378-1097</identifier><identifier>EISSN: 1574-6968</identifier><identifier>DOI: 10.1111/j.1574-6968.2002.tb10979.x</identifier><identifier>PMID: 11786250</identifier><identifier>CODEN: FMLED7</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Adaptive immunity ; Amino Acid Sequence ; Amphiphilic molecule ; Animals ; Antiinfectives and antibacterials ; Antimicrobial agent ; Antimicrobial agents ; Antiviral activity ; Bacteriology ; Biological and medical sciences ; Cations ; Cattle ; Cellular structure ; Communicable Diseases - immunology ; Defensins ; Defensins - genetics ; Defensins - physiology ; Disulfide bonds ; Fundamental and applied biological sciences. Psychology ; Gene expression ; Gene Expression Regulation ; Humans ; Immunity ; Immunity (Disease) ; Immunity, Active ; Immunity, Innate ; Immunomodulation ; Immunomodulators ; Immuno‐modulator ; Insects ; Membrane permeabilizing agent ; Microbiology ; Microorganisms ; Molecular Sequence Data ; Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains ; Peptide disulfide ; Polypeptides ; Rabbits ; Structural analysis ; α‐ and β‐defensin ; β‐Sheet peptide</subject><ispartof>FEMS microbiology letters, 2002-01, Vol.206 (1), p.9-18</ispartof><rights>2002 Federation of European Microbiological Societies 2002</rights><rights>2002 Federation of European Microbiological Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4879-7f5d5a640e5dcb164a8a9713178539d4e06a78e5da9d7b5921ee386501080d113</citedby><cites>FETCH-LOGICAL-c4879-7f5d5a640e5dcb164a8a9713178539d4e06a78e5da9d7b5921ee386501080d113</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1574-6968.2002.tb10979.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1574-6968.2002.tb10979.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27903,27904,45553,45554</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=14240647$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11786250$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Raj, Periathamby Antony</creatorcontrib><creatorcontrib>Dentino, Andrew R</creatorcontrib><title>Current status of defensins and their role in innate and adaptive immunity</title><title>FEMS microbiology letters</title><addtitle>FEMS Microbiol Lett</addtitle><description>Abstract
Naturally occurring antimicrobial cationic polypeptides play a major role in innate and adaptive immunity. These polypeptides are found to be either linear and unstructured or structured through disulfide bonds. Among the structured antimicrobial polypeptides, defensins comprise a family of cysteine-rich cationic polypeptides that contribute significantly to host defense against the invasion of microorganisms in animals, humans, insects and plants. Their wide-spread occurrence in various tissues of these diverse organisms, and their importance in innate and adaptive immunity have led to their identification, isolation and characterization. A large volume of literature is available on defensins’ occurrence, structural characterization, gene expression and regulation under normal and pathological conditions. Much has also been published regarding their antimicrobial, antiviral and chemoattractive properties, and their molecular and cellular interactions. In this review, we describe the current status of our knowledge of defensins with respect to their molecular, cellular and structural biology, their role in host defense, future research paradigms and the possibility of their utilization as a new class of non-toxic antimicrobial agents and immuno-modulators.</description><subject>Adaptive immunity</subject><subject>Amino Acid Sequence</subject><subject>Amphiphilic molecule</subject><subject>Animals</subject><subject>Antiinfectives and antibacterials</subject><subject>Antimicrobial agent</subject><subject>Antimicrobial agents</subject><subject>Antiviral activity</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Cations</subject><subject>Cattle</subject><subject>Cellular structure</subject><subject>Communicable Diseases - immunology</subject><subject>Defensins</subject><subject>Defensins - genetics</subject><subject>Defensins - physiology</subject><subject>Disulfide bonds</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene expression</subject><subject>Gene Expression Regulation</subject><subject>Humans</subject><subject>Immunity</subject><subject>Immunity (Disease)</subject><subject>Immunity, Active</subject><subject>Immunity, Innate</subject><subject>Immunomodulation</subject><subject>Immunomodulators</subject><subject>Immuno‐modulator</subject><subject>Insects</subject><subject>Membrane permeabilizing agent</subject><subject>Microbiology</subject><subject>Microorganisms</subject><subject>Molecular Sequence Data</subject><subject>Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains</subject><subject>Peptide disulfide</subject><subject>Polypeptides</subject><subject>Rabbits</subject><subject>Structural analysis</subject><subject>α‐ and β‐defensin</subject><subject>β‐Sheet peptide</subject><issn>0378-1097</issn><issn>1574-6968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqVkF1rFDEYhYMo7Vr9CzJU9G7GNzP5LN7IYquypTd6HbKTDM0yk9kmGe3-ezPdoQXRC0MgkPOcvCcHoXMMFc7rw67ClJOSSSaqGqCu0haD5LK6f4ZWj9JztIKGi3KWTtHLGHcAQGpgJ-gUYy5YTWGFvq2nEKxPRUw6TbEYu8LYzvrofCy0N0W6tS4UYext4XzeXif7IGij98n9zNfDMHmXDq_Qi0730b5ezjP04_Lz9_WXcnNz9XX9aVO2RHBZ8o4aqhkBS027xYxooSXHTY5EG2mIBaa5yKKWhm-prLG1jWAUMAgwGDdn6P3x3X0Y7yYbkxpcbG3fa2_HKSosaiokkRl8-we4G6fgczZVNxgYyxMhUxdHqg1jjMF2ah_coMNBYVBz32qn5lLVXKqa-1ZL3-o-m98sI6btYM2TdSk4A-8WQMdW913QvnXxiSM1AUZ45j4euV-ut4f_iKAurzfzV-nRPk77f5jLv-X_DVFeqs0</recordid><startdate>20020102</startdate><enddate>20020102</enddate><creator>Raj, Periathamby Antony</creator><creator>Dentino, Andrew R</creator><general>Blackwell Publishing Ltd</general><general>Blackwell</general><general>Oxford University Press</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope><scope>7T5</scope></search><sort><creationdate>20020102</creationdate><title>Current status of defensins and their role in innate and adaptive immunity</title><author>Raj, Periathamby Antony ; Dentino, Andrew R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4879-7f5d5a640e5dcb164a8a9713178539d4e06a78e5da9d7b5921ee386501080d113</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Adaptive immunity</topic><topic>Amino Acid Sequence</topic><topic>Amphiphilic molecule</topic><topic>Animals</topic><topic>Antiinfectives and antibacterials</topic><topic>Antimicrobial agent</topic><topic>Antimicrobial agents</topic><topic>Antiviral activity</topic><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Cations</topic><topic>Cattle</topic><topic>Cellular structure</topic><topic>Communicable Diseases - immunology</topic><topic>Defensins</topic><topic>Defensins - genetics</topic><topic>Defensins - physiology</topic><topic>Disulfide bonds</topic><topic>Fundamental and applied biological sciences. 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Naturally occurring antimicrobial cationic polypeptides play a major role in innate and adaptive immunity. These polypeptides are found to be either linear and unstructured or structured through disulfide bonds. Among the structured antimicrobial polypeptides, defensins comprise a family of cysteine-rich cationic polypeptides that contribute significantly to host defense against the invasion of microorganisms in animals, humans, insects and plants. Their wide-spread occurrence in various tissues of these diverse organisms, and their importance in innate and adaptive immunity have led to their identification, isolation and characterization. A large volume of literature is available on defensins’ occurrence, structural characterization, gene expression and regulation under normal and pathological conditions. Much has also been published regarding their antimicrobial, antiviral and chemoattractive properties, and their molecular and cellular interactions. In this review, we describe the current status of our knowledge of defensins with respect to their molecular, cellular and structural biology, their role in host defense, future research paradigms and the possibility of their utilization as a new class of non-toxic antimicrobial agents and immuno-modulators.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>11786250</pmid><doi>10.1111/j.1574-6968.2002.tb10979.x</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Adaptive immunity Amino Acid Sequence Amphiphilic molecule Animals Antiinfectives and antibacterials Antimicrobial agent Antimicrobial agents Antiviral activity Bacteriology Biological and medical sciences Cations Cattle Cellular structure Communicable Diseases - immunology Defensins Defensins - genetics Defensins - physiology Disulfide bonds Fundamental and applied biological sciences. Psychology Gene expression Gene Expression Regulation Humans Immunity Immunity (Disease) Immunity, Active Immunity, Innate Immunomodulation Immunomodulators Immuno‐modulator Insects Membrane permeabilizing agent Microbiology Microorganisms Molecular Sequence Data Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains Peptide disulfide Polypeptides Rabbits Structural analysis α‐ and β‐defensin β‐Sheet peptide |
title | Current status of defensins and their role in innate and adaptive immunity |
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