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Cysteine-rich antimicrobial peptides in invertebrates
Antimicrobial peptides are pivotal elements of the innate immune defense against bacterial and fungal infections. Within the impressive list of antimicrobial peptides available at present, more than half have been characterized in arthropods. Cysteine‐rich antimicrobial peptides represent the most d...
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Published in: | Biopolymers 1998, Vol.47 (6), p.465-477 |
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creator | Dimarcq, Jean-Luc Bulet, Philippe Hetru, Charles Hoffmann, Jules |
description | Antimicrobial peptides are pivotal elements of the innate immune defense against bacterial and fungal infections. Within the impressive list of antimicrobial peptides available at present, more than half have been characterized in arthropods. Cysteine‐rich antimicrobial peptides represent the most diverse and widely distributed family among arthropods and, to a larger extent, among invertebrates. Proeminent groups of cysteine‐rich peptides are peptides with the CSαβ motif and peptides forming an hairpin‐like β‐sheet structure. Although these substances exhibit a large structural diversity and a wide spectrum of activity, they have in common the ability to permeabilize microbial cytoplasmic membranes. Drosophila has proved a remarkable system for the analysis of the regulation of expression of gene encoding antimirobial cysteine‐rich peptides. These studies have unraveled the striking parallels that exist between insect immunity and innate immunity in mammals that point to a common ancestry of essential aspects of innate immunity. © 1999 John Wiley & Sons, Inc. Biopoly 47: 465–477, 1998 |
doi_str_mv | 10.1002/(SICI)1097-0282(1998)47:6<465::AID-BIP5>3.0.CO;2-# |
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Within the impressive list of antimicrobial peptides available at present, more than half have been characterized in arthropods. Cysteine‐rich antimicrobial peptides represent the most diverse and widely distributed family among arthropods and, to a larger extent, among invertebrates. Proeminent groups of cysteine‐rich peptides are peptides with the CSαβ motif and peptides forming an hairpin‐like β‐sheet structure. Although these substances exhibit a large structural diversity and a wide spectrum of activity, they have in common the ability to permeabilize microbial cytoplasmic membranes. Drosophila has proved a remarkable system for the analysis of the regulation of expression of gene encoding antimirobial cysteine‐rich peptides. These studies have unraveled the striking parallels that exist between insect immunity and innate immunity in mammals that point to a common ancestry of essential aspects of innate immunity. © 1999 John Wiley & Sons, Inc. Biopoly 47: 465–477, 1998</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Anti-Bacterial Agents - chemistry</subject><subject>antimicrobial peptides</subject><subject>arthropods</subject><subject>bacterial infections</subject><subject>Cysteine - analysis</subject><subject>fungal infections</subject><subject>innate immunity</subject><subject>insects</subject><subject>invertebrates</subject><subject>Invertebrates - chemistry</subject><subject>Life Sciences</subject><subject>Molecular Sequence Data</subject><subject>Peptides</subject><issn>0006-3525</issn><issn>2475-8817</issn><issn>1097-0282</issn><issn>2475-8817</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><recordid>eNp9kWtr2zAUhsXYWNNuf2EEBqP54OxIsiQ7G4PU2xJDaFp2-3iQ7ROq1bnMcrrl30-eSzYoDAQHiZfnRc9hbMJhzAHE6_NPeZaPOKQmApGIc56mySg2E_021moymebvo4v8Sr2TYxhnyzcievmIDY7xx2wAADqSSqgTdur9d4A4lhyeshMOUkojkwFT2cG35DYUNa68GdpN69aubLaFs_VwR7vWVeSHbhPOHTUtFY1tyT9jT1a29vT8fp6xLx8_fM7m0WI5y7PpIiqlMipKjJLAJVVC2lTHfFXaxJqy0FQB2USQEKYAYwpVCK5FIYRepVTFqQFdUKzkGRv13Btb465xa9sccGsdzqcL7N5AJiLRKr7jIfuqz-6a7Y89-RbXzpdU13ZD271HnYpQlZgQvOqD4ZveN7Q6kjlgJx6xE4-dSexMYiceY4Mag3jEIB478SgRMFuiCMgX9937Yk3VP8De89_On66mw4PC__Y9qPtzC8ioR7qwwF9HpG1uURtpFH67nOHl9exazNOvyOVvw82ovg</recordid><startdate>1998</startdate><enddate>1998</enddate><creator>Dimarcq, Jean-Luc</creator><creator>Bulet, Philippe</creator><creator>Hetru, Charles</creator><creator>Hoffmann, Jules</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><general>John Wiley & Sons, Ltd</general><scope>BSCLL</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>7X8</scope><scope>1XC</scope></search><sort><creationdate>1998</creationdate><title>Cysteine-rich antimicrobial peptides in invertebrates</title><author>Dimarcq, Jean-Luc ; Bulet, Philippe ; Hetru, Charles ; Hoffmann, Jules</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3575-8753013ed23a9641fca8a7cb6ed0ea82e227b077b5b2162b226f9ed49706be453</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Anti-Bacterial Agents - chemistry</topic><topic>antimicrobial peptides</topic><topic>arthropods</topic><topic>bacterial infections</topic><topic>Cysteine - analysis</topic><topic>fungal infections</topic><topic>innate immunity</topic><topic>insects</topic><topic>invertebrates</topic><topic>Invertebrates - chemistry</topic><topic>Life Sciences</topic><topic>Molecular Sequence Data</topic><topic>Peptides</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Dimarcq, Jean-Luc</creatorcontrib><creatorcontrib>Bulet, Philippe</creatorcontrib><creatorcontrib>Hetru, Charles</creatorcontrib><creatorcontrib>Hoffmann, Jules</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>Biopolymers</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Dimarcq, Jean-Luc</au><au>Bulet, Philippe</au><au>Hetru, Charles</au><au>Hoffmann, Jules</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cysteine-rich antimicrobial peptides in invertebrates</atitle><jtitle>Biopolymers</jtitle><addtitle>Biopolymers</addtitle><date>1998</date><risdate>1998</risdate><volume>47</volume><issue>6</issue><spage>465</spage><epage>477</epage><pages>465-477</pages><issn>0006-3525</issn><issn>2475-8817</issn><eissn>1097-0282</eissn><eissn>2475-8817</eissn><abstract>Antimicrobial peptides are pivotal elements of the innate immune defense against bacterial and fungal infections. Within the impressive list of antimicrobial peptides available at present, more than half have been characterized in arthropods. Cysteine‐rich antimicrobial peptides represent the most diverse and widely distributed family among arthropods and, to a larger extent, among invertebrates. Proeminent groups of cysteine‐rich peptides are peptides with the CSαβ motif and peptides forming an hairpin‐like β‐sheet structure. Although these substances exhibit a large structural diversity and a wide spectrum of activity, they have in common the ability to permeabilize microbial cytoplasmic membranes. Drosophila has proved a remarkable system for the analysis of the regulation of expression of gene encoding antimirobial cysteine‐rich peptides. These studies have unraveled the striking parallels that exist between insect immunity and innate immunity in mammals that point to a common ancestry of essential aspects of innate immunity. © 1999 John Wiley & Sons, Inc. 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subjects | Amino Acid Sequence Animals Anti-Bacterial Agents - chemistry antimicrobial peptides arthropods bacterial infections Cysteine - analysis fungal infections innate immunity insects invertebrates Invertebrates - chemistry Life Sciences Molecular Sequence Data Peptides |
title | Cysteine-rich antimicrobial peptides in invertebrates |
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