Loading…

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...

Full description

Saved in:
Bibliographic Details
Published in:Biopolymers 1998, Vol.47 (6), p.465-477
Main Authors: Dimarcq, Jean-Luc, Bulet, Philippe, Hetru, Charles, Hoffmann, Jules
Format: Article
Language:English
Subjects:
Citations: Items that this one cites
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by
cites cdi_FETCH-LOGICAL-c3575-8753013ed23a9641fca8a7cb6ed0ea82e227b077b5b2162b226f9ed49706be453
container_end_page 477
container_issue 6
container_start_page 465
container_title Biopolymers
container_volume 47
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-#
format article
fullrecord <record><control><sourceid>proquest_hal_p</sourceid><recordid>TN_cdi_proquest_miscellaneous_69207787</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>69207787</sourcerecordid><originalsourceid>FETCH-LOGICAL-c3575-8753013ed23a9641fca8a7cb6ed0ea82e227b077b5b2162b226f9ed49706be453</originalsourceid><addsrcrecordid>eNp9kWtr2zAUhsXYWNNuf2EEBqP54OxIsiQ7G4PU2xJDaFp2-3iQ7ROq1bnMcrrl30-eSzYoDAQHiZfnRc9hbMJhzAHE6_NPeZaPOKQmApGIc56mySg2E_021moymebvo4v8Sr2TYxhnyzcievmIDY7xx2wAADqSSqgTdur9d4A4lhyeshMOUkojkwFT2cG35DYUNa68GdpN69aubLaFs_VwR7vWVeSHbhPOHTUtFY1tyT9jT1a29vT8fp6xLx8_fM7m0WI5y7PpIiqlMipKjJLAJVVC2lTHfFXaxJqy0FQB2USQEKYAYwpVCK5FIYRepVTFqQFdUKzkGRv13Btb465xa9sccGsdzqcL7N5AJiLRKr7jIfuqz-6a7Y89-RbXzpdU13ZD271HnYpQlZgQvOqD4ZveN7Q6kjlgJx6xE4-dSexMYiceY4Mag3jEIB478SgRMFuiCMgX9937Yk3VP8De89_On66mw4PC__Y9qPtzC8ioR7qwwF9HpG1uURtpFH67nOHl9exazNOvyOVvw82ovg</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>69207787</pqid></control><display><type>article</type><title>Cysteine-rich antimicrobial peptides in invertebrates</title><source>Wiley</source><creator>Dimarcq, Jean-Luc ; Bulet, Philippe ; Hetru, Charles ; Hoffmann, Jules</creator><creatorcontrib>Dimarcq, Jean-Luc ; Bulet, Philippe ; Hetru, Charles ; Hoffmann, Jules</creatorcontrib><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 &amp; Sons, Inc. Biopoly 47: 465–477, 1998</description><identifier>ISSN: 0006-3525</identifier><identifier>ISSN: 2475-8817</identifier><identifier>EISSN: 1097-0282</identifier><identifier>EISSN: 2475-8817</identifier><identifier>DOI: 10.1002/(SICI)1097-0282(1998)47:6&lt;465::AID-BIP5&gt;3.0.CO;2-#</identifier><identifier>PMID: 10333738</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>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</subject><ispartof>Biopolymers, 1998, Vol.47 (6), p.465-477</ispartof><rights>Copyright © 1998 John Wiley &amp; Sons, Inc.</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c3575-8753013ed23a9641fca8a7cb6ed0ea82e227b077b5b2162b226f9ed49706be453</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,885,4024,27923,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10333738$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-03828654$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Dimarcq, Jean-Luc</creatorcontrib><creatorcontrib>Bulet, Philippe</creatorcontrib><creatorcontrib>Hetru, Charles</creatorcontrib><creatorcontrib>Hoffmann, Jules</creatorcontrib><title>Cysteine-rich antimicrobial peptides in invertebrates</title><title>Biopolymers</title><addtitle>Biopolymers</addtitle><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 &amp; 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 &amp; 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 &amp; Sons, Inc. Biopoly 47: 465–477, 1998</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>10333738</pmid><doi>10.1002/(SICI)1097-0282(1998)47:6&lt;465::AID-BIP5&gt;3.0.CO;2-#</doi><tpages>13</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0006-3525
ispartof Biopolymers, 1998, Vol.47 (6), p.465-477
issn 0006-3525
2475-8817
1097-0282
2475-8817
language eng
recordid cdi_proquest_miscellaneous_69207787
source Wiley
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
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-29T14%3A15%3A27IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_hal_p&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Cysteine-rich%20antimicrobial%20peptides%20in%20invertebrates&rft.jtitle=Biopolymers&rft.au=Dimarcq,%20Jean-Luc&rft.date=1998&rft.volume=47&rft.issue=6&rft.spage=465&rft.epage=477&rft.pages=465-477&rft.issn=0006-3525&rft.eissn=1097-0282&rft_id=info:doi/10.1002/(SICI)1097-0282(1998)47:6%3C465::AID-BIP5%3E3.0.CO;2-%23&rft_dat=%3Cproquest_hal_p%3E69207787%3C/proquest_hal_p%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c3575-8753013ed23a9641fca8a7cb6ed0ea82e227b077b5b2162b226f9ed49706be453%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=69207787&rft_id=info:pmid/10333738&rfr_iscdi=true