Big defensins, a diverse family of antimicrobial peptides that follows different patterns of expression in hemocytes of the oyster Crassostrea gigas.

Background Big defensin is an antimicrobial peptide composed of a highly hydrophobic N-terminal region and a cationic C-terminal region containing six cysteine residues involved in three internal disulfide bridges. While big defensin sequences have been reported in various mollusk species, few studi...

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Published in:PLoS ONE
Main Authors: Rafael D Rosa, Adrien Santini, Julie Fievet, Philippe Bulet, Delphine Destoumieux-Garzón, Evelyne Bachère
Format: Article in Journal/Newspaper
Language:English
Published: Public Library of Science (PLoS) 2011
Subjects:
R
Q
Online Access:https://doi.org/10.1371/journal.pone.0025594
https://doaj.org/article/36f0f8df5fc54a0db9ba09ed7e8ffd7b
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spelling ftdoajarticles:oai:doaj.org/article:36f0f8df5fc54a0db9ba09ed7e8ffd7b 2023-05-15T15:58:27+02:00 Big defensins, a diverse family of antimicrobial peptides that follows different patterns of expression in hemocytes of the oyster Crassostrea gigas. Rafael D Rosa Adrien Santini Julie Fievet Philippe Bulet Delphine Destoumieux-Garzón Evelyne Bachère 2011-01-01T00:00:00Z https://doi.org/10.1371/journal.pone.0025594 https://doaj.org/article/36f0f8df5fc54a0db9ba09ed7e8ffd7b EN eng Public Library of Science (PLoS) https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21980497/?tool=EBI https://doaj.org/toc/1932-6203 1932-6203 doi:10.1371/journal.pone.0025594 https://doaj.org/article/36f0f8df5fc54a0db9ba09ed7e8ffd7b PLoS ONE, Vol 6, Iss 9, p e25594 (2011) Medicine R Science Q article 2011 ftdoajarticles https://doi.org/10.1371/journal.pone.0025594 2022-12-31T07:42:24Z Background Big defensin is an antimicrobial peptide composed of a highly hydrophobic N-terminal region and a cationic C-terminal region containing six cysteine residues involved in three internal disulfide bridges. While big defensin sequences have been reported in various mollusk species, few studies have been devoted to their sequence diversity, gene organization and their expression in response to microbial infections. Findings Using the high-throughput Digital Gene Expression approach, we have identified in Crassostrea gigas oysters several sequences coding for big defensins induced in response to a Vibrio infection. We showed that the oyster big defensin family is composed of three members (named Cg-BigDef1, Cg-BigDef2 and Cg-BigDef3) that are encoded by distinct genomic sequences. All Cg-BigDefs contain a hydrophobic N-terminal domain and a cationic C-terminal domain that resembles vertebrate β-defensins. Both domains are encoded by separate exons. We found that big defensins form a group predominantly present in mollusks and closer to vertebrate defensins than to invertebrate and fungi CSαβ-containing defensins. Moreover, we showed that Cg-BigDefs are expressed in oyster hemocytes only and follow different patterns of gene expression. While Cg-BigDef3 is non-regulated, both Cg-BigDef1 and Cg-BigDef2 transcripts are strongly induced in response to bacterial challenge. Induction was dependent on pathogen associated molecular patterns but not damage-dependent. The inducibility of Cg-BigDef1 was confirmed by HPLC and mass spectrometry, since ions with a molecular mass compatible with mature Cg-BigDef1 (10.7 kDa) were present in immune-challenged oysters only. From our biochemical data, native Cg-BigDef1 would result from the elimination of a prepropeptide sequence and the cyclization of the resulting N-terminal glutamine residue into a pyroglutamic acid. Conclusions We provide here the first report showing that big defensins form a family of antimicrobial peptides diverse not only in terms of sequences but ... Article in Journal/Newspaper Crassostrea gigas Directory of Open Access Journals: DOAJ Articles PLoS ONE 6 9 e25594
institution Open Polar
collection Directory of Open Access Journals: DOAJ Articles
op_collection_id ftdoajarticles
language English
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Rafael D Rosa
Adrien Santini
Julie Fievet
Philippe Bulet
Delphine Destoumieux-Garzón
Evelyne Bachère
Big defensins, a diverse family of antimicrobial peptides that follows different patterns of expression in hemocytes of the oyster Crassostrea gigas.
topic_facet Medicine
R
Science
Q
description Background Big defensin is an antimicrobial peptide composed of a highly hydrophobic N-terminal region and a cationic C-terminal region containing six cysteine residues involved in three internal disulfide bridges. While big defensin sequences have been reported in various mollusk species, few studies have been devoted to their sequence diversity, gene organization and their expression in response to microbial infections. Findings Using the high-throughput Digital Gene Expression approach, we have identified in Crassostrea gigas oysters several sequences coding for big defensins induced in response to a Vibrio infection. We showed that the oyster big defensin family is composed of three members (named Cg-BigDef1, Cg-BigDef2 and Cg-BigDef3) that are encoded by distinct genomic sequences. All Cg-BigDefs contain a hydrophobic N-terminal domain and a cationic C-terminal domain that resembles vertebrate β-defensins. Both domains are encoded by separate exons. We found that big defensins form a group predominantly present in mollusks and closer to vertebrate defensins than to invertebrate and fungi CSαβ-containing defensins. Moreover, we showed that Cg-BigDefs are expressed in oyster hemocytes only and follow different patterns of gene expression. While Cg-BigDef3 is non-regulated, both Cg-BigDef1 and Cg-BigDef2 transcripts are strongly induced in response to bacterial challenge. Induction was dependent on pathogen associated molecular patterns but not damage-dependent. The inducibility of Cg-BigDef1 was confirmed by HPLC and mass spectrometry, since ions with a molecular mass compatible with mature Cg-BigDef1 (10.7 kDa) were present in immune-challenged oysters only. From our biochemical data, native Cg-BigDef1 would result from the elimination of a prepropeptide sequence and the cyclization of the resulting N-terminal glutamine residue into a pyroglutamic acid. Conclusions We provide here the first report showing that big defensins form a family of antimicrobial peptides diverse not only in terms of sequences but ...
format Article in Journal/Newspaper
author Rafael D Rosa
Adrien Santini
Julie Fievet
Philippe Bulet
Delphine Destoumieux-Garzón
Evelyne Bachère
author_facet Rafael D Rosa
Adrien Santini
Julie Fievet
Philippe Bulet
Delphine Destoumieux-Garzón
Evelyne Bachère
author_sort Rafael D Rosa
title Big defensins, a diverse family of antimicrobial peptides that follows different patterns of expression in hemocytes of the oyster Crassostrea gigas.
title_short Big defensins, a diverse family of antimicrobial peptides that follows different patterns of expression in hemocytes of the oyster Crassostrea gigas.
title_full Big defensins, a diverse family of antimicrobial peptides that follows different patterns of expression in hemocytes of the oyster Crassostrea gigas.
title_fullStr Big defensins, a diverse family of antimicrobial peptides that follows different patterns of expression in hemocytes of the oyster Crassostrea gigas.
title_full_unstemmed Big defensins, a diverse family of antimicrobial peptides that follows different patterns of expression in hemocytes of the oyster Crassostrea gigas.
title_sort big defensins, a diverse family of antimicrobial peptides that follows different patterns of expression in hemocytes of the oyster crassostrea gigas.
publisher Public Library of Science (PLoS)
publishDate 2011
url https://doi.org/10.1371/journal.pone.0025594
https://doaj.org/article/36f0f8df5fc54a0db9ba09ed7e8ffd7b
genre Crassostrea gigas
genre_facet Crassostrea gigas
op_source PLoS ONE, Vol 6, Iss 9, p e25594 (2011)
op_relation https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21980497/?tool=EBI
https://doaj.org/toc/1932-6203
1932-6203
doi:10.1371/journal.pone.0025594
https://doaj.org/article/36f0f8df5fc54a0db9ba09ed7e8ffd7b
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