Molecular characterization of antimicrobial peptide genes of the carpenter ant Camponotus floridanus.

The production of antimicrobial peptides (AMPs) is a major defense mechanism against pathogen infestation and of particular importance for insects relying exclusively on an innate immune system. Here, we report on the characterization of three AMPs from the carpenter ant Camponotus floridanus. Due t...

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Autores principales: Carolin Ratzka, Frank Förster, Chunguang Liang, Maria Kupper, Thomas Dandekar, Heike Feldhaar, Roy Gross
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spelling oai:doaj.org-article:7f6c1df47ccf4a8780d3ed3eb0366a3b2021-11-18T07:09:12ZMolecular characterization of antimicrobial peptide genes of the carpenter ant Camponotus floridanus.1932-620310.1371/journal.pone.0043036https://doaj.org/article/7f6c1df47ccf4a8780d3ed3eb0366a3b2012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22912782/?tool=EBIhttps://doaj.org/toc/1932-6203The production of antimicrobial peptides (AMPs) is a major defense mechanism against pathogen infestation and of particular importance for insects relying exclusively on an innate immune system. Here, we report on the characterization of three AMPs from the carpenter ant Camponotus floridanus. Due to sequence similarities and amino acid composition these peptides can be classified into the cysteine-rich (e.g. defensin) and glycine-rich (e.g. hymenoptaecin) AMP groups, respectively. The gene and cDNA sequences of these AMPs were established and their expression was shown to be induced by microbial challenge. We characterized two different defensin genes. The defensin-2 gene has a single intron, whereas the defensin-1 gene has two introns. The deduced amino acid sequence of the C. floridanus defensins is very similar to other known ant defensins with the exception of a short C-terminal extension of defensin-1. The hymenoptaecin gene has a single intron and a very peculiar domain structure. The corresponding precursor protein consists of a signal- and a pro-sequence followed by a hymenoptaecin-like domain and six directly repeated hymenoptaecin domains. Each of the hymenoptaecin domains is flanked by an EAEP-spacer sequence and a RR-site known to be a proteolytic processing site. Thus, proteolytic processing of the multipeptide precursor may generate several mature AMPs leading to an amplification of the immune response. Bioinformatical analyses revealed the presence of hymenoptaecin genes with similar multipeptide precursor structure in genomes of other ant species suggesting an evolutionary conserved important role of this gene in ant immunity.Carolin RatzkaFrank FörsterChunguang LiangMaria KupperThomas DandekarHeike FeldhaarRoy GrossPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 8, p e43036 (2012)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Carolin Ratzka
Frank Förster
Chunguang Liang
Maria Kupper
Thomas Dandekar
Heike Feldhaar
Roy Gross
Molecular characterization of antimicrobial peptide genes of the carpenter ant Camponotus floridanus.
description The production of antimicrobial peptides (AMPs) is a major defense mechanism against pathogen infestation and of particular importance for insects relying exclusively on an innate immune system. Here, we report on the characterization of three AMPs from the carpenter ant Camponotus floridanus. Due to sequence similarities and amino acid composition these peptides can be classified into the cysteine-rich (e.g. defensin) and glycine-rich (e.g. hymenoptaecin) AMP groups, respectively. The gene and cDNA sequences of these AMPs were established and their expression was shown to be induced by microbial challenge. We characterized two different defensin genes. The defensin-2 gene has a single intron, whereas the defensin-1 gene has two introns. The deduced amino acid sequence of the C. floridanus defensins is very similar to other known ant defensins with the exception of a short C-terminal extension of defensin-1. The hymenoptaecin gene has a single intron and a very peculiar domain structure. The corresponding precursor protein consists of a signal- and a pro-sequence followed by a hymenoptaecin-like domain and six directly repeated hymenoptaecin domains. Each of the hymenoptaecin domains is flanked by an EAEP-spacer sequence and a RR-site known to be a proteolytic processing site. Thus, proteolytic processing of the multipeptide precursor may generate several mature AMPs leading to an amplification of the immune response. Bioinformatical analyses revealed the presence of hymenoptaecin genes with similar multipeptide precursor structure in genomes of other ant species suggesting an evolutionary conserved important role of this gene in ant immunity.
format article
author Carolin Ratzka
Frank Förster
Chunguang Liang
Maria Kupper
Thomas Dandekar
Heike Feldhaar
Roy Gross
author_facet Carolin Ratzka
Frank Förster
Chunguang Liang
Maria Kupper
Thomas Dandekar
Heike Feldhaar
Roy Gross
author_sort Carolin Ratzka
title Molecular characterization of antimicrobial peptide genes of the carpenter ant Camponotus floridanus.
title_short Molecular characterization of antimicrobial peptide genes of the carpenter ant Camponotus floridanus.
title_full Molecular characterization of antimicrobial peptide genes of the carpenter ant Camponotus floridanus.
title_fullStr Molecular characterization of antimicrobial peptide genes of the carpenter ant Camponotus floridanus.
title_full_unstemmed Molecular characterization of antimicrobial peptide genes of the carpenter ant Camponotus floridanus.
title_sort molecular characterization of antimicrobial peptide genes of the carpenter ant camponotus floridanus.
publisher Public Library of Science (PLoS)
publishDate 2012
url https://doaj.org/article/7f6c1df47ccf4a8780d3ed3eb0366a3b
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