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2003
Thouzeau Cécile, Maho Yvon Le, Froget Guillaume, Sabatier Laurence, Bohec Céline Le, Hoffmann Jules A, Bulet Philippe
Spheniscins, avian beta-defensins in preserved stomach contents of the king penguin, Aptenodytes patagonicus Journal Article
In: J. Biol. Chem., vol. 278, no. 51, pp. 51053–51058, 2003, ISSN: 0021-9258.
Abstract | Links | BibTeX | Tags: Animals, Antimicrobial Cationic Peptides, bacteria, beta-Defensins, Birds, Feeding Behavior, Fungi, Gastrointestinal Contents, hoffmann, M3i, Male, Mass, Matrix-Assisted Laser Desorption-Ionization, Protein Isoforms, Sequence Alignment, Spectrometry
@article{thouzeau_spheniscins_2003,
title = {Spheniscins, avian beta-defensins in preserved stomach contents of the king penguin, Aptenodytes patagonicus},
author = {Cécile Thouzeau and Yvon Le Maho and Guillaume Froget and Laurence Sabatier and Céline Le Bohec and Jules A Hoffmann and Philippe Bulet},
doi = {10.1074/jbc.M306839200},
issn = {0021-9258},
year = {2003},
date = {2003-12-01},
journal = {J. Biol. Chem.},
volume = {278},
number = {51},
pages = {51053--51058},
abstract = {During the last part of egg incubation in king penguins, the male can preserve undigested food in the stomach for several weeks. This ensures survival of the newly hatched chick, in cases where the return of the foraging female from the sea is delayed. In accordance with the characterization of stress-induced bacteria, we demonstrate the occurrence of strong antimicrobial activities in preserved stomach contents. We isolated and fully characterized two isoforms of a novel 38-residue antimicrobial peptide (AMP), spheniscin, belonging to the beta-defensin subfamily. Spheniscin concentration was found to strongly increase during the period of food storage. Using a synthetic version of one of two spheniscin isoforms, we established that this peptide has a broad activity spectrum, affecting the growth of both pathogenic bacteria and fungi. Altogether, our data suggest that spheniscins and other, not yet identified, antimicrobial substances may play a role in the long term preservation of stored food in the stomach of king penguins.},
keywords = {Animals, Antimicrobial Cationic Peptides, bacteria, beta-Defensins, Birds, Feeding Behavior, Fungi, Gastrointestinal Contents, hoffmann, M3i, Male, Mass, Matrix-Assisted Laser Desorption-Ionization, Protein Isoforms, Sequence Alignment, Spectrometry},
pubstate = {published},
tppubtype = {article}
}
During the last part of egg incubation in king penguins, the male can preserve undigested food in the stomach for several weeks. This ensures survival of the newly hatched chick, in cases where the return of the foraging female from the sea is delayed. In accordance with the characterization of stress-induced bacteria, we demonstrate the occurrence of strong antimicrobial activities in preserved stomach contents. We isolated and fully characterized two isoforms of a novel 38-residue antimicrobial peptide (AMP), spheniscin, belonging to the beta-defensin subfamily. Spheniscin concentration was found to strongly increase during the period of food storage. Using a synthetic version of one of two spheniscin isoforms, we established that this peptide has a broad activity spectrum, affecting the growth of both pathogenic bacteria and fungi. Altogether, our data suggest that spheniscins and other, not yet identified, antimicrobial substances may play a role in the long term preservation of stored food in the stomach of king penguins.
1999
Lowenberger C A, Smartt C T, Bulet Philippe, Ferdig M T, Severson D W, Hoffmann Jules A, Christensen B M
Insect immunity: molecular cloning, expression, and characterization of cDNAs and genomic DNA encoding three isoforms of insect defensin in Aedes aegypti Journal Article
In: Insect Mol. Biol., vol. 8, no. 1, pp. 107–118, 1999, ISSN: 0962-1075.
Abstract | BibTeX | Tags: Aedes, Amino Acid, Animals, Base Sequence, Blotting, Chromosome Mapping, Cloning, Complementary, Defensins, DNA, Gene Expression, Hemolymph, hoffmann, M3i, Molecular, Northern, Protein Isoforms, Proteins, Sequence Homology
@article{lowenberger_insect_1999,
title = {Insect immunity: molecular cloning, expression, and characterization of cDNAs and genomic DNA encoding three isoforms of insect defensin in Aedes aegypti},
author = {C A Lowenberger and C T Smartt and Philippe Bulet and M T Ferdig and D W Severson and Jules A Hoffmann and B M Christensen},
issn = {0962-1075},
year = {1999},
date = {1999-02-01},
journal = {Insect Mol. Biol.},
volume = {8},
number = {1},
pages = {107--118},
abstract = {Aedes aegypti were immune activated by injection with bacteria, and the expression of insect defensins was measured over time. Northern analyses indicated that defensin transcriptional activity continued for at least 21 days after bacterial injection, and up to 10 days after saline inoculation. Mature defensin levels in the haemolymph reached approximately 45 microM at 24 h post inoculation. cDNAs encoding the preprodefensins of three previously described mature Ae. aegypti defensins were amplified by PCR, cloned and sequenced. Genomic clones were amplified using primers designed against the cDNA sequence. Sequence comparison indicates that there is significant inter- and intra-isoform variability in the signal peptide and prodefensin sequences of defensin genes. Preprodefensin sequences of isoforms A and B are very similar, consisting of a signal peptide region of twenty amino acids, a prodefensin region of thirty-eight amino acids and a forty amino acid mature peptide domain. The sequence encoding isoform C is significantly different, comprising a signal peptide region of twenty-three amino acids, a prodefensin region of thirty-six amino acids, and the mature protein domain of forty amino acids. Analysis of the genomic clones of each isoform revealed one intron spatially conserved in the prodefensin region of all sequences. The intron in isoforms A and B is 64 nt long, and except for a 4 nt substitution in one clone, these intron sequences are identical. The intron in isoform C is 76 nt long and does not share significant identity with the intron sequences of isoforms A or B. The defensin gene mapped to chromosome 3, between two known loci, blt and LF168.},
keywords = {Aedes, Amino Acid, Animals, Base Sequence, Blotting, Chromosome Mapping, Cloning, Complementary, Defensins, DNA, Gene Expression, Hemolymph, hoffmann, M3i, Molecular, Northern, Protein Isoforms, Proteins, Sequence Homology},
pubstate = {published},
tppubtype = {article}
}
Aedes aegypti were immune activated by injection with bacteria, and the expression of insect defensins was measured over time. Northern analyses indicated that defensin transcriptional activity continued for at least 21 days after bacterial injection, and up to 10 days after saline inoculation. Mature defensin levels in the haemolymph reached approximately 45 microM at 24 h post inoculation. cDNAs encoding the preprodefensins of three previously described mature Ae. aegypti defensins were amplified by PCR, cloned and sequenced. Genomic clones were amplified using primers designed against the cDNA sequence. Sequence comparison indicates that there is significant inter- and intra-isoform variability in the signal peptide and prodefensin sequences of defensin genes. Preprodefensin sequences of isoforms A and B are very similar, consisting of a signal peptide region of twenty amino acids, a prodefensin region of thirty-eight amino acids and a forty amino acid mature peptide domain. The sequence encoding isoform C is significantly different, comprising a signal peptide region of twenty-three amino acids, a prodefensin region of thirty-six amino acids, and the mature protein domain of forty amino acids. Analysis of the genomic clones of each isoform revealed one intron spatially conserved in the prodefensin region of all sequences. The intron in isoforms A and B is 64 nt long, and except for a 4 nt substitution in one clone, these intron sequences are identical. The intron in isoform C is 76 nt long and does not share significant identity with the intron sequences of isoforms A or B. The defensin gene mapped to chromosome 3, between two known loci, blt and LF168.
