A genome-wide screen identifies a single β-defensin gene cluster in the chicken: implications for the origin and evolution of mammalian defensins

Xiao, Yanjing; Hughes, Austin L.; Ando, Junko; Matsuda, Yoichi; Cheng, Jan‐Fang; Skinner-Noble, Donald; Zhang, Guolong

doi:10.1186/1471-2164-5-56

Cited by 264 publications

(192 citation statements)

References 44 publications

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“…Chickens have a single cluster of 13 beta-defensin genes (chromosome 3q) (Xiao et al 2004), opossums possess 37 genes in three clusters , and dog, human, mouse, and rat have 43, 39, 52, and 43 beta-defensin genes, respectively, in four to five clusters (Patil et al 2005). There is a clear evolutionary relationship between these conserved syntenic groups (Patil et al 2005), as the genes within syntenic clusters form separate clades in phylogenetic trees (Patil et al 2005;Belov et al 2007).…”

Section: Synteny Analysismentioning

confidence: 99%

“…2, 3; Supplemental material 5). The single chicken beta-defensin cluster (Xiao et al 2004) also shares homology with members of synteny group A, making this conserved beta-defensin cluster the most ancient synteny group. Synteny group A also contains the alpha-defensins, which are believed to have evolved from beta-defensins (Liu et al 1997;Patil et al 2004).…”

Section: Synteny Analysismentioning

confidence: 99%

“…The OvNGF-like peptide library consisted of endogenous beta-NGFs from vertebrates, and snake venom vNGFs (Supplemental Table 3). The OvDLP-like peptide library consisted of lizard venom crotamine-like peptides, snake crotasins, snake venom crotamines (Supplemental Table 4), eutherian beta-defensins (Patil et al 2005), chicken beta-defensins (Xiao et al 2004), and platypus beta-defensins identified as above. The alpha-defensin tree consisted of platypus alpha-defensins identified as above, plus eutherian alpha-defensins (Patil et al 2004), an opossum alpha-defensin , and chicken betadefensin-12 to root the resulting phylogenetic tree (GenBank accession no.…”

Section: Phylogenetic Analysismentioning

confidence: 99%

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Defensins and the convergent evolution of platypus and reptile venom genes

Whittington¹,

Papenfuss²,

Bansal³

et al. 2008

Genome Res.

131

104

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When the platypus (Ornithorhynchus anatinus) was first discovered, it was thought to be a taxidermist's hoax, as it has a blend of mammalian and reptilian features. It is a most remarkable mammal, not only because it lays eggs but also because it is venomous. Rather than delivering venom through a bite, as do snakes and shrews, male platypuses have venomous spurs on each hind leg. The platypus genome sequence provides a unique opportunity to unravel the evolutionary history of many of these interesting features. While searching the platypus genome for the sequences of antimicrobial defensin genes, we identified three Ornithorhynchus venom defensin-like peptide (OvDLP) genes, which produce the major components of platypus venom. We show that gene duplication and subsequent functional diversification of beta-defensins gave rise to these platypus OvDLPs. The OvDLP genes are located adjacent to the beta-defensins and share similar gene organization and peptide structures. Intriguingly, some species of snakes and lizards also produce venoms containing similar molecules called crotamines and crotamine-like peptides. This led us to trace the evolutionary origins of other components of platypus and reptile venom. Here we show that several venom components have evolved separately in the platypus and reptiles. Convergent evolution has repeatedly selected genes coding for proteins containing specific structural motifs as templates for venom molecules.

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Section: Synteny Analysismentioning

confidence: 99%

Section: Synteny Analysismentioning

confidence: 99%

Section: Phylogenetic Analysismentioning

confidence: 99%

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Defensins and the convergent evolution of platypus and reptile venom genes

Whittington¹,

Papenfuss²,

Bansal³

et al. 2008

Genome Res.

131

104

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“…The vertebrate defensins can be classified into three sub-families α, β, and θ, on the base of the pairs of cysteines that form intramolecular disulphide bridges [51][52][53][54]. The β-defensins are expressed in a wide range of tissues and organs such as the intestine and epithelium [55].…”

Section: Discussionmentioning

confidence: 99%

Antimicrobial Peptides Are Expressed during Early Development of Zebrafish (Danio rerio) and Are Inducible by Immune Challenge

Caccia

Agnello

Ceci

et al. 2017

Fishes

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Antimicrobial peptides (AMPS) are ancestral components in the evolution of immunity from protozoans to metazoans. Their expression can be constitutive or inducible by infectious challenge. Although characterized in detail in their structure and activity, the temporal and spatial expression of AMPS during vertebrate embryogenesis is still poorly understood. In the present study, we identified selected AMPs in zebrafish, and characterized their expression during early development, and upon experimental immune challenge in adult animals, with the goal of establishing this genetically-tractable model system for further AMP studies. By mining available genomic databases, zebrafish AMP sequences homologous to AMPs from other vertebrates were selected for further study. These included parasin I and its enzyme cathepsin D, β-defensin (DB1), liver-expressed antimicrobial peptide 2 (LEAP2), bactericidal permeability-increasing protein (BPI), and chromogranin-A and -B (CgA and CgB). Specific primers were designed for RT-PCR amplification of each AMP gene of interest and amplicons between 242 bp and 504 bp were obtained from RNA extracted from adult zebrafish. Sequencing of the amplicons and alignment of their deduced amino acid sequences with those from AMPs from other vertebrate species confirmed their identity. The temporal expression of AMPs was investigated by RT-PCR analysis in fertilized oocytes, embryos, and adult individuals. Parasin I and chatepsin D transcripts were detectable immediately after fertilization, while the transcripts for CgA and CgB became evident starting at 48 h post fertilization. Mature transcripts of LEAP2 and DB1 were detectable only in the adult zebrafish, while BPI transcripts were detectable starting from the 12th day post fertilization. To explore the possible upregulation of AMP expression by infectious challenge, experiments were carried out in adult zebrafish by intraperitoneal injection of a cocktail of lipopolysaccharide and lipoteichoic acid. Except for CgA and CgB, amplicons corresponding to all tested AMPs showed stronger signals in the experimental animals as compared to the unchallenged controls. This study provided information on the early expression of AMPs in zebrafish from ontogeny to adulthood and their inducibility by microbials. This information could be useful to actuate new prophylactic strategies as an alternative to the use of antibiotics in culture.

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“…a-and b-defensins are widely distributed in vertebrates, invertebrates and plants [8][9][10][11], while h-defensins are expressed only in rhesus macaque [12]. In human and mouse, more than 30 while in birds 14 b-defensins have been identified [13][14][15][16]. There are few fish species including Danio rerio (zfDB1-3) [1], Tetraodon nigroviridis (tnDB 1 and 2) [1], Takifugu rubripes (fuDB) [1], Oncorhynchus mykiss (omDB [1][2][3][4] [17,18], medaka (mkDB) [19], Epinephelus coioides (ogDB) [20], Paralichthys olivaceus of (DBI 1-5) [21] where single and multiple isoforms of b-defensin have been reported.…”

Section: Introductionmentioning

confidence: 99%

Molecular Characterization and In Silico Analysis of Defensin From Tor putitora (Hamilton)

Chaturvedi

Dhanik

Pande

2015

Probiotics & Antimicro. Prot.

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Antimicrobial peptides (AMPs) are vital constituents of innate immune system. In fish, one of the most important AMP is β-defensin that has a potential to activate the adaptive immune system. β-defensin is a cysteine-arginine-rich cationic AMP with broad spectrum activity against microbes. In this study, we identified cloned and characterized β-defensin 1 from Tor putitora, a cold water fish species also known as mahseer. An open reading frame of β-defensin 1 was amplified, cloned and sequenced which encodes a peptide of 67 amino acid residues. The pro-peptide includes a signal peptide comprising 24 amino acids as predicted by Signal P along with a mature peptide of 43 amino acid residues. Tor putitora β-defensin 1 (TP-βdf1) has a molecular weight of 4.6 kDa with a pI of 8.35. Six cysteine residues are present in the mature peptide which is a characteristic feature of defensins. All six cysteine residues are involved in the formation of three intra-molecular disulfide bonds. Three-dimensional modeling of mature peptide of TP-βdf1 was carried out using Modeller 9.10, and validated TP-βdf1 model revealed three β-sheets. The cysteine residues form three disulfide bonds in the pattern of Cys(1)-Cys(5), Cys(2)-Cys(4), Cys(3)-Cys(6) stabilizing the β-sheet. Structural analysis revealed three β-strands and an α-helix at the N terminus. Phylogenetic analysis revealed that the β-defensin 1 of Tor putitora was close to Megalobrama amblycephala which possibly suggests that TP-βdf1 peptide sequence is quite similar to β-defensin peptide sequences of carps and minnows.

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A genome-wide screen identifies a single β-defensin gene cluster in the chicken: implications for the origin and evolution of mammalian defensins

Cited by 264 publications

References 44 publications

Defensins and the convergent evolution of platypus and reptile venom genes

Defensins and the convergent evolution of platypus and reptile venom genes

Antimicrobial Peptides Are Expressed during Early Development of Zebrafish (Danio rerio) and Are Inducible by Immune Challenge

Molecular Characterization and In Silico Analysis of Defensin From Tor putitora (Hamilton)

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