Solution structure of a defensin-like peptide from platypus venom

Torres, Allan M.; WANG, Xiuhong; FLETCHER, Jamie I.; Alewood, Dianne; Alewood, Paul F.; SMITH, Ross; Simpson, Richard J.; Nicholson, Graham M.; SUTHERLAND, Struan K.; GALLAGHER, Cliff H.; King, Glenn F.; Kuchel, Philip W.

doi:10.1042/0264-6021:3410785

Cited by 41 publications

(46 citation statements)

References 28 publications

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“…Three of these unidentified genes were found to encode defensin-like peptides (OvDLPs), the main peptide components of platypus venom, as they matched partial peptide sequences obtained experimentally (Torres et al 1999), and the remaining gene appeared to be an intermediate between betadefensins and OvDLPs. It has also previously been suggested that some components of reptile venom may be homologous to betadefensins (Zhao et al 2001).…”

Section: Identification Of Platypus Venom Genesmentioning

confidence: 99%

“…The platypus OvDLPs are a family of 5-kD peptides (Torres et al 1999). The similarity in sequence and structure between betadefensins and OvDLPs suggests that they are evolutionarily related.…”

Section: Platypus Venom Ovdlpsmentioning

confidence: 99%

“…The unusual nature of the symptoms of platypus envenomation may be due to the complex mixture of many different peptides and proteins in the venom, some of which have unknown function (de Plater et al 1995;Whittington and Belov 2007). Nineteen different fractions have been found in platypus venom (de Plater et al 1995;Kourie 1999), but only three have been sequenced: OvDLPs (Torres et al 1999), C-type natriuretic peptides (OvCNPs) (de Plater et al 1998), and nerve growth factors (OvNGFs) (partially sequenced by A. Torres and P.W.…”

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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.

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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: Identification Of Platypus Venom Genesmentioning

confidence: 99%

Section: Platypus Venom Ovdlpsmentioning

confidence: 99%

mentioning

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.

Self Cite

131

104

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“…This shows that high toxin diversity in venoms is attained not only by the expression of multiple paralogs, but also by domain variation in a multidomain single-product gene formed by tandem repeats within an ancestral monodomain gene. The defensin-like peptides isolated from platypus venom are related to the β-defensin class found only in vertebrates but their bioactivities remain to be elucidated (152).…”

Section: Figurementioning

confidence: 99%

The Toxicogenomic Multiverse: Convergent Recruitment of Proteins Into Animal Venoms

Fry

Roelants

Champagne

et al. 2009

Annu. Rev. Genom. Hum. Genet.

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722

778

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Throughout evolution, numerous proteins have been convergently recruited into the venoms of various animals, including centipedes, cephalopods, cone snails, fish, insects (several independent venom systems), platypus, scorpions, shrews, spiders, toxicoferan reptiles (lizards and snakes), and sea anemones. The protein scaffolds utilized convergently have included AVIT/colipase/prokineticin, CAP, chitinase, cystatin, defensins, hyaluronidase, Kunitz, lectin, lipocalin, natriuretic peptide, peptidase S1, phospholipase A 2 , sphingomyelinase D, and SPRY. Many of these same venom protein types have also been convergently recruited for use in the hematophagous gland secretions of invertebrates (e.g., fleas, leeches, kissing bugs, mosquitoes, and ticks) and vertebrates (e.g., vampire bats). Here, we discuss a number of overarching structural, functional, and evolutionary generalities of the protein families from which these toxins have been frequently recruited and propose a revised and expanded working definition for venom. Given the large number of striking similarities between the protein compositions of conventional venoms and hematophagous secretions, we argue that the latter should also fall under the same definition. 483

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“…A search of protein structures using DALI (33) found structural homology of hBD2 with the two other defensins, as well as a defensin-like peptide from platypus venom (1b8w) (34) and two sea anemone toxins (35,36). A comparison of the electrostatic surface potential of hBD2 and these homologous structures (Protein Data Bank accession codes 1bnb, 1dfn, 1b8w, 1ahl, and 1sh1) shows a wide range of charges and charge positions.…”

Section: Fig 2 Stereo Drawing Of the Over-mentioning

confidence: 99%

The Structure of Human β-Defensin-2 Shows Evidence of Higher Order Oligomerization

Hoover¹,

Rajashankar²,

Blumenthal³

et al. 2000

Journal of Biological Chemistry

322

321

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Defensins are small cationic peptides that are crucial components of innate immunity, serving as both antimicrobial agents and chemoattractant molecules. The specific mechanism of antimicrobial activity involves permeabilization of bacterial membranes. It has been postulated that individual monomers oligomerize to form a pore through anionic membranes, although the evidence is only indirect. Here, we report two high resolution x-ray structures of human ␤-defensin-2 (hBD2). The phases were experimentally determined by the multiwavelength anomalous diffraction method, utilizing a novel, rapid method of derivatization with halide ions. Although the shape and charge distribution of the monomer are similar to those of other defensins, an additional ␣-helical region makes this protein topologically distinct from the mammalian ␣-and ␤-defensin structures reported previously. hBD2 forms dimers topologically distinct from that of human neutrophil peptide-3. The quaternary octameric arrangement of hBD2 is conserved in two crystal forms. These structures provide the first detailed description of dimerization of ␤-defensins, and we postulate that the mode of dimerization of hBD2 is representative of other ␤-defensins. The structural and electrostatic properties of the hBD2 octamer support an electrostatic charge-based mechanism of membrane permeabilization by ␤-defensins, rather than a mechanism based on formation of bilayer-spanning pores.

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Solution structure of a defensin-like peptide from platypus venom

Cited by 41 publications

References 28 publications

Defensins and the convergent evolution of platypus and reptile venom genes

Defensins and the convergent evolution of platypus and reptile venom genes

The Toxicogenomic Multiverse: Convergent Recruitment of Proteins Into Animal Venoms

The Structure of Human β-Defensin-2 Shows Evidence of Higher Order Oligomerization

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