Lateral gene transfer of a dermonecrotic toxin between spiders and bacteria

Cordes, Matthew; Binford, Greta J.

doi:10.1093/bioinformatics/bti811

Cited by 38 publications

(36 citation statements)

References 18 publications

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“…This enzyme display broad specificity for glycerophosphodiesters, glycerophosphocholine, glycerophosphoethanolamine, glycerophosphoglycerol and bis (glycerophosphoglycerol), all of which are hydrolysed by this enzyme. This gene also has been reported to be involved in HGT between spider and bacteria [40]. Expression analysis suggested that this gene was not only highly expressed in integument and fat body but also in midgut and hemocyte.…”

Section: Resultsmentioning

confidence: 98%

Horizontal gene transfer in silkworm, Bombyx mori

et al. 2011

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BackgroundThe domesticated silkworm, Bombyx mori, is the model insect for the order Lepidoptera, has economically important values, and has gained some representative behavioral characteristics compared to its wild ancestor. The genome of B. mori has been fully sequenced while function analysis of BmChi-h and BmSuc1 genes revealed that horizontal gene transfer (HGT) maybe bestow a clear selective advantage to B. mori. However, the role of HGT in the evolutionary history of B. mori is largely unexplored. In this study, we compare the whole genome of B. mori with those of 382 prokaryotic and eukaryotic species to investigate the potential HGTs.ResultsTen candidate HGT events were defined in B. mori by comprehensive sequence analysis using Maximum Likelihood and Bayesian method combining with EST checking. Phylogenetic analysis of the candidate HGT genes suggested that one HGT was plant-to- B. mori transfer while nine were bacteria-to- B. mori transfer. Furthermore, functional analysis based on expression, coexpression and related literature searching revealed that several HGT candidate genes have added important characters, such as resistance to pathogen, to B. mori.ConclusionsResults from this study clearly demonstrated that HGTs play an important role in the evolution of B. mori although the number of HGT events in B. mori is in general smaller than those of microbes and other insects. In particular, interdomain HGTs in B. mori may give rise to functional, persistent, and possibly evolutionarily significant new genes.

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Section: Resultsmentioning

confidence: 98%

Horizontal gene transfer in silkworm, Bombyx mori

et al. 2011

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“…Smase D enzymes in both lineages contain similar C-terminal plug motifs and, in the absence of phylogenetic analyses, the disjunct presence of this motif in both lineages was put forward as evidence for a lateral gene transfer event (32 …”

Section: Sphingomyelinase Dmentioning

confidence: 99%

“…This scenario gains support from the fact that both the fungal and the tick enzymes contain C-terminal plug motifs that differ from the identical motifs in the bacterial and spider toxins. In SmaseD of both Corynebacterium (bacteria) and Loxosceles (spider), Asn residues at position 278 contribute a backbone hydrogen bond, causing subsequent residues to form a type-I β-turn, which blocks the N-terminal end of the TIM (triosephosphate isomerase) barrel (32). In the enzymes of the tick, fungi, and non-Corynebacterium bacteria, various other residues occupy position 278 (Asp in the tick; Ala, Lys, Ser, or Thr in fungi; and Ile in Arcanobacterium), potentially affecting the plugging of the barrel.…”

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.

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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“…8, below). GDPDs are distantly related to the SicTox proteins (27,64,65), and their mechanism has been proposed to proceed through a five-membered cyclic phosphate intermediate (45) analogous to the product of the toxin action on lysophospholipids (15). We felt that the conformation of the glycerol phosphate in the GDPD active site was a reasonable model for the phosphoglycerol portion of LPC or LPE bound to the toxin in a catalytically competent mode.…”

Section: Structural Comparison Of St_␤ib1i With Other Sictox Proteinsmentioning

confidence: 99%

“…One possibility is that the SicTox mechanism is homologous to the first step of the mechanism of GDPD enzymes, which are distantly related (27,64,65). GDPDs hydrolyze phosphoglycerol substrates and have been proposed to form a cyclic intermediate analogous to the lipid product of the action of SicTox enzymes on lysophospholipids (45).…”

Section: Structural Comparison Of St_␤ib1i With Other Sictox Proteinsmentioning

confidence: 99%

Variable Substrate Preference among Phospholipase D Toxins from Sicariid Spiders

Lajoie

Roberts

Zobel-Thropp

et al. 2015

Journal of Biological Chemistry

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Background: Phospholipase D toxins from brown spider venoms can cause disease in humans. Results: Different toxin family members show specificity for lipid substrates with choline or ethanolamine headgroups or can be ambiguous. Conclusion: Spider phospholipase D toxins have evolved diverse substrate preferences. Significance: The diverse substrate preference may be significant for predation and the mammalian toxicity of venom.

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Lateral gene transfer of a dermonecrotic toxin between spiders and bacteria

Cited by 38 publications

References 18 publications

Horizontal gene transfer in silkworm, Bombyx mori

Horizontal gene transfer in silkworm, Bombyx mori

The Toxicogenomic Multiverse: Convergent Recruitment of Proteins Into Animal Venoms

Variable Substrate Preference among Phospholipase D Toxins from Sicariid Spiders

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