Sphingomyelinase D in sicariid spider venom is a potent insecticidal toxin

Zobel-Thropp, Pamela A.; Kerins, Alec E.; Binford, Greta J.

doi:10.1016/j.toxicon.2012.04.350

Cited by 45 publications

(47 citation statements)

References 61 publications

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“…CPE is a major phosphosphingolipid in insects (47), the main prey item of the sicariid spiders (30); SM, by contrast, dominates in mammals (71,72). As noted above, some ␤I clade members show diminished toxicity in mammalian models (7-10, 25, 26).…”

Section: Discussionmentioning

confidence: 99%

“…The three toxins in this study are as follows: La_␣IB2bi (gb:AY699703); La_␤ID1 from L. arizonica (gb:KM884812); St_␤IB1i from S. terrosus (gb:KM884813). La_␣IB2bi has been identified and studied previously (15,30) and is used here as a representative of the SicTox ␣ clade. St_␤IB1i from S. terrosus was chosen as a representative of the ␤ clade.…”

Section: Methodsmentioning

confidence: 99%

“…Cloning of DNA sequences, encoding the mature PLD toxins St_␤IB1i and La_␤ID1 obtained from cDNA libraries, into pHis8 expression vectors (34) was performed as described previously for La_␣IB2bi (15,30). Sequence variants of St_ ␤IB1i were generated using QuikChange site-directed mutagenesis according to the manufacturer's protocol.…”

Section: Methodsmentioning

confidence: 99%

“…In the case of ␤1A1 (SMase II) from L. laeta, SMase D activity has been observed but with a 3-fold higher K m value and a reported 2-fold lower reaction rate at saturating substrate concentrations compared with ␣III1 (SMase I) from the same species (26). References for structure and activity data are as follows: IsSMase (74); LiRecDT6 (11); LiRecDT7 (14); SMase I (8,18,27,35,59,64,75); Ll2 (8); LiRecDT4 (9); LgRec1 (76); Lr1/Lb1/Lb2 (8,25); L. arizonica ␣IB2bi (15,30); Lr2 (19,25); P1/P2 (77-79); LiRecDT1 (6,7,12,13,20,60); 3RLG (61); 3RLH (28); LiRecDT2 (7); LiRecDT5 (9); Lb3 (8,25); LiRecDT3 (7,10); and SMase II (26).…”

Section: Methodsmentioning

confidence: 99%

“…Here, we utilize 31 P NMR-based substrate screening to identify substrates and substrate preferences for two diverse ␤I clade members as follows: St_␤IB1i from Sicarius terrosus, a New World species that lacks venom SMase D activity in vitro and has no known ␣ clade toxins (24); and La_␤ID1 from Loxosceles arizonica, a species that is known to cause loxoscelism and does produce ␣ clade toxins (30 -32). We include parallel characterization of La_␣IB2bi, a previously characterized ␣ clade toxin from L. arizonica (15,30), both as a positive control for activity against SM and LPC ( Fig. 2) and to provide a direct comparison between substrate preferences of ␣ clade and ␤I clade members.…”

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confidence: 99%

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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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Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

See 3 more Smart Citations

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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Predation on a pygmy shrew, Sorex minutus, by the noble false widow spider, Steatoda nobilis

et al. 2023

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The noble false widow spider Steatoda nobilis is a globally invasive species with implications for public health and possibly for native ecosystems. Here, we report on a case of predation on a protected species of vertebrate, a pygmy shrew Sorex minutus in Britain. The importance and novelty of this report are: (1) this is the third documented case of S. nobilis preying on a vertebrate in five years, suggesting that small vertebrates are likely to be a more frequent component of their diet than previously thought; (2) this is the first case of a Theridiidae spider preying on a shrew in Britain; and (3) this is the first case of predation on shrews by the genus Steatoda globally. Overall, S. nobilis fits the profile of a habitual vertebrate-eating spider.

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Protein salvage and repurposing in evolution: Phospholipase D toxins are stabilized by a remodeled scrap of a membrane association domain

Cordes,

Sundman,

Fox

et al. 2023

Protein Science

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The glycerophosphodiester phosphodiesterase (GDPD)‐like SMaseD/PLD domain family, which includes phospholipase D (PLD) toxins in recluse spiders and actinobacteria, evolved anciently in bacteria from the GDPD. The PLD enzymes retained the core (β/α)8 barrel fold of GDPD, while gaining a signature C‐terminal expansion motif and losing a small insertion domain. Using sequence alignments and phylogenetic analysis, we infer that the C‐terminal motif derives from a segment of an ancient bacterial PLAT domain. Formally, part of a protein containing a PLAT domain repeat underwent fusion to the C terminus of a GDPD barrel, leading to attachment of a segment of a PLAT domain, followed by a second complete PLAT domain. The complete domain was retained only in some basal homologs, but the PLAT segment was conserved and repurposed as the expansion motif. The PLAT segment corresponds to strands β7–β8 of a β‐sandwich, while the expansion motif as represented in spider PLD toxins has been remodeled as an α‐helix, a β‐strand, and an ordered loop. The GDPD‐PLAT fusion led to two acquisitions in founding the GDPD‐like SMaseD/PLD family: (1) a PLAT domain that presumably supported early lipase activity by mediating membrane association, and (2) an expansion motif that putatively stabilized the catalytic domain, possibly compensating for, or permitting, loss of the insertion domain. Of wider significance, messy domain shuffling events can leave behind scraps of domains that can be salvaged, remodeled, and repurposed.

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Sphingomyelinase D in sicariid spider venom is a potent insecticidal toxin

Cited by 45 publications

References 61 publications

Variable Substrate Preference among Phospholipase D Toxins from Sicariid Spiders

Variable Substrate Preference among Phospholipase D Toxins from Sicariid Spiders

Predation on a pygmy shrew, Sorex minutus, by the noble false widow spider, Steatoda nobilis

Protein salvage and repurposing in evolution: Phospholipase D toxins are stabilized by a remodeled scrap of a membrane association domain

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