Dataset Information

Inhibitors molecules isolated from midgut and midgut diverticula of the spider Nephilingis cruentata

ABSTRACT: Spiders are insect predators and their venoms are important to prey capture. Spider venomshave several potential applications as pharmaceutical compounds and insecticides. However,transcriptomic and proteomic analyses of the digestive system (DS) of spiders show that DS is also a rich source of new inhibitor molecules. Biochemical, transcriptomic and proteomic data of crude DS extracts show the presence of molecules with inhibitor potential in the spider Nephilingis cruentata. Therefore, the aims of this work were to isolate and characterize molecules with serine peptidase inhibitory activity. The DS of fasting adult females was homogenized under acidic conditions and subjected to heat treatment. After that, samples were submitted to ion exchange batch and high-performance reverse-phase chromatography. The fractions with inhibitory activity were confirmed by mass spectrometry, identifying 6 molecules with inhibitor potential. The inhibitor Nc6834 was kinetically characterized, showing a KD value of 30.25 nM ± 8.13. Analysis of the tertiary structure by molecular modeling using Alpha-Fold2 indicates that the inhibitor Nc6834 structurally belongs to theMIT1-like atracotoxin family. This is the first time that a serine peptidase inhibitory function is attributed to this structural family and the reactive site inhibitor residue is identified. Sequence analysis indicates that these molecules may be present in the DS of other spiders.

INSTRUMENT(S): Dionex instrument model

ORGANISM(S): Nephilengys Cruentata

TISSUE(S): Epithelium Of Midgut, Midgut Diverticulum

SUBMITTER: Oscar Bento

LAB HEAD: Adriana Rios Lopes

PROVIDER: PXD037594 | Pride | 2023-03-11

REPOSITORIES: Pride

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Publications

Spiders' digestive system as a source of trypsin inhibitors: functional activity of a member of atracotoxin structural family.

Neto Oscar Bento Silva OBS Valladão Rodrigo R Coelho Guilherme Rabelo GR Dias Renata R Pimenta Daniel Carvalho DC Lopes Adriana Rios AR

Scientific reports 20230210 1

Spiders are important predators of insects and their venoms play an essential role in prey capture. Spider venoms have several potential applications as pharmaceutical compounds and insecticides. However, transcriptomic and proteomic analyses of the digestive system (DS) of spiders show that DS is also a rich source of new peptidase inhibitor molecules. Biochemical, transcriptomic and proteomic data of crude DS extracts show the presence of molecules with peptidase inhibitor potential in the spi ...[more]

PMID: 36765114

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Project description:Spiders are a highly diverse group of arthropods that occur in most habitats on land. Notably, spiders have significant ecological impact as predators because of their extraordinary prey capture adaptations, venom and silk. Spider venom is among the most heterogeneous animal venoms and has pharmacological applications, while spider silk is characterized by great toughness with potential for biomaterial application. We describe the genome sequences of two spiders representing two major taxonomic groups, the social velvet spider Stegodyphus mimosarum (Araneomorphae), and the Brazilian white-knee tarantula Acanthoscurria geniculata (Mygalomorphae). We annotate genes using a combination of transcriptomic and in-depth proteomic analyses. The genomes are large (2.6 Gb and 6 Gb, respectively) with short exons and long introns and approximately 50% repeats, reminiscent of typical mammalian genomes. Phylogenetic analyses show that spiders and ticks are sister groups outgrouped by mites, and phylogenetic dating using a molecular clock dates separation of velvet spider and tarantula at 270 my. Based on the genomes and proteomes, we characterize the genetic basis of venom and silk production of both species in detail. Venom protein composition differs markedly between the two spiders, with lipases as the most abundant protein in the velvet spider and present only at low concentration in tarantula. Venom in both spiders contains proteolytic enzymes, and our analyses suggest that these enzymes target and process precursor peptides that subsequently mediate the toxic effects of venom. Complete analysis of silk genes reveal a diverse suite of silk proteins in the velvet spider including novel types of spidroins, and dynamic evolution of major ampullate spidroin genes, whereas silk protein diversity in tarantula is far less complex. The difference in silk proteins between species is consistent with a more complex silk gland morpholgy and use of three-dimentional capture webs consisting of multiple silk types in aranomorph spiders.

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Dataset Information

Inhibitors molecules isolated from midgut and midgut diverticula of the spider Nephilingis cruentata

Publications

Spiders' digestive system as a source of trypsin inhibitors: functional activity of a member of atracotoxin structural family.

Similar Datasets

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