Neoscona shillongensis (Araneidae), also known as the Shillong orb-weaving spider, is a species that constructs a typically shaped round web, is inactive during the daytime and comes out at dusk to forage, primarily preying on flying insects such as mosquitoes, flies, and moths. This spider serves as an important natural enemy of agricultural and forest pests. Neoscona shillongensis primarily uses its web to capture prey, but its venom also plays a crucial role in subduing and processing prey. To date, no research has been conducted on the composition of N. shillongensis venom. In This study, conducted high-throughput sequencing on the venom gland transcriptome and the venom gland extract proteome. A cDNA library of the venom gland tissue of N. shillongensis was constructed, yielding over 62 million reads, which were assembled into 90,481 sequences, predicting 171 toxin-like sequences, including 94 peptide toxins and 77 protein toxins. Furthermore, proteomic analyses of the venom gland extract samples identified 53 peptides and proteins, including 23 peptide toxins and 30 enzymes or proteins such as acetylcholinesterase, hyaluronidase, and astacin-like metalloproteases. The results revealed that the toxin composition of N. shillongensis is diverse and complex. This study provides essential baseline data for further research on the evolution and physiological activity of spider venom, as well as the potential development of pharmaceutical compounds therefrom.
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http://dx.doi.org/10.1016/j.ibmb.2025.104289 | DOI Listing |
J Proteomics
March 2025
Universidad de Panamá, Facultad de Medicina, Centro de Investigación e Información de Medicamentos y Tóxicos, Ciudad de Panamá, Panama; Universidad de Panamá, Facultad de Ciencias Naturales, Exactas y Tecnología, Departamento de Bioquímica, Ciudad de Panamá, Panama. Electronic address:
The sting of the scorpion Centruroides bicolor causes a large morbidity in Panama. To characterize its venom, transcriptomic and proteomic analyses of the venom glands and the crude venom were performed. These two approaches utilized high-throughput sequencing to enhance the likelihood of detecting a wide range of venom proteins correlated with the venom proteome.
View Article and Find Full Text PDFInsect Biochem Mol Biol
March 2025
Yunnan Provincial Key Laboratory of Entomological Biopharmaceutical Research & Development, College of Pharmacy, Dali University, Dali, Yunnan, 671000, China; National Local Joint Engineering Research Centre for the Development of Medicinal Specialty Insects, Dali University, Dali, Yunnan, 671000, China. Electronic address:
Neoscona shillongensis (Araneidae), also known as the Shillong orb-weaving spider, is a species that constructs a typically shaped round web, is inactive during the daytime and comes out at dusk to forage, primarily preying on flying insects such as mosquitoes, flies, and moths. This spider serves as an important natural enemy of agricultural and forest pests. Neoscona shillongensis primarily uses its web to capture prey, but its venom also plays a crucial role in subduing and processing prey.
View Article and Find Full Text PDFJ Proteomics
February 2025
Departamento de Medicina Molecular y Bioprocesos, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Cuernavaca, Morelos, Mexico.
Species of the genus Micrurus belong to the family Elapidae and possess venoms of significant clinical importance. This study presents an analysis of the venom composition of Micrurus ephippifer, employing transcriptomic and proteomic methodologies. A total of 2885 venom gland transcripts were assembled, of which 42 were identified as toxins.
View Article and Find Full Text PDFPestic Biochem Physiol
March 2025
Key Laboratory of Integrated Management of Crop Diseases and Pests (Ministry of Education), College of Plant Protection, Nanjing Agricultural University, Nanjing 210095, China. Electronic address:
Spider peptide toxins, as potent insecticides, distinguish them from current insecticides, and thus expand the range of viable molecular targets of insecticides in insect pests. This study reports the isolation of two neurotoxic peptides, ω-Atyptoxin-Cs2a (Cs2a) and ω-Atyptoxin-Cs2b (Cs2b), from the venom gland of the burrowing spider Calommata signata. These peptides exhibit strong insecticidal activity against two insect pests with agricultural importance, Nilaparvata lugens and Spodoptera frugiperda.
View Article and Find Full Text PDFBMC Genomics
February 2025
Department of Ecology, Center of Infectious Animal Diseases, Faculty of Environmental Sciences, Czech University of Life Sciences, Prague, Czechia.
Background: Venom allergen-like proteins (VALs) are abundant in the excretory-secretory products (ESPs) of numerous parasitic helminths and have been extensively studied for over 30 years because of their potential to interact with host systems. Despite substantial research, however, the precise functions of these proteins remain largely unresolved. Schistosomes, parasites of the circulatory system, are no exception, with 29 SmVAL genes identified in the genome of Schistosoma mansoni to date.
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