Recombinant Production and Characterization of a New Toxin from Cryptops iheringi Centipede Venom Revealed by Proteome and Transcriptome Analysis

• Published in: Toxins Vol. 13; no. 12; p. 858
• Main Authors: De Lucca Caetano, Lhiri Hanna, Nishiyama-Jr, Milton Yutaka, de Carvalho Lins Fernandes Távora, Bianca, de Oliveira, Ursula Castro, de Loiola Meirelles Junqueira-de-Azevedo, Inácio, Faquim-Mauro, Eliana L, Magalhães, Geraldo Santana
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 02-12-2021; MDPI
• Subjects: Animals; Arthropod Venoms - chemistry; Arthropod Venoms - toxicity; centipede; Chilopoda - chemistry; Chilopoda - genetics; Cloning; Cryptops iheringi; E coli; Edema; Edema - chemically induced; Gene expression; Gene Expression Profiling; Immune Sera; Leukocytes (neutrophilic); Male; Mass spectrometry; Metropolitan areas; Mice; Mice, Inbred BALB C; Peptides; Proteins; Proteome; Proteomes; Proteomics; Rabbits; Recombinant Proteins; Scientific imaging; toxin; Toxins; transcriptome; Transcriptomes; Transcriptomics; Venom; Venom gland; Brazil; venom; Cryptops iheringi; toxin; recombinant protein; transcriptome; chilopoda; venomics; centipede; proteome
• ISSN: 2072-6651; 2072-6651
• DOI: 10.3390/toxins13120858

Among the Chilopoda class of centipede, the
genus is one of the most associated with envenomation in humans in the metropolitan region of the state of São Paulo. To date, there is no study in the literature about the toxins present in its venom. Thus, in this work, a transcriptomic characterization of the
venom gland, as well as a proteomic analysis of its venom, were performed to obtain a toxin profile of this species. These methods indicated that 57.9% of the sequences showed to be putative toxins unknown in public databases; among them, we pointed out a novel putative toxin named Cryptoxin-1. The recombinant form of this new toxin was able to promote edema in mice footpads with massive neutrophils infiltration, linking this toxin to envenomation symptoms observed in accidents with humans. Our findings may elucidate the role of this toxin in the venom, as well as the possibility to explore other proteins found in this work.