In-depth transcriptome reveals the potential biotechnological application of Bothrops jararaca venom gland

Abstract

Background: Lack of complete genomic data of Bothrops jararaca impedes molecular biology research focusing on biotechnological applications of venom gland components. Identification of full-length coding regions of genes is crucial for the correct molecular cloning design. Methods: RNA was extracted from the venom gland of one adult female specimen of Bothrops jararaca . Deep sequencing of the mRNA library was performed using Illumina NextSeq 500 platform. De novo assembly of B. jararaca transcriptome was done using Trinity. Annotation was performed using Blast2GO. All predicted proteins after clustering step were blasted against non-redundant protein database of NCBI using BLASTP. Metabolic pathways present in the transcriptome were annotated using the KAAS-KEGG Automatic Annotation Server. Toxins were identified in the B. jararaca predicted proteome using BLASTP against all protein sequences obtained from Animal Toxin Annotation Project from Uniprot KB/Swiss-Pro database. Figures and data visualization were performed using ggplot2 package in R language environment. Results: We described the in-depth transcriptome analysis of B. jararaca venom gland, in which 76,765 de novo assembled isoforms, 96,044 transcribed genes and 41,196 unique proteins were identified. The most abundant transcript was the zinc metalloproteinase-disintegrin-like jararhagin. Moreover, we identified 78 distinct functional classes of proteins, including toxins, inhibitors and tumor suppressors. Other venom proteins identified were the hemolytic lethal factors stonustoxin and verrucotoxin. Conclusion: It is believed that the application of deep sequencing to the analysis of snake venom transcriptomes may represent invaluable insight on their biotechnological potential focusing on candidate molecules.

Altered RNome expression in Murine Gastrocnemius Muscle following Exposure to Jararhagin, a Metalloproteinase from Bothrops jararaca Venom

“…The venom of B. jararaca is extremely protein rich and contains a range of enzymes, including metalloproteases, serine proteinases, phospholipases A2 (PLA2), and L-amino acid oxidases [ 8 , 9 ]. Several metalloproteases have been identified from the venom of B. jararaca , including bothropasin, HF3 [ 10 ] jararafibrase I [ 11 ], and jararhagin [ 12 ].…”

Altered RNome expression in Murine Gastrocnemius Muscle Following Exposure to Jararhagin, a Metalloproteinase from Bothrops Jararaca Venom

“…Clinically, serumtherapy is the only effective treatment for Bothrops envenoming; however, this approach is ineffective in reducing the fast setting local effects induced by the envenomation, implying that activation of endogenous mediators plays an important role in the local reaction [5]. Previous studies conducted by our group has shown that the pro-inflammatory effect of Bothrops jararaca venom is caused by the presence of metalloproteases in the venom [6,7] The venom of B. jararaca is extremely protein-rich and contains a range of enzymes, including metalloproteases, serine proteinases, phospholipases (PLA2), and L-amino acid oxidases [8,9]. Several metalloproteases have been identified from the venom of B. jararaca, including bothropasin, HF3 [10] jararafibrase I [11], and jararhagin [12].…”

Bothrops Jararaca Snake Venom Modulates Key Cancer-Related Proteins in Breast Tumor Cell Lines

“…About 90 to 95% of the dry weight of the B. jararaca venom is composed of a complex mixture of proteins, mainly metalloproteinases, serine proteinases, phospholipases (PLA2), and L-amino acid oxidases. The metalloproteinases comprise most of the venom composition [ 20 , 21 ]. They are proteolytic enzymes associated with fibrinolysis and coagulation, and they are involved in cell migration and tissue repair, besides being related to pathological effects such as cancer [ 22 , 23 ].…”