» Articles » PMID: 33149734

In-depth Transcriptome Reveals the Potential Biotechnological Application of Venom Gland

Abstract

Background: Lack of complete genomic data of 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 . Deep sequencing of the mRNA library was performed using Illumina NextSeq 500 platform. assembly of 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 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 venom gland, in which 76,765 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.

Citing Articles

Exploring the Venom Gland Transcriptome of and : De Novo Assembly and Analysis of Novel Toxic Proteins.

Espin-Angulo J, Vela D Toxins (Basel). 2024; 16(12.

PMID: 39728769 PMC: 11728684. DOI: 10.3390/toxins16120511.


Current Technologies in Snake Venom Analysis and Applications.

Roman-Ramos H, Ho P Toxins (Basel). 2024; 16(11).

PMID: 39591213 PMC: 11598588. DOI: 10.3390/toxins16110458.


Proteomics and life-history variability of Endogenous Phospholipases A2 Inhibitors (PLIs) in Bothrops jararaca plasma.

Serino-Silva C, Bittencourt Rodrigues C, Miyamoto J, Hatakeyama D, Kavazoi V, Teixeira da Rocha M PLoS One. 2024; 19(2):e0295806.

PMID: 38319909 PMC: 10846723. DOI: 10.1371/journal.pone.0295806.


Crosstalk of Inflammation and Coagulation in Snakebite Envenoming: Endogenous Signaling Pathways and Pathophysiology.

Cavalcante J, de Almeida D, Santos-Filho N, Sartim M, de Almeida Baldo A, Brasileiro L Int J Mol Sci. 2023; 24(14).

PMID: 37511277 PMC: 10380640. DOI: 10.3390/ijms241411508.


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

Nascimento A, Zychar B, Pessoa R, Duarte A, Clissa P, Sanabani S Toxins (Basel). 2022; 14(7).

PMID: 35878210 PMC: 9321239. DOI: 10.3390/toxins14070472.


References
1.
Kanehisa M, Goto S, Sato Y, Furumichi M, Tanabe M . KEGG for integration and interpretation of large-scale molecular data sets. Nucleic Acids Res. 2011; 40(Database issue):D109-14. PMC: 3245020. DOI: 10.1093/nar/gkr988. View

2.
Goncalves-Machado L, Pla D, Sanz L, Jorge R, Leitao-De-Araujo M, Alves M . Combined venomics, venom gland transcriptomics, bioactivities, and antivenomics of two Bothrops jararaca populations from geographic isolated regions within the Brazilian Atlantic rainforest. J Proteomics. 2015; 135:73-89. DOI: 10.1016/j.jprot.2015.04.029. View

3.
Wilson D, Madera M, Vogel C, Chothia C, Gough J . The SUPERFAMILY database in 2007: families and functions. Nucleic Acids Res. 2006; 35(Database issue):D308-13. PMC: 1669749. DOI: 10.1093/nar/gkl910. View

4.
. UniProt: a hub for protein information. Nucleic Acids Res. 2014; 43(Database issue):D204-12. PMC: 4384041. DOI: 10.1093/nar/gku989. View

5.
Boldrini-Franca J, Cologna C, Pucca M, de Castro Figueiredo Bordon K, Amorim F, Anjolette F . Minor snake venom proteins: Structure, function and potential applications. Biochim Biophys Acta Gen Subj. 2016; 1861(4):824-838. DOI: 10.1016/j.bbagen.2016.12.022. View