Computational Modeling of Low-Abundance Proteins in Venom Gland Transcriptomes: Bothrops asper and Bothrops jararaca

Snake venoms contain numerous toxic proteins, but low-abundance proteins often remain uncharacterized due to identification challenges. This study employs a bioinformatics approach to identify and structurally model low-abundance proteins from the venom gland transcriptomes of <i>Bothrops asper</i> and <i>Bothrops jararaca</i>. Using tools such as tblastn, Jalview, and CHIMERA, we analyzed sequences and structural features of proteins including arylsulfatase, CRISP (Cysteine-Rich Secretory Protein), von Willebrand factor type D (vWFD), and dihydroorotate dehydrogenase (DHODH), and identified potential new isoforms of SVMP-PIIIb (Ba_1) and botrocetin in <i>B. asper</i>. Protein models were generated with AlphaFold2, compared with crystallized structures from the Protein Data Bank (PDB), and validated using Procheck, ERRAT, and Verify3D. Conserved motifs and domains were annotated through Pfam and InterPro, revealing structural elements that suggest possible roles in venom physiology and toxicity. These findings emphasize the potential of computational biology to characterize structurally relevant but experimentally inaccessible venom proteins, and to lay the groundwork for future functional validation.

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Publication Details

Journal
Toxins
Published
2025-05-22
DOI
https://doi.org/10.3390/toxins17060262
Citations
1
Primary Topic
Venomous Animal Envenomation and Studies
Type
article
Field-Weighted Citation Impact
1.82

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article

Computational Modeling of Low-Abundance Proteins in Venom Gland Transcriptomes: Bothrops asper and Bothrops jararaca

Doris Vela, Joseph Espín-Angulo
1 citations
Toxins
Venomous Animal Envenomation and Studies
1.82
article

Computational Modeling of Low-Abundance Proteins in Venom Gland Transcriptomes: Bothrops asper and Bothrops jararaca

Doris Vela, Joseph Espín-Angulo
article en
1 citations

Abstract

Snake venoms contain numerous toxic proteins, but low-abundance proteins often remain uncharacterized due to identification challenges. This study employs a bioinformatics approach to identify and structurally model low-abundance proteins from the venom gland transcriptomes of <i>Bothrops asper</i> and <i>Bothrops jararaca</i>. Using tools such as tblastn, Jalview, and CHIMERA, we analyzed sequences and structural features of proteins including arylsulfatase, CRISP (Cysteine-Rich Secretory Protein), von Willebrand factor type D (vWFD), and dihydroorotate dehydrogenase (DHODH), and identified potential new isoforms of SVMP-PIIIb (Ba_1) and botrocetin in <i>B. asper</i>. Protein models were generated with AlphaFold2, compared with crystallized structures from the Protein Data Bank (PDB), and validated using Procheck, ERRAT, and Verify3D. Conserved motifs and domains were annotated through Pfam and InterPro, revealing structural elements that suggest possible roles in venom physiology and toxicity. These findings emphasize the potential of computational biology to characterize structurally relevant but experimentally inaccessible venom proteins, and to lay the groundwork for future functional validation.

ToxinsVol. 17(6)
Pontificia Universidad Católica del Ecuador (EC)
Pontificia Universidad Católica del Ecuador
Life in Land
Openalex Percentile: Top 16%
Venomous Animal Envenomation and Studies
1.82
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