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Transcriptomic and Proteomic Analyses Reveal the Diversity of Venom Components from the Vaejovid Scorpion Serradigitus gertschi

To understand the diversity of scorpion venom, RNA from venomous glands from a sawfinger scorpion, Serradigitus gertschi, of the family Vaejovidae, was extracted and used for transcriptomic analysis. A total of 84,835 transcripts were assembled after Illumina sequencing. From those, 119 transcripts...

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Autores principales: Romero-Gutiérrez, Maria Teresa, Santibáñez-López, Carlos Eduardo, Jiménez-Vargas, Juana María, Batista, Cesar Vicente Ferreira, Ortiz, Ernesto, Possani, Lourival Domingos
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6162517/
https://www.ncbi.nlm.nih.gov/pubmed/30189638
http://dx.doi.org/10.3390/toxins10090359
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author Romero-Gutiérrez, Maria Teresa
Santibáñez-López, Carlos Eduardo
Jiménez-Vargas, Juana María
Batista, Cesar Vicente Ferreira
Ortiz, Ernesto
Possani, Lourival Domingos
author_facet Romero-Gutiérrez, Maria Teresa
Santibáñez-López, Carlos Eduardo
Jiménez-Vargas, Juana María
Batista, Cesar Vicente Ferreira
Ortiz, Ernesto
Possani, Lourival Domingos
author_sort Romero-Gutiérrez, Maria Teresa
collection PubMed
description To understand the diversity of scorpion venom, RNA from venomous glands from a sawfinger scorpion, Serradigitus gertschi, of the family Vaejovidae, was extracted and used for transcriptomic analysis. A total of 84,835 transcripts were assembled after Illumina sequencing. From those, 119 transcripts were annotated and found to putatively code for peptides or proteins that share sequence similarities with the previously reported venom components of other species. In accordance with sequence similarity, the transcripts were classified as potentially coding for 37 ion channel toxins; 17 host defense peptides; 28 enzymes, including phospholipases, hyaluronidases, metalloproteases, and serine proteases; nine protease inhibitor-like peptides; 10 peptides of the cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 protein superfamily; seven La1-like peptides; and 11 sequences classified as “other venom components”. A mass fingerprint performed by mass spectrometry identified 204 components with molecular masses varying from 444.26 Da to 12,432.80 Da, plus several higher molecular weight proteins whose precise masses were not determined. The LC-MS/MS analysis of a tryptic digestion of the soluble venom resulted in the de novo determination of 16,840 peptide sequences, 24 of which matched sequences predicted from the translated transcriptome. The database presented here increases our general knowledge of the biodiversity of venom components from neglected non-buthid scorpions.
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spelling pubmed-61625172018-10-03 Transcriptomic and Proteomic Analyses Reveal the Diversity of Venom Components from the Vaejovid Scorpion Serradigitus gertschi Romero-Gutiérrez, Maria Teresa Santibáñez-López, Carlos Eduardo Jiménez-Vargas, Juana María Batista, Cesar Vicente Ferreira Ortiz, Ernesto Possani, Lourival Domingos Toxins (Basel) Article To understand the diversity of scorpion venom, RNA from venomous glands from a sawfinger scorpion, Serradigitus gertschi, of the family Vaejovidae, was extracted and used for transcriptomic analysis. A total of 84,835 transcripts were assembled after Illumina sequencing. From those, 119 transcripts were annotated and found to putatively code for peptides or proteins that share sequence similarities with the previously reported venom components of other species. In accordance with sequence similarity, the transcripts were classified as potentially coding for 37 ion channel toxins; 17 host defense peptides; 28 enzymes, including phospholipases, hyaluronidases, metalloproteases, and serine proteases; nine protease inhibitor-like peptides; 10 peptides of the cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 protein superfamily; seven La1-like peptides; and 11 sequences classified as “other venom components”. A mass fingerprint performed by mass spectrometry identified 204 components with molecular masses varying from 444.26 Da to 12,432.80 Da, plus several higher molecular weight proteins whose precise masses were not determined. The LC-MS/MS analysis of a tryptic digestion of the soluble venom resulted in the de novo determination of 16,840 peptide sequences, 24 of which matched sequences predicted from the translated transcriptome. The database presented here increases our general knowledge of the biodiversity of venom components from neglected non-buthid scorpions. MDPI 2018-09-05 /pmc/articles/PMC6162517/ /pubmed/30189638 http://dx.doi.org/10.3390/toxins10090359 Text en © 2018 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Romero-Gutiérrez, Maria Teresa
Santibáñez-López, Carlos Eduardo
Jiménez-Vargas, Juana María
Batista, Cesar Vicente Ferreira
Ortiz, Ernesto
Possani, Lourival Domingos
Transcriptomic and Proteomic Analyses Reveal the Diversity of Venom Components from the Vaejovid Scorpion Serradigitus gertschi
title Transcriptomic and Proteomic Analyses Reveal the Diversity of Venom Components from the Vaejovid Scorpion Serradigitus gertschi
title_full Transcriptomic and Proteomic Analyses Reveal the Diversity of Venom Components from the Vaejovid Scorpion Serradigitus gertschi
title_fullStr Transcriptomic and Proteomic Analyses Reveal the Diversity of Venom Components from the Vaejovid Scorpion Serradigitus gertschi
title_full_unstemmed Transcriptomic and Proteomic Analyses Reveal the Diversity of Venom Components from the Vaejovid Scorpion Serradigitus gertschi
title_short Transcriptomic and Proteomic Analyses Reveal the Diversity of Venom Components from the Vaejovid Scorpion Serradigitus gertschi
title_sort transcriptomic and proteomic analyses reveal the diversity of venom components from the vaejovid scorpion serradigitus gertschi
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6162517/
https://www.ncbi.nlm.nih.gov/pubmed/30189638
http://dx.doi.org/10.3390/toxins10090359
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