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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MDPI AG
2018-09-01
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| Series: | Toxins |
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| Online Access: | http://www.mdpi.com/2072-6651/10/9/359 |
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| author | Maria Teresa Romero-Gutiérrez Carlos Eduardo Santibáñez-López Juana María Jiménez-Vargas Cesar Vicente Ferreira Batista Ernesto Ortiz Lourival Domingos Possani |
| author_facet | Maria Teresa Romero-Gutiérrez Carlos Eduardo Santibáñez-López Juana María Jiménez-Vargas Cesar Vicente Ferreira Batista Ernesto Ortiz Lourival Domingos Possani |
| author_sort | Maria Teresa Romero-Gutiérrez |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-04-14T01:21:47Z |
| format | Article |
| id | doaj.art-8af1ec0ce66145ff9961de73fe36bac4 |
| institution | Directory Open Access Journal |
| issn | 2072-6651 |
| language | English |
| last_indexed | 2024-04-14T01:21:47Z |
| publishDate | 2018-09-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Toxins |
| spelling | doaj.art-8af1ec0ce66145ff9961de73fe36bac42022-12-22T02:20:37ZengMDPI AGToxins2072-66512018-09-0110935910.3390/toxins10090359toxins10090359Transcriptomic and Proteomic Analyses Reveal the Diversity of Venom Components from the Vaejovid Scorpion Serradigitus gertschiMaria Teresa Romero-Gutiérrez0Carlos Eduardo Santibáñez-López1Juana María Jiménez-Vargas2Cesar Vicente Ferreira Batista3Ernesto Ortiz4Lourival Domingos Possani5Departamento de Medicina Molecular y Bioprocesos, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Avenida Universidad 2001, Apartado Postal 510-3, Cuernavaca, Morelos 62210, MexicoDepartamento de Medicina Molecular y Bioprocesos, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Avenida Universidad 2001, Apartado Postal 510-3, Cuernavaca, Morelos 62210, MexicoDepartamento de Medicina Molecular y Bioprocesos, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Avenida Universidad 2001, Apartado Postal 510-3, Cuernavaca, Morelos 62210, MexicoLaboratorio Universitario de Proteómica, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Avenida Universidad 2001, Apartado Postal 510-3, Cuernavaca, Morelos 62210, MexicoDepartamento de Medicina Molecular y Bioprocesos, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Avenida Universidad 2001, Apartado Postal 510-3, Cuernavaca, Morelos 62210, MexicoDepartamento de Medicina Molecular y Bioprocesos, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Avenida Universidad 2001, Apartado Postal 510-3, Cuernavaca, Morelos 62210, MexicoTo 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.http://www.mdpi.com/2072-6651/10/9/359proteomeSerradigitus gertschiscorpiontranscriptomevenom |
| spellingShingle | Maria Teresa Romero-Gutiérrez Carlos Eduardo Santibáñez-López Juana María Jiménez-Vargas Cesar Vicente Ferreira Batista Ernesto Ortiz Lourival Domingos Possani Transcriptomic and Proteomic Analyses Reveal the Diversity of Venom Components from the Vaejovid Scorpion Serradigitus gertschi Toxins proteome Serradigitus gertschi scorpion transcriptome venom |
| 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 | proteome Serradigitus gertschi scorpion transcriptome venom |
| url | http://www.mdpi.com/2072-6651/10/9/359 |
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