Proteomic Investigations of Two Pakistani <i>Naja</i> Snake Venoms Species Unravel the Venom Complexity, Posttranslational Modifications, and Presence of Extracellular Vesicles
Latest advancement of omics technologies allows in-depth characterization of venom compositions. In the present work we present a proteomic study of two snake venoms of the genus <i>Naja</i> i.e., <i>Naja naja</i> (black cobra) and <i>Naja oxiana</i> (brown cobra)...
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| Format: | Article |
| Language: | English |
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MDPI AG
2020-10-01
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| Series: | Toxins |
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| Online Access: | https://www.mdpi.com/2072-6651/12/11/669 |
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| author | Aisha Manuwar Benjamin Dreyer Andreas Böhmert Anwar Ullah Zia Mughal Ahmed Akrem Syed Abid Ali Hartmut Schlüter Christian Betzel |
| author_facet | Aisha Manuwar Benjamin Dreyer Andreas Böhmert Anwar Ullah Zia Mughal Ahmed Akrem Syed Abid Ali Hartmut Schlüter Christian Betzel |
| author_sort | Aisha Manuwar |
| collection | DOAJ |
| description | Latest advancement of omics technologies allows in-depth characterization of venom compositions. In the present work we present a proteomic study of two snake venoms of the genus <i>Naja</i> i.e., <i>Naja naja</i> (black cobra) and <i>Naja oxiana</i> (brown cobra) of Pakistani origin. The present study has shown that these snake venoms consist of a highly diversified proteome. Furthermore, the data also revealed variation among closely related species. High throughput mass spectrometric analysis of the venom proteome allowed to identify for the <i>N. naja</i> venom 34 protein families and for the <i>N. oxiana</i> 24 protein families. The comparative evaluation of the two venoms showed that <i>N. naja</i> consists of a more complex venom proteome than <i>N. oxiana</i> venom. Analysis also showed N-terminal acetylation (N-ace) of a few proteins in both venoms. To the best of our knowledge, this is the first study revealing this posttranslational modification in snake venom. N-ace can shed light on the mechanism of regulation of venom proteins inside the venom gland. Furthermore, our data showed the presence of other body proteins, e.g., ankyrin repeats, leucine repeats, zinc finger, cobra serum albumin, transferrin, insulin, deoxyribonuclease-2-alpha, and other regulatory proteins in these venoms. Interestingly, our data identified Ras-GTpase type of proteins, which indicate the presence of extracellular vesicles in the venom. The data can support the production of distinct and specific anti-venoms and also allow a better understanding of the envenomation and mechanism of distribution of toxins. Data are available via ProteomeXchange with identifier PXD018726. |
| first_indexed | 2024-03-10T15:24:16Z |
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| institution | Directory Open Access Journal |
| issn | 2072-6651 |
| language | English |
| last_indexed | 2024-03-10T15:24:16Z |
| publishDate | 2020-10-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Toxins |
| spelling | doaj.art-0ac4039b4c744e6297d89787c097b0822023-11-20T18:10:23ZengMDPI AGToxins2072-66512020-10-01121166910.3390/toxins12110669Proteomic Investigations of Two Pakistani <i>Naja</i> Snake Venoms Species Unravel the Venom Complexity, Posttranslational Modifications, and Presence of Extracellular VesiclesAisha Manuwar0Benjamin Dreyer1Andreas Böhmert2Anwar Ullah3Zia Mughal4Ahmed Akrem5Syed Abid Ali6Hartmut Schlüter7Christian Betzel8Department of Chemistry, University of Engineering and Technology, Lahore 54890, PakistanInstitute of Clinical Chemistry and Laboratory Medicine, Mass Spectrometric Proteomics, University Medical Centre Hamburg-Eppendorf (UKE), Martinistraße 52, 20246 Hamburg, GermanyInstitute of Clinical Chemistry and Laboratory Medicine, Mass Spectrometric Proteomics, University Medical Centre Hamburg-Eppendorf (UKE), Martinistraße 52, 20246 Hamburg, GermanyDepartment of Biosciences, COMSATS University Islamabad, Park Road, Chack Shahzad, Islamabad 45550, PakistanPet Centre, University of Veterinary and Animal Sciences, Lahore 54890, PakistanBotany Division, Institute of Pure and Applied Biology, Bahauddin Zakariya University, Multan 60800, PakistanHusein Ebrahim Jamal Research Institute of Chemistry, (International Center for Chemical and Biological Sciences), University of Karachi, Karachi 75270, PakistanInstitute of Clinical Chemistry and Laboratory Medicine, Mass Spectrometric Proteomics, University Medical Centre Hamburg-Eppendorf (UKE), Martinistraße 52, 20246 Hamburg, GermanyLaboratory for Structural Biology of Infection and Inflammation, Institute of Biochemistry and Molecular Biology, Deutsches Elektronen-Synchrotron, Build. 22a, Notkestr. 85, University of Hamburg, 22603 Hamburg, GermanyLatest advancement of omics technologies allows in-depth characterization of venom compositions. In the present work we present a proteomic study of two snake venoms of the genus <i>Naja</i> i.e., <i>Naja naja</i> (black cobra) and <i>Naja oxiana</i> (brown cobra) of Pakistani origin. The present study has shown that these snake venoms consist of a highly diversified proteome. Furthermore, the data also revealed variation among closely related species. High throughput mass spectrometric analysis of the venom proteome allowed to identify for the <i>N. naja</i> venom 34 protein families and for the <i>N. oxiana</i> 24 protein families. The comparative evaluation of the two venoms showed that <i>N. naja</i> consists of a more complex venom proteome than <i>N. oxiana</i> venom. Analysis also showed N-terminal acetylation (N-ace) of a few proteins in both venoms. To the best of our knowledge, this is the first study revealing this posttranslational modification in snake venom. N-ace can shed light on the mechanism of regulation of venom proteins inside the venom gland. Furthermore, our data showed the presence of other body proteins, e.g., ankyrin repeats, leucine repeats, zinc finger, cobra serum albumin, transferrin, insulin, deoxyribonuclease-2-alpha, and other regulatory proteins in these venoms. Interestingly, our data identified Ras-GTpase type of proteins, which indicate the presence of extracellular vesicles in the venom. The data can support the production of distinct and specific anti-venoms and also allow a better understanding of the envenomation and mechanism of distribution of toxins. Data are available via ProteomeXchange with identifier PXD018726.https://www.mdpi.com/2072-6651/12/11/669<i>Naja naja</i><i>Naja oxiana</i>venom proteomeRas-GTPaseankyrin repeatN-terminal acetylation |
| spellingShingle | Aisha Manuwar Benjamin Dreyer Andreas Böhmert Anwar Ullah Zia Mughal Ahmed Akrem Syed Abid Ali Hartmut Schlüter Christian Betzel Proteomic Investigations of Two Pakistani <i>Naja</i> Snake Venoms Species Unravel the Venom Complexity, Posttranslational Modifications, and Presence of Extracellular Vesicles Toxins <i>Naja naja</i> <i>Naja oxiana</i> venom proteome Ras-GTPase ankyrin repeat N-terminal acetylation |
| title | Proteomic Investigations of Two Pakistani <i>Naja</i> Snake Venoms Species Unravel the Venom Complexity, Posttranslational Modifications, and Presence of Extracellular Vesicles |
| title_full | Proteomic Investigations of Two Pakistani <i>Naja</i> Snake Venoms Species Unravel the Venom Complexity, Posttranslational Modifications, and Presence of Extracellular Vesicles |
| title_fullStr | Proteomic Investigations of Two Pakistani <i>Naja</i> Snake Venoms Species Unravel the Venom Complexity, Posttranslational Modifications, and Presence of Extracellular Vesicles |
| title_full_unstemmed | Proteomic Investigations of Two Pakistani <i>Naja</i> Snake Venoms Species Unravel the Venom Complexity, Posttranslational Modifications, and Presence of Extracellular Vesicles |
| title_short | Proteomic Investigations of Two Pakistani <i>Naja</i> Snake Venoms Species Unravel the Venom Complexity, Posttranslational Modifications, and Presence of Extracellular Vesicles |
| title_sort | proteomic investigations of two pakistani i naja i snake venoms species unravel the venom complexity posttranslational modifications and presence of extracellular vesicles |
| topic | <i>Naja naja</i> <i>Naja oxiana</i> venom proteome Ras-GTPase ankyrin repeat N-terminal acetylation |
| url | https://www.mdpi.com/2072-6651/12/11/669 |
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