Investigating Camel Superoxide Dismutase 1: A Computational Analysis of Potential Key Player in Heat Stress Adaptation

Investigating camel superoxide dismutase 1

Keywords: camel, Camelus bactrianus, Camelus dromedarius, Camelus ferus, heat tolerance, In-silico, stress

Abstract

Abstract Views: 0

Background. Superoxide dismutase 1 (SOD1) is crucial for cellular defense against oxidative stress induced by superoxide radicals, particularly in challenging conditions, such as elevated temperature and humidity. This study investigated SOD1 in Bactrian camel (Camelus bactrianus), Wild Bactrian camel (C. ferus), and Arabian camel (C. dromedarius) to understand its role in heat tolerance.

Methodology. The current study employed bioinformatics analysis to assess the genomic features including GC% content. It also investigated the structure and location of the SOD1 gene on the chromosomes. Phylogenetic analysis was conducted to elucidate the evolutionary relationships based on SOD1 protein sequences. Structural analyses encompassed secondary and tertiary structure predictions, emphasizing stability and potential functional implications. Subcellular localization of the SOD1 protein was also explored.

Results. C. dromedarius displayed the highest GC% in its genome, indicating improved thermostability. With the exception of C. bactrianus whose chromosomal location was unknown, all other species contained SOD1 gene on their first chromosome. Based upon SOD1 protein sequences, phylogenetic investigation emphasized the close evolutionary link within the Camelidae family. Structurally, all three species of camel shared an acidic, globular, and thermally-stable SOD1 protein having high glycine content and lack of cleavage sites. Analysis of secondary structure indicated a frequency of random coils, highlighting the adaptability and evolutionary conservation of protein. Predictions of tertiary structure verified that SOD1 was stable in all species. The protein is predominantly found in cytoplasm although, also present in nucleus, extracellular region, and mitochondria.

Conclusion. This inclusive analysis of SOD1 in three different species of camel highlighted their strong adaptation to desert environment by elucidating their genomic and proteomic stability. Further research is necessary to investigate the biochemical mechanisms behind camels’ extraordinary ability to thrive in desert conditions and respond to the challenges posed by climate change.

Downloads

Download data is not yet available.

References

Rauf A, Khalil AA, Awadallah S, et al. Reactive oxygen species in biological systems: Pathways, associated diseases, and potential inhibitors—a review. Food Sci Nutr. 2024;12(2):675–693. https://doi.org/10.1002/fsn3.3784

Jena AB, Samal RR, Bhol NK, Duttaroy AK. Cellular Red-Ox system in health and disease: the latest update. Biomed Pharmacother. 2023;162:e114606. https://doi.org/10.1016/j.biopha.2023.114606

Jomova K, Alomar SY, Alwasel SH, Nepovimova E, Kuca K, Valko M. Several lines of antioxidant defense against oxidative stress: antioxidant enzymes, nanomaterials with multiple enzyme-mimicking activities, and low-molecular-weight antioxidants. Arch Toxicol. 2024;98(5):1323–1367. https://doi.org/10.1007/s00204-024-03696-4

Li X, Qiu S, Shi J, et al. A new function of copper zinc superoxide dismutase: as a regulatory DNA-binding protein in gene expression in response to intracellular hydrogen peroxide. Nucleic Acids Res. 2019;47(10):5074–5085. https://doi.org/10.1093/nar/gkz256

Chafik A, Essamadi A, Çelik SY, Mavi A. Purification and biochemical characterization of a novel copper, zinc superoxide dismutase from liver of camel (Camelus dromedarius): an antioxidant enzyme with unique properties. Bioorg Chem. 2019;86:428–436. https://doi.org/10.1016/j.bioorg.2019.02.024

Oselu S, Ebere R, Arimi JM. Camels, Camel milk, and Camel milk product situation in kenya in relation to the world. Int J Food Sci. 2022;2022. https://doi.org/10.1155/2022/1237423

Zakir S, Adem F, Tafese W. Review on composition , nutritive and therapeutic value of camel milk. Int J Innov Sci Res Technol. 2021;6(12):227–233.

Adah A, Ayo J, Adah D. Unique physiological and behavioural adaptive features of the one-humped Camel (Camelus dromedarius) to arid environments. J Appl Vet Sci. 2022;8(1):57–64.

Padalino B, Menchetti L. The first protocol for assessing the welfare of dromedary camels (Camelus dromedarius) kept under nomadic pastoralism. Front Vet Sci. 2024;11:e1416714. https://doi.org/10.3389/fvets.2024.1416714

Demirci-Çekiç S, Özkan G, Avan AN, Uzunboy S, Çapanoğlu E, Apak R. Biomarkers of oxidative stress and antioxidant defense. J Pharm Biomed Anal. 2022;209:e114477.

Khan ZA, Mishra C, Jyotiranjan T. In silico analysis of caprine superoxide dismutase 1 (SOD1) gene. Genomics. 2020;112(1):212–217. https://doi.org/10.1016/j.ygeno.2019.01.016

Bateman A, Martin MJ, Orchard S, et al. UniProt: the universal protein knowledgebase in 2021. Nucleic Acids Res. 2021;49(D1):D480–D489.

Garg VK, Avashthi H, Tiwari A, et al. MFPPI – multi FASTA protparam Interface. Bioinformation. 2016;12(2):74–77. https://doi.org/10.6026/97320630012074

Emanuelsson O, Brunak S, von Heijne G, Nielsen H. Locating proteins in the cell using TargetP, SignalP and related tools. Nat Protoc. 2007;2(4):953–971. https://doi.org/10.1038/nprot.2007.131

Geourjon C, Deléage G. Sopma: significant improvements in protein secondary structure prediction by consensus prediction from multiple alignments. Bioinformatics. 1995;11(6):681–684.

Burley SK, Bhikadiya C, Bi C, et al. Protein data bank: celebrating 50 years of the PDB with new tools for understanding and visualizing biological macromolecules in 3D. Protein Sci. 2022;31(1):187–208. https://doi.org/10.1002/pro.4213

Robin X, Waterhouse AM, Bienert S, et al. The SWISS-MODEL repository of 3D protein structures and models. In: Daina A, Przewosny M, Zoete V, eds. Open Access Databases and Datasets for Drug Discovery. Wiley Publishers; 2024:175–99.

Abramson J, Adler J, Dunger J, et al. Accurate structure prediction of biomolecular interactions with AlphaFold 3. Nature. 2024;630(8016):493–500. https://doi.org/10.1038/s41586-024-07487-w

Powell HR, Islam SA, David A, Sternberg MJE. Phyre2.2: a community resource for template-based protein structure prediction. J Mol Biol. 2025;e168960. https://doi.org/10.1016/j.jmb.2025.168960

Yu CS, Cheng CW, Su WC, et al. CELLO2GO: a web server for protein subCELlular lOcalization prediction with functional gene ontology annotation. PLoS One. 2014;9(6):e99368. https://doi.org/10.1371/journal.pone.0099368

Raza SHA, Hassanin AA, Dhshan AIM, et al. In silico genomic and proteomic analyses of three heat shock proteins (HSP70, HSP90-α, and HSP90-β) in even-toed ungulates. Electron J Biotechnol. 2021;53:61–70. https://doi.org/10.1016/j.ejbt.2021.07.002

Chen H, Skylaris CK. Analysis of DNA interactions and GC content with energy decomposition in large-scale quantum mechanical calculations. Phys Chem Chem Phys. 2021;23(14):8891–8899. https://doi.org/10.1039/D0CP06630C

Kebir NE, Berber N, Zahzeh MR. Anatomical and physiological properties of the dromedary: a potential sustainability alternative and a vital asset in the era of climate change. J Anim Behav Biometeorol. 2024;12(4):e2024031. https://doi.org/10.31893/jabb.2024031

Bornstein S. Evolution, distribution, and economic importance of the Camels. In: Khalafalla AI, Hussein MF, eds. Infectious Diseases of Dromedary Camels: A Concise Guide. Springer International Publishing; 2021:1–19.

Qing R, Hao S, Smorodina E, Jin D, Zalevsky A, Zhang S. Protein design: from the aspect of water solubility and stability. Chem Rev. 2022;122(18):14085–14179.

Gamage DG, Gunaratne A, Periyannan GR, Russell TG. Applicability of instability index for in vitro protein stability prediction. Protein Pept Lett. 2019;26(5):339–347. https://doi.org/10.2174/0929866526666190228144219

Flores-Castañón N, Sarkar S, Banerjee A. Structural, functional, and molecular docking analyses of microbial cutinase enzymes against polyurethane monomers. J Hazard Mater Lett. 2022;3:e100063. https://doi.org/10.1016/j.hazl.2022.100063

Grossmann L, McClements DJ. Current insights into protein solubility: a review of its importance for alternative proteins. Food Hydrocoll. 2023;137:e108416. https://doi.org/10.1016/j.foodhyd.2022.108416

Kovács D, Bodor A. The influence of random-coil chemical shifts on the assessment of structural propensities in folded proteins and IDPs. RSC Adv. 2023;13(15):10182–10203. https://doi.org/10.1039/D3RA00977G

Guan T, Guo Y, Zhou T, et al. Oxidized SOD1 accelerates cellular senescence in neural stem cells. Stem Cell Res Ther. 2024;15(1):e55. https://doi.org/10.1186/s13287-024-03669-5

Martinelli I, Zucchi E, Simonini C, et al. The landscape of cognitive impairment in superoxide dismutase 1-amyotrophic lateral sclerosis. Neural Regen Res. 2023;18(7):1427–1433. https://doi.org/10.4103/1673-5374.361535

Published
2025-05-02
How to Cite
Yousaf, M. A., & Khan, M. A. (2025). Investigating Camel Superoxide Dismutase 1: A Computational Analysis of Potential Key Player in Heat Stress Adaptation. BioScientific Review, 7(1), 106-123. https://doi.org/10.32350/bsr.71.07
Section
Research Articles