Prediction of Quaternary Protein Structure of HSP90AA1 Gene in Three Nigerian Indigenous Breeds of Sheep

De Campos, J.S., Olatunji, O.I., Okunlola, M.A., Oliyide, O.M., Bajomo, E.T., *Aremu, J.O*., Bello, T.S., Adegoke, S.J., Kujero, G.O., Onasanya, G.O., Adeleye, A.A., Olusoji, B. I.,Popoola, A.A., Badmus, M.O., Ajayi, B.J., Abatti, O.S., Adeneye, I.B., Amoo, S.T., Dairo, C.O., Ikeobi, C.O.N.

Prediction of Quaternary Protein Structure of HSP90AA1 Gene in Three Nigerian Indigenous Breeds of Sheep

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De Campos NJAST 2026.pdf(410.96 KB)

Date

2026-09-07

Authors

De Campos, J.S., Olatunji, O.I., Okunlola, M.A., Oliyide, O.M., Bajomo, E.T., *Aremu, J.O*., Bello, T.S., Adegoke, S.J., Kujero, G.O., Onasanya, G.O., Adeleye, A.A., Olusoji, B. I.,Popoola, A.A., Badmus, M.O., Ajayi, B.J., Abatti, O.S., Adeneye, I.B., Amoo, S.T., Dairo, C.O., Ikeobi, C.O.N.

Publisher

Nigerian Journal of Animal Science and Technology (NJAST),Department of Animal Science, University of Maiduguri, Borno State, Nigeria.

Abstract

This study aimed to predict and compare the quaternary structure and functions of the HSP90AA1 protein in three indigenous sheep breeds in Nigeria: West African Dwarf (WAD), Yankasa, and Uda. Fifteen healthy adult sheep, comprising five animals per breed, were randomly selected for the study. 2 mls of blood was collected from each animal via jugular vein and preserved on FTA cards for genomic DNA extraction. The HSP90AA1 gene was amplified using two primer sets targeting the 5′ flanking region (300 bp) and intron 10 (700 bp), followed by bidirectional Sanger sequencing. A total of thirty (30) sequence reads were generated, quality-checked using Phred scores (≥30), and aligned using BioEdit software to produce consensus sequences for each breed. The nucleotide sequences were translated into amino acid sequences and analysed using ExPASy. ProtParam software was used for detecting the physicochemical properties and SOPMA software was used for secondary structure prediction. Quaternary structures were predicted using AlphaFold2 Multimer software and visualised using Mol* Viewer. Results revealed clear breedspecific variation in amino acid length, with WAD, Yankasa, and Uda having 1540, 1680, and 1890 amino acids, respectively. Physicochemical analysis showed that the Uda breed exhibited a lower instability index (31.25) and higher aliphatic index (40.68), indicating greater structural stability and thermo-tolerance compared to WAD and Yankasa. All predicted proteins were slightly acidic and hydrophilic. Quaternary structure prediction confirmed a conserved homodimeric organisation across all breeds; however, structural differences were observed, with WAD and Yankasa displaying compact V-shaped conformations, while Uda exhibited a more elongated open-state structure. The study demonstrates that breed-specific variations in the HSP90AA1 gene result in distinct structural and functional differences in the protein, which may contribute to environmental adaptabilities of the Nigerian indigenous sheep. The findings highlight the potential of HSP90AA1 as a molecular marker for breeding heat-resilient sheep and underscores the importance of computational approaches in livestock genetic improvement.

Citation

https://www.njast.com.ng/?utm_source=chatgpt.com

URI

https://kwasuspace.kwasu.edu.ng/handle/123456789/7619

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