Ranjit Shaw¹, Zishan Ansari² and Radha Chaube³*

¹Department of Biosciences and Bioengineering, IIT Bombay, Powai, Mumbai, Maharashtra, India
²Department of Biotechnology, School of Studies of Interdisciplinary Education and Research, Guru Ghasidas Vishwavidyalaya (A Central University), Koni, Bilaspur, (C.G.), India
³Department of Zoology, Institute of Science Banaras, Hindu University, Varanasi, Uttar Pradesh, India

*Corresponding Author: Radha Chaube, Department of Zoology, Institute of Science, Banaras Hindu University, Varanasi, Uttar Pradesh, India.

Received: September 04, 2024; Published: September 30, 2024

Abstract

The stinging catfish (Heteropneustes fossilis) is an important aquaculture species, which plays a pivotal role in the global fishing industry due to its rapid growth rates and high nutritional value. It is an excellent model for genomic studies due to high levels of biological conservation and fecundity rate. Follicle-stimulating hormone (FSH) is a key regulator of reproductive processes in vertebrates, including catfish. It stimulates the growth and maturation of ovarian follicles in females and spermatogenesis in males. Despite its significance, its three-dimensional (3-D) structure is not found in the Protein Data Bank. To bridge this gap, we retrieved the protein sequence of the β-subunit of the FSH of H. fossilis from NCBI. The preliminary 3-D structure was generated by automated homology modeling using SWISS MODEL. This model was further refined through energy minimization using KoBaMIN. The Ramachandran plots were obtained from the RAMPAGE server. The sequences from three other model organisms, Mus musculus, Columba livia, and Homo sapiens, retrieved from NCBI, were used for a comparative physicochemical characterization using ProtParam. The functional regions were predicted using the Vector Alignment Search Tool. Finally, Hydrophobic Cluster Analysis was conducted to assess hydrophobicity patterns within the structure. A first attempt to model the 3-D structure of FSH of H. fossilis reveals that it consists of a single peptide chain and two pairs of anti-parallel β-sheets and loops. Our research has practical applications in developing targeted breeding programs and hormonal therapies to enhance reproductive efficiency in catfish aquaculture.

 Keywords: Heteropneustes Fossilis; Follicle-Stimulating Hormone; Protein Data Bank; Homology Modelling; Catfish Aquaculture

References

1. Sonawani S Niazi and SI Thomas. “In Silico Study on Binding Specificity of Gonadotropins and Their Receptors: Design of a Novel and Selective Peptidomimetic for Human Follicle Stimulating Hormone Receptor”. J PLOS ONE 8 (2013): 1-14.
2. Kumar P., et al. “Current knowledge on the biology, captive breeding and aquaculture of the brackishwater catfish, Mystus gulio (Hamilton, 1822): A review”. Aquaculture 499 (2019): 243-250.
3. J Aizen., et al. “Experimental and computational study of inter and intra- species specificity of gonadotropins for various receptor”. Molecular and cellular Endocrinology 36 (2012): 89-100.
4. Adelakun KM., et al. “Seasonal variation in nutritional quality of Catfish (Clarias gariepinus) from Upper Jebba Basin, Nigeria”. Journal of Nutrition and Food Science 7 (2017): 5-9.
5. H Ashkenazy., et al. “ConSurf 2010: Calculating evolutionary conservation in sequence and structure of proteins and nucleic acids”. Nucleic Acids Research 38 (2010): 529-533.
6. Adan RIY. “Catfish culture in Southeast Asia”. SEAFDEC Asian Aquaculture1 (2000): 16-17.
7. Dunham RA and Elaswad A. “Catfish biology and farming”. Annual Review of Animal Biosciences1 (2018): 305-325.
8. J Bogerd., et al. “Fish FSH receptor bind LH: How to make human FSH receptor to be fishier?” Science direct”. General and Comparative Endocrinology 142 (2005): 34-43.
9. J Bogerd. “Ligand -selective determinants in gonadotropins receptors”. Molecular and Cellular Endocrinology 260-262 (2007): 144-152.
10. Foulkes NS., et al. “Pituitary hormone FSH directs the CREM functional switch during spermatogenesis”. Nature6417 (1993): 264-267.
11. JK Sundaray., et al. “Simple sequence repeats (SSRs) markers in fish genomic research and their acceleration via next-generation sequencing and computational approaches”. Aquaculture International 4 (2016): 1089-1102.
12. J Peute., et al. “Ultrastructure and immunolabelling of gonadotrops and thyrotrops in the pituitary of the African catfish Clariaslazera”. Cell Tissue Res238 (1984): 95-103.
13. Xie and PE Bourne. “Structure-based systems biology for analyzing off-target binding”. Science Direct 21 (2011): 189-199.
14. MH Abel., et al. “The effect of null mutation in the Follicle Stimulating Hormone gene on Mouse Reproduction”. Endocrinology5 (2000): 1795-1803.
15. N Bhogireddy., et al. “Inferences from the ADMET analysis of predicted inhibitors to Follicle Stimulating Hormone in the context of infertility”. Journal Biomedical Informatics15 (2013): 788-791.
16. Lambalk CB and De Koning CH. “Interpretation of elevated FSH in the regular menstrual cycle”. Maturitas2 (1998): 215-220.
17. R Shenoy., et al. “Proteins: Sequence to Structure and Function, Current status”. Current Protein and Peptide Science 11 (2010): 498-514.
18. Casarini L and Crépieux P. “Molecular mechanisms of action of FSH”. Frontiers in endocrinology 10 (2019):
19. TR Kumar., et al. “Transgenic Models to Study Gonadotropin Function: The Role of Follicle-Stimulating Hormone in Gonadal Growth and Tumorigenesis”. Molecular Endocrinology6 (1999): 851-865.
20. W Xing and MR Sairam. “Role of CACC-Box in the Regulation of ovine Follicle Stimulating Hormone Receptor Expression”. Biology of Reproductively 65 (2001): 1142-1149.
21. Saha S., et al. “Behavioral and physiological toxicity thresholds of a freshwater vertebrate (Heteropneustes fossilis) and invertebrate (Branchiura sowerbyi), exposed to zinc oxide nanoparticles (nZnO): A General Unified Threshold model of Survival (GUTS)”. Comparative Biochemistry and Physiology Part C: Toxicology and Pharmacology 262 (2022):
22. Reddy PB. “Study on the toxic effects of wastewater in catfish (Heteropneustes fossilis)”. Life Sciences International Research Journal2 (2018): 165-174.
23. Paital B. “Antioxidant and oxidative stress parameters in brain of Heteropneustes fossilis under air exposure condition; role of mitochondrial electron transport chain”. Ecotoxicology and Environmental Safety95 (2013): 69-77.
24. XY Wu., et al. “Early Bone mineral density decrease is associated with FSH AND LH, not estrogens”. Clinica Chimica Acta 415 (2013): 69-73.
25. Z Liu. “A review of catfish genomics: Progress and Perspective”. Wiley Inter Science 4 (2003): 259-265.
26. Z Yang., et al. “UCSF Chimera, Modeller and IMP: An integrated modeling system”. Journal of Structural Biology 179 (2011): 269-278.
27. S Ramachandran., et al. “Automated minimization of steric clashes in protein structure”. Protein: Structure, Function, and Bioinformatics 79 (2010): 261-270.
28. Lovell SC., et al. “Structure validation by Calpha geometry: phi, psi and Cbeta deviation”. Proteins: Structure, Function and Genetics 50 (2002): 437-450.
29. Gaboriaud V., et al. “Hydrophobic cluster analysis, an efficient new way to compare and analyse amino acid sequence”. FEBS Letters1 (1987): 149-155.
30. FR Qing and HA Wayne. “Structure of Human Follicle Stimulating Hormone in complex with its receptor”. Nature 433 (2005): 269-277.
31. Lisachov A., et al. “Emerging importance of bighead catfish (Clarias macrocephalus) and north African catfish (C. gariepinus) as a bioresource and their genomic perspective”. Aquaculture 573 (2023): 739585.
32. Jin Y., et al. “Catfish genomic studies: progress and perspectives”. Genomics in Aquaculture (2016): 73-104.
33. Soudy M., et al. “UniprotR: Retrieving and visualizing protein sequence and functional information from Universal Protein Resource (UniProt knowledgebase)”. Journal of Proteomics213 (2020):
34. Schwede T., et al. “SWISS-MODEL: an automated protein homology-modeling server”. Nucleic Acids Research13 (2003): 3381-3385.
35. Terp GE., et al. “Structural differences of matrix metalloproteinases. Homology modeling and energy minimization of enzyme-substrate complexes”. Journal of Biomolecular Structure and Dynamics6 (2000): 933-946.
36. Santhoshkumar R and Yusuf A. “In silico structural modeling and analysis of physicochemical properties of curcumin synthase (CURS1, CURS2, and CURS3) proteins of Curcuma longa”. Journal of Genetic Engineering and Biotechnology1 (2020): 24.
37. Zhu J and Weng Z. “FAST: a novel protein structure alignment algorithm”. PROTEINS: Structure, Function, and Bioinformatics3 (2005): 618-627.
38. Glaser F., et al. “ConSurf: identification of functional regions in proteins by surface-mapping of phylogenetic information”. Bioinformatics1 (2003): 163-164.
39. Woodcock S., et al. “Detection of secondary structure elements in proteins by hydrophobic cluster analysis”. Protein Engineering, Design and Selection7 (1992): 629-635.
40. Whittig LD and Allardice WR. “X‐ray diffraction techniques”. Methods of Soil Analysis: Part 1 Physical and Mineralogical Methods 5 (1986): 331-362.

Citation

Citation: Radha Chaube., et al. “Computational Three-Dimensional Modelling of the β-Subunit of Follicle-Stimulating Hormone in Stinging Catfish (Heteropneustes Fossilis)". Acta Scientific Veterinary Sciences 6.10 (2024): 52-61.

Copyright

Copyright: © 2024 Radha Chaube., et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.