Network and structural analysis of quail mucins with expression pattern of mucin 1 and mucin 4 in the intestines of the Iraqi common quail (Coturnix coturnix)

Author:

Almhanna Hazem1ORCID,AL-Mahmodi Aqeel Mohsin Mahdi2ORCID,Kadhim Abdulrazzaq B1ORCID,Kumar Arun H. S.3ORCID

Affiliation:

1. Department of Anatomy and Histology, College of Veterinary Medicine, University of Al-Qadisiyah, Al Diwaniyah, Iraq.

2. Department of Anatomy, Histology and Embryology, Faculty of Veterinary Medicine, University of Kufa, Kufa, Iraq.

3. Department of Veterinary Biosciences, Stemcology, School of Veterinary Medicine, University College Dublin, Belfield, Dublin, Ireland.

Abstract

Background and Aim: In avian and other species, mucins (MUCs) play a crucial role in the gastrointestinal tract (GIT), and constitute a large group of O-glycosylated glycoproteins, are glycoconjugate proteins. MUCs present in two forms: (1) membrane-attached on cell surfaces to repel external threats and (2) detachable, gel-forming proteins in the soluble form. In quail GIT, the specific types of MUCs that are expressed remain largely unknown. We investigated the expression of MUC1 and MUC4 MUCs in the GIT of Iraqi common quails and conducted network and structural analyses of all known MUC types across quail breeds. Materials and Methods: Histological and gene expression analyses of MUC1 and MUC4 were conducted using fresh small intestine and large intestine samples from 10 quails. Using the STRING Database, Chimera software, and PrankWeb-ligand binding site prediction tool, network and structural analyses of all reported types of quail MUCs were conducted. Results: Most intestinal MUCs in quails were acidic, with few neutral MUCs detectable through Alcian blue and periodic acid-schiff stains. Acidic MUCs were more expressed in the duodenum, ileum, cecum, and colon, whereas neutral MUCs were more expressed in the jejunum. MUC1 and MUC4 messenger RNA expression was significantly higher in the jejunum and colon than in the duodenum and ileum. The analysis of the network revealed that MUC 1, 15, 16, and 24 formed homologous networks, while MUC 2, 4, 5, and 6 formed heterologous networks. Specific MUC combinations, including MUC5A-MUC6, MUC5A-MUC5B, and MUC5B-MUC6, show higher intermolecular hydrogen bond formation affinity. MUC15, MUC16, and MUC24 showed minimal interaction with other MUC types. Among the analyzed MUCs, MUC5B, and MUC6 had the highest probability for binding, while MUC2, MUC4, and MUC5A showed lower probabilities despite greater numbers of binding sites. Conclusion: This study’s results offer significant insights into quails’ MUCs’ composition, expression, network interactions, and binding sites, advancing knowledge of MUC-related processes in gastrointestinal physiology and their potential connection to gastrointestinal diseases. Keywords: gastrointestinal tract and network analysis, gene expression, mucin, quail.

Publisher

Veterinary World

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