Microbial Air Quality Assessment of a Tertiary Hospital in Makurdi, North-Central Nigeria

Veterinary / Animal Sciences | Research article | https://doi.org/10.47262/SL/14.1.132026120

In Silico Structural and Functional Profiling of FGIG_11154, a Novel Immune-Interacting Protein of Fasciola gigantica

Areeba Yousaf 1, 2, Muhammad Ehsan 1*, Kinza Shahid 1, 2, Mirza Imran Shahzad 2, Amir Javed 3

¹Department of Parasitology, Faculty of Veterinary and Animal Sciences, The Islamia University of Bahawalpur, 63100, Punjab, Pakistan

²Department of Biochemistry & Molecular Biology, Institute of Biochemistry, Biotechnology & Bioinformatics, The Islamia University of Bahawalpur, 63100 Punjab, Pakistan

³Department of Physiology and Biochemistry, Cholistan University of Veterinary and Animal Sciences, Bahawalpur, 63100, Punjab, Pakistan

Abstract

Fasciola gigantica is a major trematode parasite of veterinary and public health importance, yet a substantial proportion of its proteome remains functionally uncharacterized. In this study, in silico characterization of the hypothetical protein FGIG_11154 (226 amino acids) was performed to infer its structural and functional properties. Physicochemical analysis revealed a hydrophilic, instability-prone protein with a negative GRAVY value and a high proportion of charged residues, suggesting potential involvement in molecular interactions. Sequence similarity analysis demonstrated moderate conservation among Fasciola species, while limited homology with bacterial proteins indicated lineage-specific functionality. Conserved domain analysis identified a significant superantigen-like protein SSL4 domain, implicating a possible role in host immune modulation. Subcellular localization predictions yielded contrasting results, indicating potential extracellular as well as nuclear localization, suggesting multifunctional or context-dependent behavior. Signal peptide and transmembrane helix analyses confirmed that FGIG_11154 is a non-membrane, soluble protein likely secreted via a non-classical pathway. Secondary structure prediction revealed a coil-rich architecture, consistent with intrinsic disorder. Three-dimensional structure modeling using AlphaFold indicated low per-residue confidence, further supporting the presence of disordered regions; however, structural validation via ProSA-web and Ramachandran plot analysis confirmed overall model plausibility. Collectively, these findings suggest that FGIG_11154 may function as a flexible, immune-interacting protein potentially involved in host-parasite interactions.