In silico characterization of OprD protein in Pseudomonas aeruginosa: Structural, immunological, and functional insights | ||
| Microbes and Infectious Diseases | ||
| Articles in Press, Accepted Manuscript, Available Online from 31 October 2025 | ||
| Document Type: Original Article | ||
| DOI: 10.21608/mid.2025.426873.3254 | ||
| Authors | ||
| allyaa Natheer Al-Abase1; Mawj Saddam Zabn2; Zahraa Khalid Al-Kheroo* 1; Mahmmood A. Al-tobje1 | ||
| 1Department of Biology, College of Sciences, University of Mosul, Mosul, Iraq | ||
| 2Department of Biology, College of Sciences, University of Tikrit, Tikrit, Iraq | ||
| Abstract | ||
| Background: Pseudomonas aeruginosa is a resistant pathogen where OprD porin plays a key role in carbapenem uptake. Its structural and immunological features remain underexplored computationally. This study characterizes OprD, focusing on sequence conservation, glycosylation, epitope prediction, and structural modeling for resistance insights. Methods: We applied a multi-step in silico pipeline to analyze OprD’s sequence, glycosylation sites, antigenic regions, and 3D structure. Tools included domain prediction, epitope mapping, and structural modeling using validated bioinformatics platforms. Results: OprD showed 97.6% sequence similarity with known porins, confirming conserved domains. GlycoEP predicted N- and O-linked glycosylation at residues 121, 198, and 380. TNFepitope analysis revealed short peptides with TNF-α induction potential. Structural modeling highlighted hydrophobic and charged surface regions, with a boundary near residue 380 suggesting functional flexibility. Conclusion: This study provides computational insights into OprD’s structure and immunogenicity, supporting its role in resistance and host interaction. These findings lay groundwork for future experimental validation. | ||
| Keywords | ||
| Bioinformatics; Interleukin; OprD; P. aeruginosa; Physiochemical | ||
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