FliC Protein from Enterobacteriaceae Family revealed aPromising Epitope-Delivery Platform

سال انتشار: 1401
نوع سند: مقاله کنفرانسی
زبان: انگلیسی
مشاهده: 170

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شناسه ملی سند علمی:

MEDISM23_056

تاریخ نمایه سازی: 16 مهر 1401

چکیده مقاله:

Background and Aim : Flagella are filamentous organelles with essential roles in bacterialphysiology, such as motility and chemotaxis. Studies have shown that more than ۵۰ genes arecomplicated in the assembly and function of flagella. Flagellin (FliC) is an essential subunit offlagella in motile bacteria. The flagellin subunit, encoded by the fliC gene, has a tubular structureat the distal end of flagella. The atomic model of flagellin as a component of the ۱۱ proto-filamentswas constructed from electron micrographs. The ۳D structure of the FliC protein showed that thisprotein typically has four main domains, consisting of D۰, D۱, D۲ and D۳. The D۰ and D۱ domainsare required to mediate flagellar polymerization. Analysis of the sequence diversity of the FliCprotein in the Enterobacteriaceae family may provide insight into the pathogenic strategy of thesebacteria in the context of interaction with pathogen -associated molecular patterns. In addition, theefficacy of FliC as an adjuvant or a component of the multi-epitope vaccine has been demonstrated.Methods : We analyzed ۳۹۲ full-length FliC proteins from the Enterobacteriaceae family. In thefirst step, isoelectric pH, molecular weight, and amino acid composition of FliC protein sequenceswere calculated using the ProtParam program. Next, the tertiary structure of the FliC proteins andits interaction with zebrafish TLR -۵ was performed. Sequence alignments were performed usingClustalW software and the curricular phylogenetic tree was depicted using MEGA -۷ software andiTOL web server. Finally, we evaluated the interaction of FliC proteins of Enterobacteriaceaefamily with TLR-۵ to find the strongest docking.Results : Physicochemical properties and multiple sequence alignments revealed that FliC has aunique characterization in each genus. However, D۱ as the binding domain site associated withTLR-۵ exhibited high sequence conservation and the FliC protein of S. enterica subsp. entericahad the strongest interaction with TLR-۵.Conclusion : FliC protein of S. enterica subsp. enterica can be considered as a promising epitope-delivery platform. In addition, phylogenetic analysis revealed that FliC may be acceptable markerfor distinguishing genera in the Enterobacteriaceae family.

نویسندگان

Amin Sepehr

Department of Bacteriology, Pasteur Institute of Iran, Tehran, Iran.

Sepideh Fereshteh

Department of Bacteriology, Pasteur Institute of Iran, Tehran, Iran.