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Assessing TLR5 Binding Potential to Helicobacter pylori Pathogen-Associated Molecular Patterns: An In-Silico Approach
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TLRs are essential to the pathophysiology of H. pylori infection through their identification of Pathogen-Associated Molecular Patterns (PAMPs). The role of TLR5 in identifying H. pylori flagellin and other PAMPs has been studied but with conflicting reports. In the present study, TLR5 interaction with H. pylori PAMPs Flagellin A, Flagellin B, CagA and VacA has been carried out in an in-silico approach. The molecules under investigation were downloaded from protein databases such as Protein Data Bank and AlphaFold and the docking study was carried out using ClusPro. The interaction results were visualized using PyMol. Results were interpreted in terms of negative binding energy score and members in clusters. The study showed that TLR5 had a stable and strong binding in terms of binding energy and members in cluster with Flagellin A. TLR5-CagA interaction also showed better interaction than TLR5-Flagellin B and TLR5-VacA.
Title: Assessing TLR5 Binding Potential to Helicobacter pylori Pathogen-Associated Molecular Patterns: An In-Silico Approach
Description:
TLRs are essential to the pathophysiology of H.
pylori infection through their identification of Pathogen-Associated Molecular Patterns (PAMPs).
The role of TLR5 in identifying H.
pylori flagellin and other PAMPs has been studied but with conflicting reports.
In the present study, TLR5 interaction with H.
pylori PAMPs Flagellin A, Flagellin B, CagA and VacA has been carried out in an in-silico approach.
The molecules under investigation were downloaded from protein databases such as Protein Data Bank and AlphaFold and the docking study was carried out using ClusPro.
The interaction results were visualized using PyMol.
Results were interpreted in terms of negative binding energy score and members in clusters.
The study showed that TLR5 had a stable and strong binding in terms of binding energy and members in cluster with Flagellin A.
TLR5-CagA interaction also showed better interaction than TLR5-Flagellin B and TLR5-VacA.
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