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Publication Type : Journal Article
Thematic Areas : Medical Sciences, Nanosciences and Molecular Medicine
Publisher : Biochim Biophys Acta Gen
Source : Biochimica et Biophysica Acta - General Subjects, Volume 1865, Issue 1, January 2021
Campus : Kochi
School : Centre for Cybersecurity Systems and Networks, School of Medicine
Center : Amrita Center for Nanosciences and Molecular Medicine Move
Department : Nanosciences and Molecular Medicine, Microbiology
Verified : No
Year : 2021
Abstract : Background: Bacterial surface proteins act as potential adhesins or invasins. The GroEL is a signal peptide-free surface expressed protein that aids adhesion in Escherichia coli by binding to LOX-1 receptor of the host cells. Mycobacterium tuberculosis (Mtb) expresses GroEL2 protein, having high level sequence identity with E. coli GroEL. This study investigates the interaction mechanism of GroEL2 protein of Mtb with LOX-1 of macrophages using integrated computational and experimental approach. Methods: Mtb GroEL2 protein was purified as histidine tagged protein using Ni-NTA chromatography. Confocal and scanning electron microscopies were used to study the uptake of GroEL2 coated fluorescent latex beads through the LOX-1 receptor in RAW264.7 macrophage cell line. Docking studies were performed to understand the interaction between the GroEL2 and LOX-1 proteins. Polyinosinic acid (PIA) was used as a LOX-1 inhibitor in both in silico and in vitro experiments. Results: GroEL2 protein coating enhances uptake of latex beads into macrophages through LOX-1 receptor. LOX-1 inhibitor PIA decreased the uptake of GroEL2 coated latex beads. GroEL2 interacts with the key ligand binding regions of the LOX-1 receptor, such as the basic spine and the saddle hydrophobic patch. PIA molecule destabilized the LOX-1-GroEL2 docked complex.
Cite this Research Publication : Vivek Vinod, Anju Choorakottayil Pushkaran, Anil Kumar, Chethampadi Gopi Mohan, RajaBiswas "Interaction mechanism of Mycobacterium tuberculosis GroEL2 protein with macrophage Lectin-like, oxidized low-density lipoprotein receptor-1: An integrated computational and experimental study", Biochimica et Biophysica Acta - General Subjects, 2021.