Exploring insights of syntaxin superfamily proteins from Entamoeba histolytica: a prospective simulation, protein‐protein interaction, and docking study. Issue 6 (3rd January 2021)

• Record Type: Journal Article
• Authors: Batra, Sagar; Pancholi, Puranjaya; Roy, Mrinalini; Kaushik, Sanket; Jyoti, Anupam; Verma, Kuldeep; Srivastava, Vijay Kumar
• Is Part Of: Journal of molecular recognition. Volume 34:Issue 6(2021)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2021-01-03
• Subjects: Amoebiasis -- Entamoeba histolytica -- Molecular simulation -- Protein‐protein interaction -- SNARE proteins; Molecular recognition -- Periodicals; Models, Molecular -- Periodicals; Molecular Conformation -- Periodicals; Molecular Sequence Data -- Periodicals; Molecular Structure -- Periodicals; Carrier Proteins -- Periodicals; 572.8
• DOI: 10.1002/jmr.2886
• Languages: English
• ISSNs: 0952-3499

Abstract

Abstract: Entamoeba histolytica ( Eh ), a parasitic protozoan and the causative agent of invasive Amoebiasis, invade the host tissue through an effective secretory pathway. There are several lines of evidence suggesting that amoebic trophozoite pore‐forming complex amoebapore and a large class of proteases enzymes including rhomboid proteases, cysteine proteases, and metalloproteases are implicated in host tissue invasion. For successful delivery of these molecules/cargos, trophozoites heavily rely on sorting machinery from the endoplasmic reticulum, Golgi to plasma membrane. Although, sole secretion machinery in E. histolytica is not characterized yet. Therefore, here our aim is to understand the properties of key molecules N ‐ethylmaleimide‐sensitive fusion protein attached to protein receptors (SNAREs) in E. histolytica . SNAREs proteins are an important component of the membrane‐trafficking machinery and have been associated in a range of processes including vesicle tethering, fusion as well as specificity of vesicular transport in all eukaryotic cells. SNARE proteins are architecturally simple, categorized by the presence of one copy of a homologous coiled‐coil forming motif. However, the structural information and protein‐protein interaction study of Eh‐ associated syntaxin proteins are still not known. Here, we characterize the syntaxin 1 like molecule and VAMP from Eh through physiochemical profiling, modeling, atomistic simulation, protein‐protein interaction, and docking approaches on the proteins containing SNARE and synaptobrevin domain. The modeled structures and the critical residues recognized through protein interaction and docking study may provide better structural and functional insights into these proteins and may aid in the development of newer diagnostic assays. Abstract : The study demonstrates the critical role of SNAREs protein receptors in Entamoeba histolytica (Eh), a causative agent of Amoebiasis. Vesicle‐associated membrane protein and Syntaxin proteins in Eh were targeted to unravel the interactions with the protein receptor followed by the structural investigations, which could be a plausible approach to develop a potential inhibitor for the therapeutic management of the disease.