Exploring insights of syntaxin superfamily proteins from Entamoeba histolytica: a prospective simulation, protein‐protein interaction, and docking study

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.

Probing the Peculiarity of EhRabX10, a pseudoRab GTPase, from the Enteric Parasite Entamoeba histolytica through In Silico Modeling and Docking Studies

“…Additionally, Eh RabX10 is predicted to interact with syntaxin-binding protein of the Sec1 family (EHI_093130). These observations suggest the putative involvement of Eh RabX10 in the cascade of Rab-Sec signalling in the late-stage vesicular pathway [ 53 ]. There is limited knowledge about the role of amoebic Rab GTPases, except Eh Rab5, in the early stages of the endocytic pathway [ 15 , 47 ].…”

Molecular interplays of the Entamoeba histolytica endosomal sorting complexes required for transport during phagocytosis

“…The ESCRT and retromer pathways drive opposing endosomal functions that must somehow coexist; therefore, understanding the segregation of ESCRT and retromer domains on the endosome may be particularly relevant to understanding endosome function. In E. histolytica , the retromer is formed by EhVps26, EhVps29, EhVps35 ( Loftus et al., 2005 ; Nakada-Tsukui et al., 2005 ), EhSNX1 and EhSNX ( Batra et al., 2021 ), and has been associated with the EhCP’s pool maintenance ( Nakada-Tsukui et al., 2005 ). The association among EhVps26, EhVps29, and EhVps35 was evidenced by immunoprecipitation and mass spectrometric analysis ( Nakada-Tsukui et al., 2005 ).…”