A Study on Structure and Function of Coronavirus Spike Proteins
Author(s): Sonal Setya*, Arminder Kaur, Divya Prakash and Ramneet Kaur
Abstract
Coronavirus spike enzyme, like a cell-invading biological mechanism, due of their great diversity, they provide an evolutionary challenge. This review paper discovered the cryo-EM structures of the genus' avian respiratory syncytial coronavirus spike proteins. The trimeric n?lƒmmƒo› Bronchitis Virus (IBV) spike ectodomain is made up of 3 receptors binding S1 head as well as trimeric membranes lipid S2 stalks. IBV S1 spans the gap between these different spikes and forms an evolutionary spectrum, whereas IBV S2 is structurally akin to those from new genera, and two S1 domain, comprising the N terminals domains (S1-NTD) or the C-terminals domains deviate from simple tertiaries structure or quaternaries packing to the more complicated ones across various species, resulting in varied roles of the spike in receptors use or membranes synthesis. Based on the system and functionals similarities stated above, the evolution spectra of coronavirus spike followed the sequence of γ-, δ--, and β- genera. The goal of this study is to learn more about the evolutionary relationships amongst coronavirus spike proteins while also broadening our understanding of their structural as well as functional diversity. Despite the fact that considerable study has been done in this area, there is still need for further research in the future.