Year: 2018
Type: dissertation
Abstract: Coronaviruses are emerging pathogens that threaten human health and prosperity. Each year, hundreds of millions of people are infected with continually circulating coronaviruses that cause the common cold in healthy individuals and kill the most vulnerable of us. Coronaviruses adapt to environmental change at a remarkable rate. The HCoV-229E coronavirus has adapted and evolved over the last 50 years by mutating residues in the receptor-binding loops of the receptor binding domain (RBD) of its spike (S) protein. These sequences phylogenetically segregate into Classes whose viruses have successively replaced one another in the human population. These Classes possess different receptor (hAPN) and antibody binding characteristics and the crystal structures of RBD-hAPN complexes have been solved. Structural insights into the ever-changing RBD and its interaction with hAPN show the use of secondary structure-less loops facilitate tremendous structural variability, a trait that likely enables changes in viral fitness and immune evasion.
Source: TSpace (University of Toronto)
Author: Aidan Charles Andrew Tomlinson
Language: English
Subfield: Infectious Diseases
Field: Medicine
Domain: Health Sciences
Open Access status: green
OpenAlex ID: W3159382739