Analysis of Interaction between odorant receptors and flexible spike of SARS CoV-2- key to loss of smell.

ABSTRACT

The vaccine development for severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is primarily focused on structure of the spike (S) protein. The heavy glycosylation of S with flexible hinges at stalk shields from antibodies. The flexible nature of hinges may be one of the important factors which are responsible for binding the odorant receptor of those neurons which are responsible for the loss of smell in patients with COVID-19 infection. In this study strong and stable bond formation results from reaction between R14 Trp and Phe at the residue, the expected outcome of this research may help in designing a novel vaccine that targets the flexible hinges of SARS-CoV-2. The difference in the conformational structure of S protein and their binding with the odorant receptor in COVID-19 are prime factor for the loss of smell and taste in patients supported by the concept of Antigen (epitope) Antibody interaction by stable formation of Hydrogen bond among odorant receptor and the S protein. The flexibility of structural proteins determines if the antibodies or other defense proteins produced are homologous participating in antigen antibody reaction thus maintaining the most neutralization sensitive epitope to produce the new vaccine strain or in isolating most effectively neutralizing human mABs. Molecular and atomic level details potentiate the design and screening of small molecules that can inhibit the fusion at entry level or at odorant receptors and potentially be used in prevention and treatment of infection particularly when formulated as nasal drops, paving a new approach for pharmacologist in treatment of COVID-19 infection.