SARS-CoV-2 B.1.1.7 and B.1.351 mutants show enhanced affinity for the ACE2 receptor

Some severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants are highlighted, including the B.1.351 variant first identified in South Africa and the B.1.1.7 variant known as the British variant. It has been.

In a recently uploaded short correspondence Lancet By Ramanasan, Mutsukumar and others. (May 19th^th, 2021) Using microscale thermophoresis to determine the affinity of labeled SARS-CoV-2 spike receptor binding domain proteins supplied by each of these two substances of concern for human angiotensin converting enzyme 2 (ACE2) recombinant protein. Receptors investigated and observed in other studies.

Variant of concern

Both B.1.1.7 and B.1.351 variants of SARS-CoV-2 are Spike protein Receptor binding domains with B.1.351 with two additional mutations suspected of increasing pathogenicity: K417N and E484K.

There is a concern that these mutations will decrease Effectiveness of In essence developed or manipulated immunity. However, there are still no variants that nullify the vaccines developed so far.

Numerous studies have confirmed improved transmissibility of these strains using a number of approaches. In silico Modeling for population meta-study.

This group suggests that several factors may explain the observed increase in transmission of these mutants. Improves accessibility to furin cleavage and promotes improved cell invasion. And / or increased binding affinity for the ACE2 receptor.

Affinity with ACE2

It was found that the B.1.1.7 mutant receptor binding domain binds to the recombinant ACE2 receptor with a 1.98-fold higher affinity than the wild-type. By comparison, the B.1.351 mutant showed 4.62-fold higher affinity, confirming that enhanced affinity plays a role, at least in part, in the increased transmissibility observed in these strains.

As discussed, in several other studies, these mutations are the major SARS-CoV-2 peplomer and ACE2 receptor (commonly found in the lungs that allow the virus to enter cells). It has been suggested to increase the affinity with interacting receptors).The mechanism of enhanced affinity is not completely clear, but other In silico Work is approaching a solid answer elsewhere.

Whatever the mechanism, increased affinity for the ACE2 receptor increases infectivity by lowering the minimum effective concentration of viral particles required to increase the likelihood of cell invasion. That is, less exposure can infect more individuals.

This group used microscale thermophoresis in this study. This suggests that it may be a useful monitoring technique for predicting increased transmission rates of new mutants. It is based on the observation of changes in fluorescence with temperature. This affects the fluorophore microenvironment and therefore changes the intensity of the signal reaching the detector. In this case, the binding event between the ACE2 receptor and the SARS-CoV-2 peplomer receptor binding domain also releases or absorbs energy from the local environment during development and can be detected and quantified in terms of affinity.

Because this technique relies on molecules in solution contained within small capillaries, the equipment is relatively maintenance-free, requires less sample preparation than other fluorescence-based experiments, and is high in a field clinic environment. High-throughput usage is more feasible. ..

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