Biology subjects

Hossen, M. L.

Publications and source records attributed to Hossen, M. L..

3 recordsLinked to original sources

bioRxiv2022

Significance of the RBD mutations in the SARS-CoV-2 Omicron: from spike opening to antibody escape and cell attachment

We computationally investigated the role of the Omicron RBD mutations on its structure and interactions with ACE2. Our results suggest that, compared to the WT and Delta, the mutations in the Omicron RBD facilitate a more efficient RBD opening and ACE2 attachment. These effects, combined with antibody evasion, may contribute to its dominance over Delta. While the Omicron RBD escapes most antibodies from prior infections, epitope analysis shows that it harbors sequences with significantly improved antigenicity compared to other variants, suggesting more potent Omicron-specific neutralizing antibodies.

biophysics↗

bioRxiv2022

A dual-receptor mechanism between integrins and ACE2 widens SARS-CoV-2 tissue tropism

In addition to the ACE2 receptor, SARS-CoV-2 binds to integrins to gain host cell entry and trigger pro-inflammatory integrin-mediated signalling cascades. Integrins, therefore, are likely candidates for a dual-receptor mechanism with ACE2 to explain the increased infectivity seen in SARS-CoV-2 models. As integrins are primarily expressed in vasculature and persistent vasculopathy is seen in COVID-19, examining the role of endothelial integrin involvement is crucial in uncovering the pathophysiology of SARS-CoV-2.

cell biology↗

bioRxiv2021

Mutation-induced Changes in the Receptor-binding Interface of the SARS-CoV-2 Delta Variant B.1.617.2 and Implications for Immune Evasion

While the vaccination efforts against SARS-CoV-2 infections are ongoing worldwide, new genetic variants of the virus are emerging and spreading. Following the initial surges of the Alpha (B.1.1.7) and the Beta (B.1.351) variants, a more infectious Delta variant (B.1.617.2) is now surging, further deepening the health crises caused by the pandemic. The sharp rise in cases attributed to the Delta variant has made it especially disturbing and is a variant of concern. Fortunately, current vaccines offer protection against known variants of concern, including the Delta variant. However, the Delta variant has exhibited some ability to dodge the immune system as it is found that neutralizing antibodies from prior infections or vaccines are less receptive to binding with the Delta spike protein. Here, we investigated the structural changes caused by the mutations in the Delta variants receptor-binding interface and explored the effects on binding with the ACE2 receptor as well as with neutralizing antibodies. We find that the receptor-binding {beta}-loop-{beta} motif adopts an altered but stable conformation causing separation in some of the antibody binding epitopes. Our study shows reduced binding of neutralizing antibodies and provides a possible mechanism for the immune evasion exhibited by the Delta variant.

biophysics↗