More Like this

1. Structural Characteristics of Heparin Binding to SARS-CoV-2 Spike Protein RBD of Omicron Sub-Lineages BA.2.12.1, BA.4 and BA.5

   https://doi.org/10.3390/v14122696  

   Shi, Deling; Bu, Changkai; He, Peng; Song, Yuefan; Dordick, Jonathan S.; Linhardt, Robert J.; Chi, Lianli; Zhang, Fuming (December 2022, Viruses)

   The now prevalent Omicron variant and its subvariants/sub-lineages have led to a significant increase in COVID-19 cases and raised serious concerns about increased risk of infectivity, immune evasion, and reinfection. Heparan sulfate (HS), located on the surface of host cells, plays an important role as a co-receptor for virus–host cell interaction. The ability of heparin and HS to compete for binding of the SARS-CoV-2 spike (S) protein to cell surface HS illustrates the therapeutic potential of agents targeting protein–glycan interactions. In the current study, phylogenetic tree of variants and mutations in S protein receptor-binding domain (RBD) of Omicron BA.2.12.1, BA.4 and BA.5 were described. The binding affinity of Omicron S protein RBD to heparin was further investigated by surface plasmon resonance (SPR). Solution competition studies on the inhibitory activity of heparin oligosaccharides and desulfated heparins at different sites on S protein RBD–heparin interactions revealed that different sub-lineages tend to bind heparin with different chain lengths and sulfation patterns. Furthermore, blind docking experiments showed the contribution of basic amino acid residues in RBD and sulfo groups and carboxyl groups on heparin to the interaction. Finally, pentosan polysulfate and mucopolysaccharide polysulfate were evaluated for inhibition on the interaction of heparin and S protein RBD of Omicron BA.2.12.1, BA.4/BA.5, and both showed much stronger inhibition than heparin. 

   more » « less
2. Quaternary Zintl Phases Ba ₂ InSnP ₃ and Ba ₂ InSnAs ₃ with Complex Structures and n-Type Semiconducting Behavior

   https://doi.org/10.1021/acs.chemmater.4c01669  

   Baranets, Sviatoslav; Kandabadage, Thimira; Wang, Xiaoping; Bai, Xiaojian; Young, David P; Bobev, Svilen (August 2024, Chemistry of Materials)
3. Compensatory epistasis maintains ACE2 affinity in SARS-CoV-2 Omicron BA.1

   https://doi.org/10.1038/s41467-022-34506-z  

   Moulana, Alief; Dupic, Thomas; Phillips, Angela M.; Chang, Jeffrey; Nieves, Serafina; Roffler, Anne A.; Greaney, Allison J.; Starr, Tyler N.; Bloom, Jesse D.; Desai, Michael M. (November 2022, Nature Communications)

   Abstract The Omicron BA.1 variant emerged in late 2021 and quickly spread across the world. Compared to the earlier SARS-CoV-2 variants, BA.1 has many mutations, some of which are known to enable antibody escape. Many of these antibody-escape mutations individually decrease the spike receptor-binding domain (RBD) affinity for ACE2, but BA.1 still binds ACE2 with high affinity. The fitness and evolution of the BA.1 lineage is therefore driven by the combined effects of numerous mutations. Here, we systematically map the epistatic interactions between the 15 mutations in the RBD of BA.1 relative to the Wuhan Hu-1 strain. Specifically, we measure the ACE2 affinity of all possible combinations of these 15 mutations (2¹⁵ = 32,768 genotypes), spanning all possible evolutionary intermediates from the ancestral Wuhan Hu-1 strain to BA.1. We find that immune escape mutations in BA.1 individually reduce ACE2 affinity but are compensated by epistatic interactions with other affinity-enhancing mutations, including Q498R and N501Y. Thus, the ability of BA.1 to evade immunity while maintaining ACE2 affinity is contingent on acquiring multiple interacting mutations. Our results implicate compensatory epistasis as a key factor driving substantial evolutionary change for SARS-CoV-2 and are consistent with Omicron BA.1 arising from a chronic infection. 

   more » « less
4. Thermal and Electronic Properties of Ba ₂ MnSe ₃

   https://doi.org/10.1021/acs.inorgchem.2c04048  

   Ojo, Oluwagbemiga P.; Gunatilleke, Wilarachchige D.; Biacchi, Adam J.; Wang, Hsin; Nolas, George S. (February 2023, Inorganic Chemistry)
5. Omicron BA.2 (B.1.1.529.2): High potential to becoming the next dominating variant

   Jiahui Chen; Guo-Wei Wei (April 2022, The journal of physical chemistry letters)