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( A ) Diagram of the RBD substitutions that distinguish Omicron BA.2.86 from Wuhan-Hu-1 (top), Omicron KP.3.1.1 from BA.2.86 (middle), and Omicron LP.8.1 from BA.2.86 (bottom). Dashed lines show propagation of BA.2.86 changes to KP.3.1.1 and LP.8.1, and italicized mutation in LP.8.1 (H445R) indicates a secondary substitution at a site that previously changed from Wuhan-Hu-1 to BA.2.86. Wuhan-Hu-1 reference spike numbering is used throughout the manuscript. ( B-D ) Quality control of the KP.3.1.1 and LP.8.1 <t>RBD</t> <t>site-saturation</t> <t>mutagenesis</t> library as assessed by PacBio sequencing, illustrating the distribution of number of amino acid mutations per barcoded variant (B), the average number of mutations of each type across library variants (C), and the distribution of mutations across sites in the RBD over all variants (D). ( E, F ) Representative FACS gates used to sort RBD + singlet cells for ACE2 binding (E) and singlet cells for RBD expression (F), which is followed by high-throughput sequencing of cells sorted into each bin. ( G, H ) Correlation in per-mutant deep mutational scanning measurements between independently barcoded replicate libraries for ACE2-binding affinity (G) and RBD expression (H) experiments. Red dash indicates the 1:1 line.
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( A ) Diagram of the RBD substitutions that distinguish Omicron BA.2.86 from Wuhan-Hu-1 (top), Omicron KP.3.1.1 from BA.2.86 (middle), and Omicron LP.8.1 from BA.2.86 (bottom). Dashed lines show propagation of BA.2.86 changes to KP.3.1.1 and LP.8.1, and italicized mutation in LP.8.1 (H445R) indicates a secondary substitution at a site that previously changed from Wuhan-Hu-1 to BA.2.86. Wuhan-Hu-1 reference spike numbering is used throughout the manuscript. ( B-D ) Quality control of the KP.3.1.1 and LP.8.1 RBD site-saturation mutagenesis library as assessed by PacBio sequencing, illustrating the distribution of number of amino acid mutations per barcoded variant (B), the average number of mutations of each type across library variants (C), and the distribution of mutations across sites in the RBD over all variants (D). ( E, F ) Representative FACS gates used to sort RBD + singlet cells for ACE2 binding (E) and singlet cells for RBD expression (F), which is followed by high-throughput sequencing of cells sorted into each bin. ( G, H ) Correlation in per-mutant deep mutational scanning measurements between independently barcoded replicate libraries for ACE2-binding affinity (G) and RBD expression (H) experiments. Red dash indicates the 1:1 line.

Journal: bioRxiv

Article Title: Deep mutational scanning of recent SARS-CoV-2 variants highlights changing amino acid preferences within epistatic hotspot residues

doi: 10.64898/2026.03.11.711006

Figure Lengend Snippet: ( A ) Diagram of the RBD substitutions that distinguish Omicron BA.2.86 from Wuhan-Hu-1 (top), Omicron KP.3.1.1 from BA.2.86 (middle), and Omicron LP.8.1 from BA.2.86 (bottom). Dashed lines show propagation of BA.2.86 changes to KP.3.1.1 and LP.8.1, and italicized mutation in LP.8.1 (H445R) indicates a secondary substitution at a site that previously changed from Wuhan-Hu-1 to BA.2.86. Wuhan-Hu-1 reference spike numbering is used throughout the manuscript. ( B-D ) Quality control of the KP.3.1.1 and LP.8.1 RBD site-saturation mutagenesis library as assessed by PacBio sequencing, illustrating the distribution of number of amino acid mutations per barcoded variant (B), the average number of mutations of each type across library variants (C), and the distribution of mutations across sites in the RBD over all variants (D). ( E, F ) Representative FACS gates used to sort RBD + singlet cells for ACE2 binding (E) and singlet cells for RBD expression (F), which is followed by high-throughput sequencing of cells sorted into each bin. ( G, H ) Correlation in per-mutant deep mutational scanning measurements between independently barcoded replicate libraries for ACE2-binding affinity (G) and RBD expression (H) experiments. Red dash indicates the 1:1 line.

Article Snippet: Site-saturation mutagenesis libraries spanning all 200 positions in the KP.3.1.1 and LP.8.1 RBDs were produced by Twist Bioscience.

Techniques: Mutagenesis, Control, PacBio Sequencing, Variant Assay, Binding Assay, Expressing, Next-Generation Sequencing

Validation of MR analysis results in mice. (A,B) Oil Red O staining of the full-length mouse aorta ( n = 5, mean ± standard deviation). (C–F) Serum levels of triglycerides, total cholesterol, high-density lipoprotein cholesterol, and low-density lipoprotein cholesterol in mice ( n = 5, mean ± standard deviation). (G) Serum levels of total NO in mice ( n = 5, mean ± standard deviation). (H) Relative levels of l -Arg in mouse serum ( n = 5, mean ± standard deviation). (I,J) Relative expression of ARG1 protein in the mouse aorta ( n = 3, mean ± standard deviation). (K) Hematoxylin and eosin staining of the mouse aorta.

Journal: ACS Omega

Article Title: Gualou-Xiebai-Baijiu Decoction Ameliorates Atherosclerosis by Inhibiting the ARG1/ l ‑Arg/NO Pathway: A Study Based on Network Pharmacology

doi: 10.1021/acsomega.5c06829

Figure Lengend Snippet: Validation of MR analysis results in mice. (A,B) Oil Red O staining of the full-length mouse aorta ( n = 5, mean ± standard deviation). (C–F) Serum levels of triglycerides, total cholesterol, high-density lipoprotein cholesterol, and low-density lipoprotein cholesterol in mice ( n = 5, mean ± standard deviation). (G) Serum levels of total NO in mice ( n = 5, mean ± standard deviation). (H) Relative levels of l -Arg in mouse serum ( n = 5, mean ± standard deviation). (I,J) Relative expression of ARG1 protein in the mouse aorta ( n = 3, mean ± standard deviation). (K) Hematoxylin and eosin staining of the mouse aorta.

Article Snippet: Reagents used in this study encompassed 4% paraformaldehyde universal tissue fixative (BL539A; Labgic, Beijing, China), saturated Oil Red O staining solutions (G1015; Servicebio, Wuhan, China), and hematoxylin and eosin staining solutions (G1076; Servicebio).

Techniques: Biomarker Discovery, Staining, Standard Deviation, Expressing