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Aa 279–405
- The P domain includes amino acids 226–520 and is subdivided into subdomains P1 and P2. The P1 subdomain (aa 226–278 and 406–520) form the sides of the capsomers whereas the P2 subdomain (aa 279–405) form the most protruding part of the capsomers' arch (Figure 162-2).
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Mar 1, 2021 · The P2 subdomain forms the outermost part of the capsid and contains the interface that binds the receptor molecules (e.g., HBGAs). The capsid structure of NoV was prepared based on the crystal protein structure of Norwalk Virus (Protein Data Bank ID: 1IHM) using the software Chimera 1.14.
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Jun 15, 2020 · The most variable region of the P domain is the subdomain P2, which is extended from the S domain to the outside of the capsid and is located in the middle part of the structural protein VP1 (28, 44). In a study of HuNoV VP1, the sequence diversity in the P2 region was determined by sequence analysis techniques and homology models using the ...
Jun 6, 2023 · The P domain is further divided into P1 and P2 subdomains where the P2 subdomain is exposed on the outer surface and is highly variable in sequence, facilitating escape from an antibody...
Mar 30, 2021 · The surface-exposed P2 subdomain is thought to dictate binding to the cellular attachment factors, histo-blood group antigen (HGBA) carbohydrates (highlighted in green), while the S domain forms the core of the viral particle.
- Lauren A. Ford-Siltz, Kentaro Tohma, Gabriel I. Parra
- 2021
Sep 1, 2013 · The localization of the key mutation G365N in the Norwalk virus VP1 P2 subdomain structure is indicated by arrows. The shell domain is shown in tan, and the P1 and P2 subdomains are shown in light blue and blue, respectively.
Oct 18, 2012 · Three blockade epitopes have been identified in GII.4 NoVs. Epitope A (residues 294, 296–298, 368, and 372; green), Epitope D (residues 393–395; orange), and Epitope E (residues 407, 412–413; yellow) all map to the P2 subdomain on the surface of the virion.
Dec 16, 2022 · Furthermore, the P2 subdomain is a hypervariable region and the most-surface exposed part of the viral particle, which harbours the histo-blood group antigens (HBGA) binding interface and “major neutralising epitopes for immune evasion and cell infiltration” .
