2ZL7

Atomic resolution structural characterization of recognition of histo-blood group antigens by Norwalk virus

2ZL7 の概要

• エントリーDOI: 10.2210/pdb2zl7/pdb
• 関連するPDBエントリー: 2ZL5 2ZL6
• 分子名称: 58 kd capsid protein, alpha-L-fucopyranose-(1-2)-[2-acetamido-2-deoxy-beta-D-galactopyranose-(1-3)]beta-D-galactopyranose, CALCIUM ION, ... (6 entities in total)
• 機能のキーワード: norovirus, norwalk virus, hbga, histo-blood group antigen, carbohydrate, vp1, p-domain, viral protein
• 由来する生物種: Norwalk virus
• 細胞内の位置: Virion: Q83884
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 63794.87

構造登録者

Choi, J.M.,Huston, A.M.,Estes, M.K.,Prasad, B.V.V. (登録日: 2008-04-02, 公開日: 2008-07-22, 最終更新日: 2023-11-01)

主引用文献

Choi, J.M.,Hutson, A.M.,Estes, M.K.,Prasad, B.V.V.
Atomic resolution structural characterization of recognition of histo-blood group antigens by Norwalk virus
Proc.Natl.Acad.Sci.Usa, 105:9175-9180, 2008

PubMed Abstract: Members of Norovirus, a genus in the family Caliciviridae, are causative agents of epidemic diarrhea in humans. Susceptibility to several noroviruses is linked to human histo-blood type, and its determinant histo-blood group antigens (HBGAs) are regarded as receptors for these viruses. Specificity for these carbohydrates is strain-dependent. Norwalk virus (NV) is the prototype genogroup I norovirus that specifically recognizes A- and H-type HBGA, in contrast to genogroup II noroviruses that exhibit a more diverse HBGA binding pattern. To understand the structural basis for how HBGAs interact with the NV capsid protein, and how the specificity is achieved, we carried out x-ray crystallographic analysis of the capsid protein domain by itself and in complex with A- and H-type HBGA at a resolution of approximately 1.4 A. Despite differences in their carbohydrate sequence and linkage, both HBGAs bind to the same surface-exposed site in the capsid protein and project outward from the capsid surface, substantiating their possible role in initiating cell attachment. Precisely juxtaposed polar side chains that engage the sugar hydroxyls in a cooperative hydrogen bonding and a His/Trp pair involved in a cation-pi interaction contribute to selective and specific recognition of A- and H-type HBGAs. This unique binding epitope, confirmed by mutational analysis, is highly conserved, but only in the genogroup I noroviruses, suggesting that a mechanism by which noroviruses infect broader human populations is by evolving different sites with altered HBGA specificities.

PubMed: 18599458
DOI: 10.1073/pnas.0803275105

実験手法

X-RAY DIFFRACTION (1.35 Å)