5VX5

VP8* of a G2P[4] Human Rotavirus in complex with LNFP1

5VX5 の概要

• エントリーDOI: 10.2210/pdb5vx5/pdb
• 分子名称: Outer capsid protein VP4, alpha-L-fucopyranose-(1-2)-beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-3)-beta-D-galactopyranose-(1-4)-beta-D-glucopyranose (3 entities in total)
• 機能のキーワード: glycan, hbga, rotavirus, viral protein
• 由来する生物種: Rotavirus A
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19352.07

構造登録者

Hu, L.,Venkataram Prasad, B.V. (登録日: 2017-05-23, 公開日: 2018-07-18, 最終更新日: 2023-10-04)

主引用文献

Hu, L.,Sankaran, B.,Laucirica, D.R.,Patil, K.,Salmen, W.,Ferreon, A.C.M.,Tsoi, P.S.,Lasanajak, Y.,Smith, D.F.,Ramani, S.,Atmar, R.L.,Estes, M.K.,Ferreon, J.C.,Prasad, B.V.V.
Glycan recognition in globally dominant human rotaviruses.
Nat Commun, 9:2631-2631, 2018

PubMed Abstract: Rotaviruses (RVs) cause life-threatening diarrhea in infants and children worldwide. Recent biochemical and epidemiological studies underscore the importance of histo-blood group antigens (HBGA) as both cell attachment and susceptibility factors for the globally dominant P[4], P[6], and P[8] genotypes of human RVs. How these genotypes interact with HBGA is not known. Here, our crystal structures of P[4] and a neonate-specific P[6] VP8*s alone and in complex with H-type I HBGA reveal a unique glycan binding site that is conserved in the globally dominant genotypes and allows for the binding of ABH HBGAs, consistent with their prevalence. Remarkably, the VP8* of P[6] RVs isolated from neonates displays subtle structural changes in this binding site that may restrict its ability to bind branched glycans. This provides a structural basis for the age-restricted tropism of some P[6] RVs as developmentally regulated unbranched glycans are more abundant in the neonatal gut.

PubMed: 29980685
DOI: 10.1038/s41467-018-05098-4

実験手法

X-RAY DIFFRACTION (1.285 Å)