6OAS

Structure of canine parvovirus in complex with transferrin receptor type-1

6OAS の概要

• エントリーDOI: 10.2210/pdb6oas/pdb
• EMDBエントリー: 20001 20002 20003
• 分子名称: Capsid protein VP1 (1 entity in total)
• 機能のキーワード: cpv, tfr, icosahedral, cryo, virus
• 由来する生物種: Canine parvovirus 2 (CPV-2)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 61562.37

構造登録者

Lee, H.,Hafenstein, S. (登録日: 2019-03-18, 公開日: 2019-09-18, 最終更新日: 2024-11-06)

主引用文献

Lee, H.,Callaway, H.M.,Cifuente, J.O.,Bator, C.M.,Parrish, C.R.,Hafenstein, S.L.
Transferrin receptor binds virus capsid with dynamic motion.
Proc.Natl.Acad.Sci.USA, 116:20462-20471, 2019

PubMed Abstract: Canine parvovirus (CPV) is an important pathogen causing severe diseases in dogs, including acute hemorrhagic enteritis, myocarditis, and cerebellar disease. Cross-species transmission of CPV occurs as a result of mutations on the viral capsid surface that alter the species-specific binding to the host receptor, transferrin receptor type-1 (TfR). The interaction between CPV and TfR has been extensively studied, and previous analyses have suggested that the CPV-TfR complex is asymmetric. To enhance the understanding of the underlying molecular mechanisms, we determined the CPV-TfR interaction using cryo-electron microscopy to solve the icosahedral (3.0-Å resolution) and asymmetric (5.0-Å resolution) complex structures. Structural analyses revealed conformational variations of the TfR molecules relative to the binding site, which translated into dynamic molecular interactions between CPV and TfR. The precise footprint of the receptor on the virus capsid was identified, along with the identity of the amino acid residues in the virus-receptor interface. Our "rock-and-roll" model provides an explanation for previous findings and gives insights into species jumping and the variation in host ranges associated with new pandemics in dogs.

PubMed: 31548398
DOI: 10.1073/pnas.1904918116

実験手法

ELECTRON MICROSCOPY (3 Å)