3M8L

Crystal Structure Analysis of the Feline Calicivirus Capsid Protein

3M8L の概要

• エントリーDOI: 10.2210/pdb3m8l/pdb
• 分子名称: Capsid protein (1 entity in total)
• 機能のキーワード: fcv-5 capsid, icosahedral virus, virus
• 由来する生物種: Feline calicivirus
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 175784.67

構造登録者

Zhou, Y.,Prasad, B.V.V. (登録日: 2010-03-18, 公開日: 2010-06-30, 最終更新日: 2023-09-06)

主引用文献

Ossiboff, R.J.,Zhou, Y.,Lightfoot, P.J.,Prasad, B.V.,Parker, J.S.
Conformational changes in the capsid of a calicivirus upon interaction with its functional receptor
J.Virol., 84:5550-5564, 2010

PubMed Abstract: Nonenveloped viral capsids are metastable structures that undergo conformational changes during virus entry that lead to interactions of the capsid or capsid fragments with the cell membrane. For members of the Caliciviridae, neither the nature of these structural changes in the capsid nor the factor(s) responsible for inducing these changes is known. Feline junctional adhesion molecule A (fJAM-A) mediates the attachment and infectious viral entry of feline calicivirus (FCV). Here, we show that the infectivity of some FCV isolates is neutralized following incubation with the soluble receptor at 37 degrees C. We used this property to select mutants resistant to preincubation with the soluble receptor. We isolated and sequenced 24 soluble receptor-resistant (srr) mutants and characterized the growth properties and receptor-binding activities of eight mutants. The location of the mutations within the capsid structure of FCV was mapped using a new 3.6-A structure of native FCV. The srr mutations mapped to the surface of the P2 domain were buried at the protruding domain dimer interface or were present in inaccessible regions of the capsid protein. Coupled with data showing that both the parental FCV and the srr mutants underwent increases in hydrophobicity upon incubation with the soluble receptor at 37 degrees C, these findings indicate that FCV likely undergoes conformational change upon interaction with its receptor. Changes in FCV capsid conformation following its interaction with fJAM-A may be important for subsequent interactions of the capsid with cellular membranes, membrane penetration, and genome delivery.

PubMed: 20357100
DOI: 10.1128/JVI.02371-09

実験手法

X-RAY DIFFRACTION (3.4 Å)