3J6L

Kinetic and Structural Analysis of Coxsackievirus B3 Receptor Interactions and Formation of the A-particle

Summary for 3J6L

• Entry DOI: 10.2210/pdb3j6l/pdb
• Related: 3J6M 3J6N 3J6O
• EMDB information: 5927 5928
• Descriptor: Coxsackievirus and adenovirus receptor, SULFATE ION (3 entities in total)
• Functional Keywords: coxsackievirus b3, cvb3, car, cell adhesion
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 14241.10

Authors

Organtini, L.J.,Makhov, A.M.,Conway, J.F.,Hafenstein, S.,Carson, S.D. (deposition date: 2014-03-19, release date: 2014-04-09, Last modification date: 2024-10-30)

Primary citation

Organtini, L.J.,Makhov, A.M.,Conway, J.F.,Hafenstein, S.,Carson, S.D.
Kinetic and structural analysis of coxsackievirus b3 receptor interactions and formation of the a-particle.
J.Virol., 88:5755-5765, 2014

PubMed Abstract: The coxsackievirus and adenovirus receptor (CAR) has been identified as the cellular receptor for group B coxsackieviruses, including serotype 3 (CVB3). CAR mediates infection by binding to CVB3 and catalyzing conformational changes in the virus that result in formation of the altered, noninfectious A-particle. Kinetic analyses show that the apparent first-order rate constant for the inactivation of CVB3 by soluble CAR (sCAR) at physiological temperatures varies nonlinearly with sCAR concentration. Cryo-electron microscopy (cryo-EM) reconstruction of the CVB3-CAR complex resulted in a 9.0-Å resolution map that was interpreted with the four available crystal structures of CAR, providing a consensus footprint for the receptor binding site. The analysis of the cryo-EM structure identifies important virus-receptor interactions that are conserved across picornavirus species. These conserved interactions map to variable antigenic sites or structurally conserved regions, suggesting a combination of evolutionary mechanisms for receptor site preservation. The CAR-catalyzed A-particle structure was solved to a 6.6-Å resolution and shows significant rearrangement of internal features and symmetric interactions with the RNA genome.

PubMed: 24623425
DOI: 10.1128/JVI.00299-14

Experimental method

ELECTRON MICROSCOPY (9 Å)