|Title||Kinetic and structural analysis of coxsackievirus B3 receptor interactions and formation of the A-particle.|
|Journal, issue, pages||J Virol, Vol. 88, Issue 10, Page 5755-5765, Year 2014|
|Publish date||Mar 12, 2014|
|Authors||Lindsey J Organtini / Alexander M Makhov / James F Conway / Susan Hafenstein / Steven D Carson /|
|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 ...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.|
IMPORTANCE: This report presents new information about receptor use by picornaviruses and highlights the importance of attaining at least an ∼9-Å resolution for the interpretation of cryo-EM complex maps. The analysis of receptor binding elucidates two complementary mechanisms for preservation of the low-affinity (initial) interaction of the receptor and defines the kinetics of receptor-catalyzed conformational change to the A-particle.
|External links||J Virol / PubMed:24623425 / PubMed Central|
|Methods||EM (single particle)|
EMDB-5927, PDB-3j6l, PDB-3j6m, PDB-3j6n, PDB-3j6o:
|Keywords||coxsackievirus b3 / cvb3 / CAR / cryoEM / A-particle / Amino Acid Sequence / Binding Sites / Coxsackie and Adenovirus Receptor-Like Membrane Protein / Cryoelectron Microscopy / Enterovirus B, Human / Kinetics / Models, Molecular / Molecular Sequence Data / Protein Binding / Protein Conformation / Virion / Virus Attachment / Virus Inactivation / CELL ADHESION|
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