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Title: Conformational Changes in the Capsid of a Calicivirus upon Interaction with Its Functional Receptor

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 functional 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 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-{angstrom} 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 C,more » 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.« less

Authors:
; ; ; ;  [1];  [2]
  1. (Baylor)
  2. (
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
USDOE
OSTI Identifier:
1002498
Resource Type:
Journal Article
Resource Relation:
Journal Name: J. Virol.; Journal Volume: 84; Journal Issue: (11) ; 06, 2010
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES; 99 GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE; VIRUSES; ADHESION; CONFORMATIONAL CHANGES; INFECTIVITY; MUTANTS; MUTATIONS; INTERACTIONS; RECEPTORS

Citation Formats

Ossiboff, Robert J., Zhou, Yi, Lightfoot, Patrick J., Prasad, B.V. Venkataram, Parker, John S.L., and Cornell). Conformational Changes in the Capsid of a Calicivirus upon Interaction with Its Functional Receptor. United States: N. p., 2010. Web. doi:10.1128/JVI.02371-09.
Ossiboff, Robert J., Zhou, Yi, Lightfoot, Patrick J., Prasad, B.V. Venkataram, Parker, John S.L., & Cornell). Conformational Changes in the Capsid of a Calicivirus upon Interaction with Its Functional Receptor. United States. doi:10.1128/JVI.02371-09.
Ossiboff, Robert J., Zhou, Yi, Lightfoot, Patrick J., Prasad, B.V. Venkataram, Parker, John S.L., and Cornell). Mon . "Conformational Changes in the Capsid of a Calicivirus upon Interaction with Its Functional Receptor". United States. doi:10.1128/JVI.02371-09.
@article{osti_1002498,
title = {Conformational Changes in the Capsid of a Calicivirus upon Interaction with Its Functional Receptor},
author = {Ossiboff, Robert J. and Zhou, Yi and Lightfoot, Patrick J. and Prasad, B.V. Venkataram and Parker, John S.L. and Cornell)},
abstractNote = {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 functional 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 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-{angstrom} 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 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.},
doi = {10.1128/JVI.02371-09},
journal = {J. Virol.},
number = (11) ; 06, 2010,
volume = 84,
place = {United States},
year = {Mon Jul 19 00:00:00 EDT 2010},
month = {Mon Jul 19 00:00:00 EDT 2010}
}