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Title: Structure and Function of a Genetically Engineered Mimic of a Nonenveloped Virus Entry Intermediate

Abstract

Divalent metal ions are components of numerous icosahedral virus capsids. Flock House virus (FHV), a small RNA virus of the family Nodaviridae, was utilized as an accessible model system with which to address the effects of metal ions on capsid structure and on the biology of virus-host interactions. Mutations at the calcium-binding sites affected FHV capsid stability and drastically reduced virus infectivity, without altering the overall architecture of the capsid. The mutations also altered the conformation of gamma, a membrane-disrupting, virus-encoded peptide usually sequestered inside the capsid, by increasing its exposure under neutral pH conditions. Our data demonstrate that calcium binding is essential for maintaining a pH-based control on gamma exposure and host membrane disruption, and they reveal a novel rationale for the metal ion requirement during virus entry and infectivity. In the light of the phenotypes displayed by a calcium site mutant of FHV, we suggest that this mutant corresponds to an early entry intermediate formed in the endosomal pathway.

Authors:
; ; ; ; ; ;  [1]
  1. UCSD
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
USDOE
OSTI Identifier:
1002347
Resource Type:
Journal Article
Journal Name:
J. Virol.
Additional Journal Information:
Journal Volume: 84; Journal Issue: (9) ; 05, 2010; Journal ID: ISSN 0022-538X
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES; 99 GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE; ARCHITECTURE; BIOLOGY; CALCIUM; INFECTIVITY; MEMBRANES; MUTANTS; MUTATIONS; PEPTIDES; RNA; STABILITY

Citation Formats

Banerjee, Manidipa, Speir, Jeffrey A, Kwan, Maggie H, Huang, Rick, Aryanpur, Peyman P, Bothner, Brian, Johnson, John E, and Montana). Structure and Function of a Genetically Engineered Mimic of a Nonenveloped Virus Entry Intermediate. United States: N. p., 2010. Web. doi:10.1128/JVI.02670-09.
Banerjee, Manidipa, Speir, Jeffrey A, Kwan, Maggie H, Huang, Rick, Aryanpur, Peyman P, Bothner, Brian, Johnson, John E, & Montana). Structure and Function of a Genetically Engineered Mimic of a Nonenveloped Virus Entry Intermediate. United States. https://doi.org/10.1128/JVI.02670-09
Banerjee, Manidipa, Speir, Jeffrey A, Kwan, Maggie H, Huang, Rick, Aryanpur, Peyman P, Bothner, Brian, Johnson, John E, and Montana). 2010. "Structure and Function of a Genetically Engineered Mimic of a Nonenveloped Virus Entry Intermediate". United States. https://doi.org/10.1128/JVI.02670-09.
@article{osti_1002347,
title = {Structure and Function of a Genetically Engineered Mimic of a Nonenveloped Virus Entry Intermediate},
author = {Banerjee, Manidipa and Speir, Jeffrey A and Kwan, Maggie H and Huang, Rick and Aryanpur, Peyman P and Bothner, Brian and Johnson, John E and Montana)},
abstractNote = {Divalent metal ions are components of numerous icosahedral virus capsids. Flock House virus (FHV), a small RNA virus of the family Nodaviridae, was utilized as an accessible model system with which to address the effects of metal ions on capsid structure and on the biology of virus-host interactions. Mutations at the calcium-binding sites affected FHV capsid stability and drastically reduced virus infectivity, without altering the overall architecture of the capsid. The mutations also altered the conformation of gamma, a membrane-disrupting, virus-encoded peptide usually sequestered inside the capsid, by increasing its exposure under neutral pH conditions. Our data demonstrate that calcium binding is essential for maintaining a pH-based control on gamma exposure and host membrane disruption, and they reveal a novel rationale for the metal ion requirement during virus entry and infectivity. In the light of the phenotypes displayed by a calcium site mutant of FHV, we suggest that this mutant corresponds to an early entry intermediate formed in the endosomal pathway.},
doi = {10.1128/JVI.02670-09},
url = {https://www.osti.gov/biblio/1002347}, journal = {J. Virol.},
issn = {0022-538X},
number = (9) ; 05, 2010,
volume = 84,
place = {United States},
year = {Wed Apr 07 00:00:00 EDT 2010},
month = {Wed Apr 07 00:00:00 EDT 2010}
}