Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form
As of April 1st VIVO Scientific Profiles will no longer updated for faculty, and the link to VIVO will be removed from the library website. Faculty profile pages will continue to be updated via Interfolio. VIVO will continue being used behind the scenes to update graduate student profiles. Please contact helplib@scripps.edu if you have questions.
How to download citations from VIVO | Alternative profile options

Human rhinovirus capsid dynamics is controlled by canyon flexibility

Academic Article
uri icon
  • Overview
  • Research
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Reisdorph, N.
  • Thomas, J. J.
  • Katpally, U.
  • Chase, E.
  • Harris, K.
  • Siuzdak, Gary
  • Smith, T. J.

publication date

  • September 2003

journal

  • Virology  Journal

abstract

  • Quantitative enzyme accessibility experiments using nano liquid chromatography electrospray mass spectrometry combined with limited proteolysis and isotope-labeling was used to examine the dynamic nature of the human rhinovirus (HRV) capsid in the presence of three antiviral compounds, a neutralizing Fab, and drug binding cavity mutations. Using these methods, it was found that the antivirals WIN 52084 and picovir (pleconaril) stabilized the capsid, while dansylaziridine caused destabilization. Site-directed mutations in the drug-binding cavity were found to stabilize the HRV14 capsid against proteolytic digestion in a manner similar to WIN 52084 and pleconaril. Antibodies that bind to the NIm-IA antigenic site and penetrate the canyon were also observed to protect the virion against proteolytic cleavage. These results demonstrate that quantifying the effects of antiviral ligands on protein "breathing" can be used to compare their mode of action and efficacy. In this case, it is apparent that hydrophobic antiviral agents, antibodies, or mutations in the canyon region block viral breathing. Therefore, these studies demonstrate that mobility in the canyon region is a major determinant in capsid breathing.

subject areas

  • Antibodies, Viral
  • Antigen-Antibody Reactions
  • Binding Sites
  • Capsid
  • HeLa Cells
  • Humans
  • Immunoglobulin Fab Fragments
  • Isoxazoles
  • Microscopy, Electron
  • Models, Molecular
  • Mutation
  • Oxadiazoles
  • Rhinovirus
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
  • Virus Assembly
scroll to property group menus

Research

keywords

  • mass spectrometry
  • rhinovirus
  • virus maturation
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 0042-6822

Digital Object Identifier (DOI)

  • 10.1016/s0042-6822(03)00452-5

PubMed ID

  • 14517058
scroll to property group menus

Additional Document Info

start page

  • 34

end page

  • 44

volume

  • 314

issue

  • 1

©2022 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support