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Thermostability of Reovirus Disassembly Intermediates (ISVPs) Correlates with Genetic, Biochemical, and Thermodynamic Properties of Major Surface Protein μ1
- Publication Year :
- 2002
- Publisher :
- American Society for Microbiology, 2002.
-
Abstract
- Kinetic analyses of infectivity loss during thermal inactivation of reovirus particles revealed substantial differences between virions and infectious subvirion particles (ISVPs), as well as between the ISVPs of reoviruses type 1 Lang (T1L) and type 3 Dearing (T3D). The difference in thermal inactivation of T1L and T3D ISVPs was attributed to the major surface protein μ1 by genetic analyses with reassortant viruses and recoated cores. Irreversible conformational changes in ISVP-bound μ1 were shown to accompany thermal inactivation. The thermal inactivation of ISVPs approximated first-order kinetics over a range of temperatures, permitting the use of Arrhenius plots to estimate activation enthalpies and entropies that account for the different behaviors of T1L and T3D. An effect similar to enthalpy-entropy compensation was additionally noted for the ISVPs of these two isolates. Kinetic analyses with other ISVP-like particles, including ISVPs of a previously reported thermostable mutant, provided further insights into the role of μ1 as a determinant of thermostability. Intact virions, which contain ς3 bound to μ1 as their major surface proteins, exhibited greater thermostability than ISVPs and underwent thermal inactivation with kinetics that deviated from first order, suggesting a role for ς3 in both these properties. The distinct inactivation behaviors of ISVPs are consistent with their role as an essential intermediate in reovirus entry.
- Subjects :
- Immunology
Kinetics
Mutant
Orthoreovirus, Mammalian
Spodoptera
Moths
Microbiology
Cell Line
Heating
Mice
Capsid
L Cells
Virology
Drug Resistance, Viral
Animals
Humans
Orthoreovirus
Mammalian orthoreovirus 3
Mathematical Computing
Thermostability
biology
Ethanol
Structure and Assembly
Viral Core Proteins
Mutagenesis
Virus Activation
Virion
RNA-Binding Proteins
biology.organism_classification
Molecular biology
Insect Science
Biophysics
Capsid Proteins
Subjects
Details
- Language :
- English
- Database :
- OpenAIRE
- Accession number :
- edsair.doi.dedup.....e9a20a4658ec73155c64eb8719d793d7