Minimum energy paths for conformational changes of viral capsids

Human rhinoviruses are causative agents of the common cold. In order to release their RNA genome into the host during a viral infection, these small viruses must undergo conformational changes in their capsids, whose detailed mechanism is strictly related to the process of RNA extrusion, which has been only partially elucidated. We study here a mathematical model for the structural transition between the native particle of human rhinovirus type 2 and its expanded form, viewing the process as an energy cascade, i.e. a sequence of metastable states with decreasing energy connected by minimum energy paths. We explore several transition pathways and discuss their implications for the RNA exit process.

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Minimum Energy Paths of Wetting Transitions on Grooved Surfaces

Langmuir ◽

10.1021/la504887w ◽

2015 ◽

Vol 31 (10) ◽

pp. 3059-3068 ◽

Cited By ~ 27

Author(s):

George Pashos ◽

George Kokkoris ◽

Andreas G. Boudouvis

Keyword(s):

Minimum Energy ◽

Wetting Transitions ◽

Minimum Energy Paths

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A theoretical study of the intramolecular solvolytic mechanism of the Meyer–Schuster reaction. MINDO/3 and CNDO/2 calculations of minimum energy paths

Journal of Molecular Structure THEOCHEM ◽

10.1016/0166-1280(83)80032-3 ◽

1983 ◽

Vol 105 (1-2) ◽

pp. 49-54 ◽

Cited By ~ 10

Author(s):

J. Andrés ◽

A. Arnau ◽

E. Silla ◽

J. Bertran ◽

O. Tapia

Keyword(s):

Theoretical Study ◽

Minimum Energy ◽

Minimum Energy Paths

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Multiple minimum-energy paths and scenarios of unwinding transitions in chiral nematic liquid crystals

Physical Review E ◽

10.1103/physreve.100.062704 ◽

2019 ◽

Vol 100 (6) ◽

Cited By ~ 1

Author(s):

Semen S. Tenishchev ◽

Alexei D. Kiselev ◽

Aleksei V. Ivanov ◽

Valery M. Uzdin

Keyword(s):

Liquid Crystals ◽

Nematic Liquid Crystals ◽

Minimum Energy ◽

Chiral Nematic ◽

Minimum Energy Paths

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

Journal of Virology ◽

10.1128/jvi.02371-09 ◽

2010 ◽

Vol 84 (11) ◽

pp. 5550-5564 ◽

Cited By ~ 42

Author(s):

Robert J. Ossiboff ◽

Yi Zhou ◽

Patrick J. Lightfoot ◽

B. V. Venkataram Prasad ◽

John S. L. Parker

Keyword(s):

Conformational Changes ◽

Viral Entry ◽

Structural Changes ◽

Feline Calicivirus ◽

Soluble Receptor ◽

Viral Capsids ◽

Dimer Interface ◽

Metastable Structures ◽

Growth Properties ◽

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 junctional 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-Å 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.

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