VP4 protein from human rhinovirus 14 is released by pressure and locked in the capsid by the antiviral compound WIN.

VP4 protein from human rhinovirus 14 is released by pressure and locked in the capsid by the antiviral compound WIN. Research Abstract Details 

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VP4 protein from human rhinovirus 14 is released by pressure and locked in the capsid by the antiviral compound WIN. Abstract Text:

Rafael B ,Ygara S Mendes,Marcia R Soares,Umesh Katpally,Thomas J Smith,Jerson L Silva, Oliveira,

Rhinoviruses are the major causative agents of the common cold in humans. Here, we studied the stability of human rhinovirus type 14 (HRV14) under conditions of high hydrostatic pressure, low temperature, and urea in the absence and presence of an antiviral drug. Capsid dissociation and changes in the protein conformation were monitored by fluorescence spectroscopy, light scattering, circular dichroism, gel filtration chromatography, mass spectrometry and infectivity assays. The data show that high pressure induces the dissociation of HRV14 and that this process is inhibited by WIN 52084. MALDI-TOF mass spectrometry experiments demonstrate that VP4, the most internal viral protein, is released from the capsid by pressure treatment. This release of VP4 is concomitant with loss of infectivity. Our studies also show that at least one antiviral effect of the WIN drugs involves the locking of VP4 inside the capsid by blocking the dynamics associated with cell attachment.

VP4 protein from human rhinovirus 14 is released by pressure and locked in the capsid by the antiviral compound WIN. Publishing Authors By Initials

RB ,YS Mendes,MR Soares,U Katpally,TJ Smith,JL Silva,AC Oliveira,

For similar biological phenomena, cell phenomena, and immunity: biological phenomena: microbiologic phenomena: viral physiology: virus replication: virus assembly research abstracts see: biological phenomena, cell phenomena, and immunity: biological phenomena: microbiologic phenomena: viral physiology: virus replication: virus assembly research

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VP4 protein from human rhinovirus 14 is released by pressure and locked in the capsid by the antiviral compound WIN. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of molecular biology

VOLUME: 366

Page Numbers: 295-306

Journal Abbreviation: J. Mol. Biol.

ISSN: 0022-2836

DAY: 11

MONTH: 11

YEAR: 2006

VP4 protein from human rhinovirus 14 is released by pressure and locked in the capsid by the antiviral compound WIN. Information

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LANGUAGE: eng

NlmUniqueID: 2985088

VP4 protein from human rhinovirus 14 is released by pressure and locked in the capsid by the antiviral compound WIN. Keywords Mesh Terms:

KEYWORDS: Virus Assembly

MESH TERMS: pharmacology

Chemical & Substance for Abstract: VP4 protein from human rhinovirus 14 is released by pressure and locked in the capsid by the antiviral compound WIN. Information

Substance Name: Win 52084

Registry Number: 98102-61-5

Grant and Affiliation Information for VP4 protein from human rhinovirus 14 is released by pressure and locked in the capsid by the antiviral compound WIN.

AFFILIATION: Programa de Biologia Estrutural, Instituto de Bioquímica Médica, CCS, Universidade Federal do Rio de Janeiro, RJ 21941-590, Brazil.

Country: England

AGENCY: United States NIGMS

GRANT: R01 GM010704-42

ACRONYM: GM

MEDLINETA: J Mol Biol

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