Anti-Infectious Bronchitis Virus (IBV) Activity of 1,8-cineole: Effect on Nucleocapsid (N) Protein

Autoren

Zhiwei Yang
Nan Wu
Yujie Fu
Gang Yang
Wei Wang
Yuangang Zu
Thomas Efferth

DOI

10.1080/07391102.2010.10507362

eISSN

1538-0254

ISSN

0739-1102

Ausgabe der Veröffentlichung

3

Zeitschrift

Journal of Biomolecular Structure and Dynamics

Sprache

en

Paginierung

323 - 330

Datum der Veröffentlichung

2010

Status

Published

Herausgeber

Informa UK Limited

Herausgeber URL

http://dx.doi.org/10.1080/07391102.2010.10507362

Datum der Datenerfassung

2019

Titel

Anti-Infectious Bronchitis Virus (IBV) Activity of 1,8-cineole: Effect on Nucleocapsid (N) Protein

Ausgabe der Zeitschrift

28

Data source: Crossref

Abstract

In the present study, anti-IBV (infectious bronchitis virus) activity of 1,8-cineole was studied by MTT assay, as well as docking and molecular dynamic (MD) simulations. The CC50 of 1,8-cineole was above 10 mM. And the maximum noncytotoxic concentration (TD0) of 1,8-cineole was determined to be 3.90 ± 0.22 mM, which was much higher than that of ribavirin (0.78 ± 0.15 mM). 1,8-cineole could inhibit IBV with an IC(50) of 0.61 mM. MTT assay showed that the inhibition of IBV by 1, 8-cineole appears to occur moderately before entering the cell but much strongly after penetration of the virus into the cell. In silico simulations indicated that the binding site of 1,8-cineole was located at the N terminus of phosphorylated nucleocapsid (N) protein, with interaction energy equaling -40.33 kcal mol(-1). The residues TyrA92, ProA134, PheA137, AspA138 and TyrA140 had important roles during the binding process and are fully or partially conserved in various IBV strains. Based on spatial and energetic criteria, 1,8-cineole interfered with the binding between RNA and IBV N-protein. Results presented here may suggest that 1,8-cineole possesses anti-IBV properties, and therefore is a potential source of anti-IBV ingredients for the pharmaceutical industry.

Addresses

Key Laboratory of Forest Plant Ecology, Ministry of Education, Northeast Forestry University, Harbin 150040, PR China.

Autoren

Zhiwei Yang
Nan Wu
Yujie Fu
Gang Yang
Wei Wang
Yuangang Zu
Thomas Efferth
Thomas Efferth

DOI

10.1080/07391102.2010.10507362

eISSN

1538-0254

Externe Identifier

PubMed Identifier: 20919748

Open access

false

ISSN

0739-1102

Ausgabe der Veröffentlichung

3

Zeitschrift

Journal of biomolecular structure & dynamics

Schlüsselwörter

Cell Line
Animals
Chickens
Infectious bronchitis virus
Coronavirus Infections
Poultry Diseases
Cyclohexanols
Monoterpenes
Nucleocapsid Proteins
Anti-Infective Agents
Sequence Alignment
Binding Sites
Molecular Structure
Amino Acid Sequence
Protein Conformation
Models, Molecular
Molecular Sequence Data
Molecular Dynamics Simulation
Eucalyptol

Sprache

eng

Medium

Print

Paginierung

323 - 330

Datum der Veröffentlichung

2010

Status

Published

Datum der Datenerfassung

2010

Titel

Anti-infectious bronchitis virus (IBV) activity of 1,8-cineole: effect on nucleocapsid (N) protein.

Sub types

Research Support, Non-U.S. Gov't
Journal Article

Ausgabe der Zeitschrift

28

Data source: Europe PubMed Central

Abstract

In the present study, anti-IBV (infectious bronchitis virus) activity of 1,8-cineole was studied by MTT assay, as well as docking and molecular dynamic (MD) simulations. The CC50 of 1,8-cineole was above 10 mM. And the maximum noncytotoxic concentration (TD0) of 1,8-cineole was determined to be 3.90 ± 0.22 mM, which was much higher than that of ribavirin (0.78 ± 0.15 mM). 1,8-cineole could inhibit IBV with an IC(50) of 0.61 mM. MTT assay showed that the inhibition of IBV by 1, 8-cineole appears to occur moderately before entering the cell but much strongly after penetration of the virus into the cell. In silico simulations indicated that the binding site of 1,8-cineole was located at the N terminus of phosphorylated nucleocapsid (N) protein, with interaction energy equaling -40.33 kcal mol(-1). The residues TyrA92, ProA134, PheA137, AspA138 and TyrA140 had important roles during the binding process and are fully or partially conserved in various IBV strains. Based on spatial and energetic criteria, 1,8-cineole interfered with the binding between RNA and IBV N-protein. Results presented here may suggest that 1,8-cineole possesses anti-IBV properties, and therefore is a potential source of anti-IBV ingredients for the pharmaceutical industry.

Autoren

Zhiwei Yang
Nan Wu
Yujie Fu
Gang Yang
Wei Wang
Yuangang Zu
Thomas Efferth

Autoren-URL

https://www.ncbi.nlm.nih.gov/pubmed/20919748

DOI

10.1080/07391102.2010.10507362

eISSN

1538-0254

Ausgabe der Veröffentlichung

3

Zeitschrift

J Biomol Struct Dyn

Schlüsselwörter

Amino Acid Sequence
Animals
Anti-Infective Agents
Binding Sites
Cell Line
Chickens
Coronavirus Infections
Cyclohexanols
Eucalyptol
Infectious bronchitis virus
Models, Molecular
Molecular Dynamics Simulation
Molecular Sequence Data
Molecular Structure
Monoterpenes
Nucleocapsid Proteins
Poultry Diseases
Protein Conformation
Sequence Alignment

Sprache

eng

Country

England

Paginierung

323 - 330

PII

c4303/Anti-Infectious-Bronchitis-Virus-IBV-Activity-of-18-cineole-Effect-on-Nucleocapsid-N-Protein-323-330-p17883.html

Datum der Veröffentlichung

2010

Status

Published

Datum, an dem der Datensatz öffentlich gemacht wurde

2011

Titel

Anti-infectious bronchitis virus (IBV) activity of 1,8-cineole: effect on nucleocapsid (N) protein.

Sub types

Journal Article
Research Support, Non-U.S. Gov't

Ausgabe der Zeitschrift

28

Data source: PubMed

Anti-Infectious Bronchitis Virus (IBV) Activity of 1,8-cineole: Effect on Nucleocapsid (N) Protein

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