Next Article in Journal
Massively Parallel Profiling of HIV-1 Resistance to the Fusion Inhibitor Enfuvirtide
Previous Article in Journal
Effect of Benzothiadiazole on the Metabolome of Tomato Plants Infected by Citrus Exocortis Viroid
Article Menu

Export Article

Open AccessArticle

Virion-Associated Cholesterol Regulates the Infection of Human Parainfluenza Virus Type 3

State Key Laboratory of Virology and Modern Virology Research Center, College of Life Sciences, Wuhan University, Wuhan 430072, China
*
Authors to whom correspondence should be addressed.
Viruses 2019, 11(5), 438; https://doi.org/10.3390/v11050438
Received: 25 March 2019 / Revised: 5 May 2019 / Accepted: 12 May 2019 / Published: 15 May 2019
  |  
PDF [2648 KB, uploaded 15 May 2019]
  |  

Abstract

The matrix (M) proteins of paramyxoviruses bind to the nucleocapsids and cytoplasmic tails of glycoproteins, thus mediating the assembly and budding of virions. We first determined the budding characterization of the HPIV3 Fusion (F) protein to investigate the assembly mechanism of human parainfluenza virus type 3 (HPIV3). Our results show that expression of the HPIV3 F protein alone is sufficient to initiate the release of virus-like particles (VLPs), and the F protein can regulate the VLP-forming ability of the M protein. Furthermore, HPIV3F-Flag, which is a recombinant HPIV3 with a Flag tag at the C-terminus of the F protein, was constructed and recovered. We found that the M, F, and hemagglutinin-neuraminidase (HN) proteins and the viral genome can accumulate in lipid rafts in HPIV3F-Flag-infected cells, and the F protein mainly exists in the form of F1 in VLPs, lipid rafts, and purified virions. Furthermore, the function of cholesterol in the viral envelope and cell membrane was assessed via the elimination of cholesterol by methyl-β-cyclodextrin (MβCD). Our results suggest that the infectivity of HPIV3 was markedly reduced, due to defective internalization ability in the absence of cholesterol. These results reveal that HPIV3 might assemble in the lipid rafts to acquire cholesterol for the envelope of HPIV3, which suggests the that disruption of the cholesterol composition of HPIV3 virions might be a useful method for the design of anti-HPIV3 therapy. View Full-Text
Keywords: HPIV3; fusion protein; viral assembly; lipid rafts; cholesterol; internalization HPIV3; fusion protein; viral assembly; lipid rafts; cholesterol; internalization
Figures

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).
SciFeed

Share & Cite This Article

MDPI and ACS Style

Tang, Q.; Liu, P.; Chen, M.; Qin, Y. Virion-Associated Cholesterol Regulates the Infection of Human Parainfluenza Virus Type 3. Viruses 2019, 11, 438.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Viruses EISSN 1999-4915 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top