Back to Search Start Over

Hantavirus Gn and Gc Glycoproteins Self-Assemble into Virus-Like Particles

Authors :
Rodrigo Acuña
Manuela Bulling
Nicole D. Tischler
Nicolás Cifuentes-Muñoz
Jonas Klingström
Chantal L. Márquez
Roberta Mancini
Pierre-Yves Lozach
Center for Integrative Infectious Diseases Research [Heidelberg, Allemagne] (CIID)
Heidelberg University Hospital [Heidelberg]
Molecular Virology Laboratory
Fundación Ciencia & Vida
Center for Infectious Medicine, Department of Medicine
Karolinska Institutet, Karolinska University Hospital
Department of Preparedness
Swedish Institute for Communicable Disease Control
Institute of Biochemistry
Eidgenössische Technische Hochschule - Swiss Federal Institute of Technology [Zürich] (ETH Zürich)
Institut Armand Frappier (INRS-IAF)
Réseau International des Instituts Pasteur (RIIP)-Institut National de la Recherche Scientifique [Québec] (INRS)
Facultad de Ciencias Biológicas
Universidad Andrés Bello [Santiago] (UNAB)
This work was financed by CONICYT through grant FONDECYT 1100756 and basal funding PFB-16. R.A. was supported by a CONICYT doctoral fellowship.
Institut National de la Recherche Scientifique [Québec] (INRS)-Réseau International des Instituts Pasteur (RIIP)
Source :
Journal of Virology, Journal of Virology, American Society for Microbiology, 2014, 88 (4), pp.2344-2348. ⟨10.1128/JVI.03118-13⟩, JOURNAL OF VIROLOGY, Artículos CONICYT, CONICYT Chile, instacron:CONICYT, Journal of Virology, American Society for Microbiology, 2014, 88 (4), pp.2344-8. ⟨10.1128/JVI.03118-13⟩
Publication Year :
2014
Publisher :
American Society for Microbiology, 2014.

Abstract

How hantaviruses assemble and exit infected cells remains largely unknown. Here, we show that the expression of Andes (ANDV) and Puumala (PUUV) hantavirus Gn and Gc envelope glycoproteins lead to their self-assembly into virus-like particles (VLPs) which were released to cell supernatants. The viral nucleoprotein was not required for particle formation. Further, a Gc endodomain deletion mutant did not abrogate VLP formation. The VLPs were pleomorphic, exposed protrusions and reacted with patient sera.

Details

ISSN :
10985514 and 0022538X
Volume :
88
Database :
OpenAIRE
Journal :
Journal of Virology
Accession number :
edsair.doi.dedup.....182eaff818b74a7a32b715c4aff450aa
Full Text :
https://doi.org/10.1128/jvi.03118-13