Halorubrum pleomorphic virus-6 Membrane Fusion Is Triggered by an S-Layer Component of Its Haloarchaeal Host

(1) Background: Haloarchaea comprise extremely halophilic organisms of the Archaea domain. They are single-cell organisms with distinctive membrane lipids and a protein-based cell wall or surface layer (S-layer) formed by a glycoprotein array. Pleolipoviruses, which infect haloarchaeal cells, have a...

Full description

Saved in:

Bibliographic Details
Published in:	Viruses Vol. 14; no. 2; p. 254
Main Authors:	Bignon, Eduardo A, Chou, Kevin R, Roine, Elina, Tischler, Nicole D
Format:	Journal Article
Language:	English
Published:	Switzerland MDPI AG 27-01-2022 MDPI
Subjects:	Archaeal Proteins - metabolism Archaeal Viruses - physiology Archaeal Viruses - ultrastructure Cell fusion Cell membranes Cell walls cell-entry Gel electrophoresis Genomes haloarchaea Halorubrum - ultrastructure Halorubrum - virology Host Microbial Interactions HRPV-6 Infections Lipids Liposomes Magnesium Mass spectroscopy Membrane Fusion Membrane Glycoproteins - metabolism Membrane proteins Molecular weight Pleolipoviridae Pore size Proteins Proteolipids - metabolism S-layer Sodium lauryl sulfate Spike protein Sucrose Viral infections Virus Internalization Viruses United States > US Pleolipoviridae receptor cell-entry S-layer haloarchaea HRPV-6 membrane fusion
Online Access:	Get full text
Tags:	Add Tag No Tags, Be the first to tag this record!

Description
Summary:	(1) Background: Haloarchaea comprise extremely halophilic organisms of the Archaea domain. They are single-cell organisms with distinctive membrane lipids and a protein-based cell wall or surface layer (S-layer) formed by a glycoprotein array. Pleolipoviruses, which infect haloarchaeal cells, have an envelope analogous to eukaryotic enveloped viruses. One such member, (HRPV-6), has been shown to enter host cells through virus-cell membrane fusion. The HRPV-6 fusion activity was attributed to its VP4-like spike protein, but the physiological trigger required to induce membrane fusion remains yet unknown. (2) Methods: We used SDS-PAGE mass spectroscopy to characterize the S-layer extract, established a proteoliposome system, and used R18-fluorescence dequenching to measure membrane fusion. (3) Results: We show that the S-layer extraction by Mg chelating from the HRPV-6 host, sp. SS7-4, abrogates HRPV-6 membrane fusion. When we in turn reconstituted the S-layer extract from sp. SS7-4 onto liposomes in the presence of Mg , HRPV-6 membrane fusion with the proteoliposomes could be readily observed. This was not the case with liposomes alone or with proteoliposomes carrying the S-layer extract from other haloarchaea, such as . (4) Conclusions: The S-layer extract from the host, sp. SS7-4, corresponds to the physiological fusion trigger of HRPV-6.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	1999-4915 1999-4915
DOI:	10.3390/v14020254