Cargando…

Archaeal Host Cell Recognition and Viral Binding of HFTV1 to Its Haloferax Host

Viruses are highly abundant and the main predator of microorganisms. Microorganisms of each domain of life are infected by dedicated viruses. Viruses infecting archaea are genomically and structurally highly diverse. Archaea are undersampled for viruses in comparison with bacteria and eukaryotes. Co...

Descripción completa

Detalles Bibliográficos
Autores principales: Schwarzer, Sabine, Hackl, Thomas, Oksanen, Hanna M., Quax, Tessa E. F.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Society for Microbiology 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9973310/
https://www.ncbi.nlm.nih.gov/pubmed/36656006
http://dx.doi.org/10.1128/mbio.01833-22
_version_ 1784898498635759616
author Schwarzer, Sabine
Hackl, Thomas
Oksanen, Hanna M.
Quax, Tessa E. F.
author_facet Schwarzer, Sabine
Hackl, Thomas
Oksanen, Hanna M.
Quax, Tessa E. F.
author_sort Schwarzer, Sabine
collection PubMed
description Viruses are highly abundant and the main predator of microorganisms. Microorganisms of each domain of life are infected by dedicated viruses. Viruses infecting archaea are genomically and structurally highly diverse. Archaea are undersampled for viruses in comparison with bacteria and eukaryotes. Consequently, the infection mechanisms of archaeal viruses are largely unknown, and most available knowledge stems from viruses infecting a select group of archaea, such as crenarchaea. We employed Haloferax tailed virus 1 (HFTV1) and its host, Haloferax gibbonsii LR2-5, to study viral infection in euryarchaea. We found that HFTV1, which has a siphovirus morphology, is virulent, and interestingly, viral particles adsorb to their host several orders of magnitude faster than most studied haloarchaeal viruses. As the binding site for infection, HFTV1 uses the cell wall component surface (S)-layer protein. Electron microscopy of infected cells revealed that viral particles often made direct contact with their heads to the cell surface, whereby the virion tails were perpendicular to the surface. This seemingly unfavorable orientation for genome delivery might represent a first reversible contact between virus and cell and could enhance viral adsorption rates. In a next irreversible step, the virion tail is orientated toward the cell surface for genome delivery. With these findings, we uncover parallels between entry mechanisms of archaeal viruses and those of bacterial jumbo phages and bacterial gene transfer agents.
format Online
Article
Text
id pubmed-9973310
institution National Center for Biotechnology Information
language English
publishDate 2023
publisher American Society for Microbiology
record_format MEDLINE/PubMed
spelling pubmed-99733102023-03-01 Archaeal Host Cell Recognition and Viral Binding of HFTV1 to Its Haloferax Host Schwarzer, Sabine Hackl, Thomas Oksanen, Hanna M. Quax, Tessa E. F. mBio Research Article Viruses are highly abundant and the main predator of microorganisms. Microorganisms of each domain of life are infected by dedicated viruses. Viruses infecting archaea are genomically and structurally highly diverse. Archaea are undersampled for viruses in comparison with bacteria and eukaryotes. Consequently, the infection mechanisms of archaeal viruses are largely unknown, and most available knowledge stems from viruses infecting a select group of archaea, such as crenarchaea. We employed Haloferax tailed virus 1 (HFTV1) and its host, Haloferax gibbonsii LR2-5, to study viral infection in euryarchaea. We found that HFTV1, which has a siphovirus morphology, is virulent, and interestingly, viral particles adsorb to their host several orders of magnitude faster than most studied haloarchaeal viruses. As the binding site for infection, HFTV1 uses the cell wall component surface (S)-layer protein. Electron microscopy of infected cells revealed that viral particles often made direct contact with their heads to the cell surface, whereby the virion tails were perpendicular to the surface. This seemingly unfavorable orientation for genome delivery might represent a first reversible contact between virus and cell and could enhance viral adsorption rates. In a next irreversible step, the virion tail is orientated toward the cell surface for genome delivery. With these findings, we uncover parallels between entry mechanisms of archaeal viruses and those of bacterial jumbo phages and bacterial gene transfer agents. American Society for Microbiology 2023-01-19 /pmc/articles/PMC9973310/ /pubmed/36656006 http://dx.doi.org/10.1128/mbio.01833-22 Text en Copyright © 2023 Schwarzer et al. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution 4.0 International license (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Research Article
Schwarzer, Sabine
Hackl, Thomas
Oksanen, Hanna M.
Quax, Tessa E. F.
Archaeal Host Cell Recognition and Viral Binding of HFTV1 to Its Haloferax Host
title Archaeal Host Cell Recognition and Viral Binding of HFTV1 to Its Haloferax Host
title_full Archaeal Host Cell Recognition and Viral Binding of HFTV1 to Its Haloferax Host
title_fullStr Archaeal Host Cell Recognition and Viral Binding of HFTV1 to Its Haloferax Host
title_full_unstemmed Archaeal Host Cell Recognition and Viral Binding of HFTV1 to Its Haloferax Host
title_short Archaeal Host Cell Recognition and Viral Binding of HFTV1 to Its Haloferax Host
title_sort archaeal host cell recognition and viral binding of hftv1 to its haloferax host
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9973310/
https://www.ncbi.nlm.nih.gov/pubmed/36656006
http://dx.doi.org/10.1128/mbio.01833-22
work_keys_str_mv AT schwarzersabine archaealhostcellrecognitionandviralbindingofhftv1toitshaloferaxhost
AT hacklthomas archaealhostcellrecognitionandviralbindingofhftv1toitshaloferaxhost
AT oksanenhannam archaealhostcellrecognitionandviralbindingofhftv1toitshaloferaxhost
AT quaxtessaef archaealhostcellrecognitionandviralbindingofhftv1toitshaloferaxhost