ArticleJournal of virology2008
Topology and membrane anchoring of the coronavirus replication complex: not all hydrophobic domains of nsp3 and nsp6 are membrane spanning.
Article in Journal of virology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 114 papers.
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Who cites it
114 citing papers in PubMed, 172 citations in OpenAlex.
- Review
- The DMV pore-forming TM2-Y region of SARS-CoV-2 nsp3 exhibits structural conservation beyond the coronavirus family.Journal of virology · 2026Article
- Unlocking the secrets of SARS-CoV-2 nsp3 by combining experiments with AlphaFold2 domain prediction.Life science alliance · 2026Article
- NSP6 regulates calcium overload-induced autophagic cell death and is regulated by KLHL22-mediated ubiquitination.Journal of advanced research · 2025Article
- RAB5 is a host dependency factor for the generation of SARS-CoV-2 replication organelles.mBio · 2025Article
- Genome-scale CRISPR screen identifies TMEM198 driving double membrane vesicle formation in swine alphacoronavirus and murine betacoronavirus infected cells.PLoS pathogens · 2025Article
- Visualizing the Active Site Oxyanion Loop Transition Upon Ensitrelvir Binding and Transient Dimerization of SARS-CoV-2 Main Protease.Journal of molecular biology · 2024Article
- Oligomeric assembly of the C-terminal and transmembrane region of SARS-CoV-2 nsp3.Journal of virology · 2024Article
- Insights into the mechanism of SARS-CoV-2 main protease autocatalytic maturation from model precursors.Communications biology · 2023Article
- SARS-CoV-2 nonstructural protein 6 from Alpha to Omicron: evolution of a transmembrane protein.mBio · 2023Article
- The multiple roles of nsp6 in the molecular pathogenesis of SARS-CoV-2.Antiviral research · 2023Review
- Molecular mechanisms of human coronavirus NL63 infection and replication.Virus research · 2023Review
- Evaluating the Virology and Evolution of Seasonal Human Coronaviruses Associated with the Common Cold in the COVID-19 Era.Microorganisms · 2023Review
- A review on structural, non-structural, and accessory proteins of SARS-CoV-2: Highlighting drug target sites.Immunobiology · 2023Review
- Structure genomics of SARS-CoV-2 and its Omicron variant: drug design templates for COVID-19.Acta pharmacologica Sinica · 2022Review
- SARS-CoV-2 Amino Acid Mutations Detection in Greek Patients Infected in the First Wave of the Pandemic.Microorganisms · 2022Article
- Identification of intrinsically disorder regions in non-structural proteins of SARS-CoV-2: New insights into drug and vaccine resistance.Molecular and cellular biochemistry · 2022Article
- Predicted coronavirus Nsp5 protease cleavage sites in the human proteome.BMC genomic data · 2022Article
- Overview of SARS-CoV-2 genome-encoded proteins.Science China. Life sciences · 2022Review
- COVID-19: A review of newly formed viral clades, pathophysiology, therapeutic strategies and current vaccination tasks.International journal of biological macromolecules · 2021Review
54 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Coronaviruses express two very large replicase polyproteins, the 16 autoproteolytic cleavage products of which collectively form the membrane-anchored replication complexes. How these structures are assembled is still largely unknown, but it is likely that the membrane-spanning members of these nonstructural proteins (nsps) are responsible for the induction of the double-membrane vesicles and for anchoring the replication complexes to these membranes. For 3 of the 16 coronavirus nsps-nsp3, nsp4, and nsp6-multiple transmembrane domains are predicted. Previously we showed that, consistent with predictions, nsp4 occurs in membranes with both of its termini exposed in the cytoplasm (M. Oostra et al., J. Virol. 81:12323-12336, 2007). Strikingly, however, for both nsp3 and nsp6, predictions based on a multiple alignment of 27 coronavirus genome sequences indicate an uneven number of transmembrane domains. As a consequence, the proteinase domains present in nsp3 and nsp5 would be separated from their target sequences by the lipid bilayer. To look into this incongruity, we studied the membrane disposition of nsp3 and nsp6 of the severe acute respiratory syndrome coronavirus and murine hepatitis virus by analyzing tagged forms of the proteins expressed in cultured cells. Contrary to the predictions, in both viruses, both proteins had their amino terminus, as well as their carboxy terminus, exposed in the cytoplasm. We established that two of the three hydrophobic domains in nsp3 and six of the seven in nsp6 are membrane spanning. Subsequently, we verified that in nsp4, all four hydrophobic domains span the lipid bilayer. The occurrence of conserved non-membrane-spanning hydrophobic domains in nsp3 and nsp6 suggests an important function for these domains in coronavirus replication.
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