Analysis of the structure and interactions of the SARS-CoV-2 ORF7b accessory protein

SARS-CoV-2 carries a sizeable number of proteins that are accessory to replication but may be essential for virus-host interactions and modulation of the host immune response. Here, we investigated the structure and interactions of the largely unknown ORF7b, a small membranous accessory membrane protein of SARS-CoV-2. We show that structural predictions indicate a transmembrane (TM) leucine zipper for ORF7b, and experimentally confirm the predominantly α-helical secondary structure within a phospholipid membrane mimetic by solid-state NMR. We also show that ORF7b forms heterogeneous higher-order multimers. We determined ORF7b interactions with cellular TM leucine zipper proteins using both biochemical and NMR approaches, providing evidence for ORF7b interaction with the TM domains of E-cadherin, as well as phospholamban. Our results place ORF7b as a hypothetical interferer in cellular processes that utilize leucine zipper motifs in transmembrane multimerization domains.

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Publication Details

Journal
Proceedings of the National Academy of Sciences
Published
2024-11-07
DOI
https://doi.org/10.1073/pnas.2407731121
Citations
8
Primary Topic
SARS-CoV-2 and COVID-19 Research
Type
article
Field-Weighted Citation Impact
3.11

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article

Analysis of the structure and interactions of the SARS-CoV-2 ORF7b accessory protein

Lauriane Lecoq, Anja Böckmann, Václav Římal, Morgane Callon et al.
8 citations
Proceedings of the National Academy of Sciences
SARS-CoV-2 and COVID-19 Research
3.11
article

Analysis of the structure and interactions of the SARS-CoV-2 ORF7b accessory protein

Lauriane Lecoq, Anja Böckmann, Václav Římal, Morgane Callon, Gyula Pálfy, Martí Ninot‐Pedrosa, Marie‐Laure Fogeron, Beat H. Meier, Alexander B. Barnes, Johannes Zehnder, Minh-Ha Nguyen
article en
8 citations

Abstract

SARS-CoV-2 carries a sizeable number of proteins that are accessory to replication but may be essential for virus-host interactions and modulation of the host immune response. Here, we investigated the structure and interactions of the largely unknown ORF7b, a small membranous accessory membrane protein of SARS-CoV-2. We show that structural predictions indicate a transmembrane (TM) leucine zipper for ORF7b, and experimentally confirm the predominantly α-helical secondary structure within a phospholipid membrane mimetic by solid-state NMR. We also show that ORF7b forms heterogeneous higher-order multimers. We determined ORF7b interactions with cellular TM leucine zipper proteins using both biochemical and NMR approaches, providing evidence for ORF7b interaction with the TM domains of E-cadherin, as well as phospholamban. Our results place ORF7b as a hypothetical interferer in cellular processes that utilize leucine zipper motifs in transmembrane multimerization domains.

Proceedings of the National Academy of SciencesVol. 121(46)
Université Claude Bernard Lyon 1 (FR), Centre National de la Recherche Scientifique (FR), Board of the Swiss Federal Institutes of Technology (CH), ETH Zurich (CH)
National Science Foundation, Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung
Openalex Percentile: Top 8%
SARS-CoV-2 and COVID-19 Research
3.11
DOIOpen Access PDFOpenAlex
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