| Autor: |
Minh-Ha Nguyen, Palfy, Gyula, Fogeron, Marie-Laure, Pedrosa, Martí Ninot, Zehnder, Johannes, Rimal, Vaclav, Callon, Morgane, Lecoq, Lauriane, Barnes, Alexander, Meier, Beat H., Böckmann, Anja |
| Předmět: |
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| Zdroj: |
Proceedings of the National Academy of Sciences of the United States of America; 11/12/2024, Vol. 121 Issue 46, p1-10, 51p |
| Abstrakt: |
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 a-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. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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