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

• DOI: 10.1073/pnas.2407731121
• Publication Date: 2024-11-07T15:21:24Z
• Authors: Minh-Ha Nguyen; Gyula Palfy; Marie-Laure Fogeron; Martí Ninot Pedrosa; Johannes Zehnder; Vaclav Rimal; Morgane Callon; Lauriane Lecoq; Alexander Barnes; Beat H. Meier; Anja Böckmann
• Keywords: Sars virus; 2019-20 coronavirus outbreak

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