Our research focuses on the multifaceted roles of the SARS-CoV-2 nucleocapsid (N) protein, a central player in the viral replication cycle and host-virus interactions. The N protein is essential for viral RNA packaging, genome stability, and replication, as well as the regulation of host immune responses. Its ability to bind and modulate viral RNA is key to the proper assembly and functioning of the viral genome. The N protein is composed of structured domains, including the RNA-binding domain (RBD) and C-terminal domain (CTD), along with several intrinsically disordered regions (IDRs) that contribute to its functional diversity.
A major aspect of our research involves investigating the molecular mechanisms by which the N protein interacts with RNA and host cell components. We aim to characterize the specific domains responsible for RNA binding and explore how these interactions are regulated, including the role of post-translational modifications such as phosphorylation.
In addition to RNA interactions, the N protein has been implicated in interactions with host cell surface components. These interactions suggest that the N protein may modulate host immune responses, potentially interfering with immune cell recruitment and cytokine signaling. Understanding these interactions is essential for unraveling how SARS-CoV-2 evades immune detection and exacerbates inflammatory responses in infected individuals.
The overall goal of our research is to identify novel therapeutic targets by screening for small molecules that could disrupt key interactions between the N protein, RNA, and host cell components. We focus on identifying inhibitors that could block the N protein's RNA binding activity or prevent its interactions with the host cell surface. These inhibitors could pave the way for the development of antiviral drugs that specifically target the N protein, offering a potential strategy for combating SARS-CoV-2 and other coronaviruses.
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