Proteomic analysis identifies intracellular targets for avian coronavirus NSP10.

Abstract

Avian coronavirus, also known as infectious bronchitis virus (IBV), is the causative agent of infectious bronchitis (IB). The non-structural proteins (NSPs) of IBV are critical for viral replication and for evading the host's immune response. The innate immune response serves as the first line of defense against viral infections. The IBV genome codes for 15 NSPs (NSP2-16). In this study, we identified host proteins interacting with IBV NSP10 using co-immunoprecipitation (Co-IP) and liquid chromatography-tandem mass spectrometry (LC/MS/MS). Proteomic analysis revealed that interactions of host proteins with NSP10 are involved in processes such as localization, transport, and metabolism, regulation of the cell cycle, and antiviral responses. We further explored the role of NSP10 in these immune and cellular regulation pathways and also confirmed the interaction between NSP10 and the host protein hnRNPA1. Further investigation showed that hnRNPA1 inhibited IBV replication. It is speculated that the binding of hnRNP A1 to NSP10 interferes with the function of the replication complex, thereby inhibiting virus replication. However, co-overexpression of NSP10 and hnRNP A1 partially restored viral replication, suggesting a complex relationship between these two proteins. These findings demonstrate that IBV NSP10 plays a significant role in viral infection and in modulating host cell processes, highlighting its potential as a target for therapeutic interventions.