Abstract
The influenza A virus (IAV), a member of the Orthomyxoviridae family, is a highly transmissible respiratory pathogen and represents a continued threat to global health with considerable economic and social impact. IAV is a zoonotic virus that comprises a plethora of strains with different pathogenic profiles. The different outcomes of viral pathogenesis are dependent on the engagement between the virus and the host cellular protein interaction network. The interactions may facilitate virus hijacking of host molecular machinery to fulfill the viral life cycle or trigger host immune defense to eliminate the virus. In recent years, much effort has been made to discover the virus–host protein interactions and understand the underlying mechanisms. In this paper, we review the recent advances in our understanding of IAV–host interactions and how these interactions contribute to host defense and viral pathogenesis.
Highlights
Influenza A virus (IAV) is a human respiratory pathogen that causes seasonal epidemics and occasional global pandemics with devastating levels of morbidity and mortality [1,2,3,4]
Each RNA segment is associated with multiple copies of nucleoproteins (NP) and a small number of heterotrimeric RNA-dependent RNA polymerase complexes that comprise polymerase acidic (PA), polymerase basic 1 (PB1) and polymerase basic 2 (PB2), which together form the ribonucleoprotein complex (RNP)
This review focuses on recent advances of the interactions between IAV proteins and host cellular factors
Summary
Influenza A virus (IAV) is a human respiratory pathogen that causes seasonal epidemics and occasional global pandemics with devastating levels of morbidity and mortality [1,2,3,4]. NS1 has been extensively studied in recent years due to its multifunctional trait [1,2,3,4,7], which involves host innate immune defense, host and viral mRNA expression, apoptosis, viral RNA splicing and morphogenesis Most of these NS1 functions are dependent on the protein interaction with host factors. The M1 protein of IAV mediates nuclear export of viral ribonucleoproteins [71], inhibits viral transcription [72,73], participates virus assembly and budding [74], and modulates host defense [75]. NP exploits cellular factors through protein interaction to promote viral replication and suppress host innate immune response. PB1-F2 binds to the mitochondrial antiviral signaling protein (MAVS), the key molecule on mitochondria of RIG-I signaling pathway and reduces mitochondrial membrane potential [113,114], indirectly inhibiting viral RNA-activated RIG-I signaling pathway
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
