Host–Viral Protein Interactions and Post-translational Modifications in Viral Infections

Dear Colleagues,

Viruses need to engage host factors to infect, replicate and assemble new pathogens. Several genome-wide siRNA or CRISPR screening studies have also identified that host factors are critical for virus infection and growth. In addition, post-translation modifications (PTMs), such as phosphorylation, ubiquitylation and SUMOylation, have been discovered to be critical for many virus life cycles. For example, Ebola, CMV and EMCV utilize SUMOylation to inhibit anti-viral intrinsic and innate immunity via, e.g., reducing interferon production and inhibiting STAT1/3, PML, IRFs and NFkB. SARS-CoV-2 also inhibits the host IFN signaling pathway to repress the host immune response for its replication. Furthermore, many viral infections and replications can manipulate the host factors to ensure their propagation and survival. Herpes simplex virus-1 (HSV-1) infection results in a three-fold decrease in the modification of over 100 cellular proteins, including antiviral promyelocytic leukemia (PML) nuclear bodies. Therapeutics targeting host–virus interactions could potentially present a potential effective and broad-spectrum treatment modality for viruses such as COVID-19 and influenzas, as exemplified in the cases of methylprednisolone and rSIFN-co with even more potential benefits, such as an anti-coinfections effect. A comprehensive understanding of host–virus protein interactions and modifications in viral infection would significantly improve our knowledge and approaches against viral infections and novel therapeutic development.

Dr. Jiayu Liao
Guest Editor

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