Viral hijacking mechanism in humans through protein-protein interactions

Adv Protein Chem Struct Biol. 2022:131:261-276. doi: 10.1016/bs.apcsb.2022.05.001. Epub 2022 Jun 2.

Abstract

Numerous viruses have evolved mechanisms to inhibit or alter the host cell's apoptotic response as part of their coevolution with their hosts. The analysis of virus-host protein interactions require an in-depth understanding of both the viral and host protein structures and repertoires, as well as evolutionary mechanisms and pertinent biological facts. Throughout the course of a viral infection, there is constant battle for binding between virus and cellular proteins. Exogenous interfaces facilitating viral-host interactions are well known for constantly targeting and suppressing endogenous interfaces mediating intraspecific interactions, such as viral-viral and host-host connections. In these interactions, the protein-protein interactions (PPIs), are mostly shown as networks (protein interaction networks, PINs), with proteins represented as nodes and their interactions represented as edges. Host proteins with a higher degree of connectivity are more likely to interact with viral proteins. Due to technical advancements, three-dimensional interactions may now be visualized computationally utilizing molecular modeling and cryo-EM approaches. The uniqueness of viral domain repertoires, their evolution, and their activities during viral infection make viruses fascinating models for research. This chapter aims to provide readers a complete picture of the viral hijacking mechanism in protein-protein interactions.

Keywords: COVID-19; Hijacking; Protein–protein interactions; SARS-CoV-2; Spike; Viral entry.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Host Microbial Interactions*
  • Humans
  • Viral Proteins* / chemistry

Substances

  • Viral Proteins