Selective Autophagy Mediated by Protein Ubiquitination in Major Prevalent Zoonoses

Abstract

Zoonotic diseases not only cause great harm to animal health but also involve the development of animal husbandry, which in turn endangers human life and health and public health safety. Protein ubiquitination and autophagy are important ways for the body to degrade invading pathogens, which correspond to the ubiquitin (Ub)-proteasome system (UPS) and autophagic lysosomal pathway (ALP), respectively, and play an important role in the occurrence and development of diseases. For UPS, the substrate is delivered to the 26S proteasome system via a ubiquitination cascade and subsequently degraded and removed. For ALP, the substrate is encapsulated to form autophagosomes, which subsequently fuse with lysosomes to form autophagolysosomes, which are eventually degraded and cleared. However, a variety of zoonotic pathogens can interfere with the protein ubiquitination pathway and autophagy process to promote self-replication and survival, and resist host immune defense. This article reviews the mechanisms by which multiple pathogens interfere with protein degradation pathways, providing a new perspective for the treatment and prevention of zoonotic diseases.