Bacterial-host protein interactions: Exploitation of host ubiquitination by pathogens

Many intracellular pathogens have been identified that exploit host ubiquitination processes and thus alter the function and stability of bacteria or host protein. These bacteria pathogens utilize type III (T3SS) and type IV secretion systems (T4SS) to translocate effector proteins into the host cells. Various proteins have been identified that interact with components of the host ubiquitin-proteasome system (UPS). Studies in microbiology and molecular biology are present multiple lines of evidence demonstrating how bacterial pathogens exploit ubiquitin to enhance pathogenecity and virulence. Strategies utilized by bacteria include molecular mimicry and secretion of effectors to enhance bacterial proliferation. This review highlights multiple ways through which human bacterial pathogens exploit ubiquitination to manipulate the host defense system. This review also provides an overview of the structural and functional features of bacterial effector proteins that mimic eukaryotic E3 ubiquitin ligases and thus exploit host cell ubiquitination. Pathogens such as C. burnetti, L. pneumophila, and Salmonella have clearly demonstrated the achievement of spatial and temporal regulation of bacterial effector proteins using the ubiquitin-proteasome system. Data gathered to date clearly highlight that pathogenic bacteria stimulate host cells responses through induction of signaling events that directly engage the ubiquitin machinery within the targeted host cells.

کلیدواژه ها:

Pathogens ، Bacteria ، Salmonella ، Proteins ، Ubiquitin ،