Viral Infections and Their Ability to Modulate Endoplasmic Reticulum Stress Response Pathways.

In eukaryotic cells, the endoplasmic reticulum is particularly important in post-translational modification of proteins before they are released extracellularly or sent to another endomembrane system. The correct three-dimensional folding of most proteins occurs in the ER lumen, which has an oxidative environment that is essential for the formation of disulfide bridges, which are important in maintaining protein structure. The ER is a versatile organelle that ensures the correct structure of proteins and is essential in the synthesis of lipids and sterols, in addition to offering support in the maintenance of intracellular calcium.

Manipulation of unfolded protein response by zoonotic and .

The replicative success of vaccinia virus (VACV) depends on its ability to subvert host functions. Poxviruses multiplication and maturation are closely associated with the endoplasmic reticulum (ER) and its membranes. This organelle responds to disturbances caused by the accumulation of misfolded proteins, leading to processing of these proteins or even programmed cell death through the unfolded protein response (UPR).

Vaccinia virus induces endoplasmic reticulum stress and activates unfolded protein responses through the ATF6α transcription factor.

Background: Cell responses to different stress inducers are efficient mechanisms that prevent and fight the accumulation of harmful macromolecules in the cells and also reinforce the defenses of the host against pathogens. Vaccinia virus (VACV) is an enveloped, DNA virus, belonging to the Poxviridae family. Members of this family have evolved numerous strategies to manipulate host responses to stress controlling cell survival and enhancing their replicative success.