Autophagy is a homeostatic process involved in the turnover or elimination of 
cytoplasmic components, damaged organelles, and protein aggregates via a 
lysosomal degradation mechanism. Autophagy also provides a mechanism of innate 
immunity, known as xenophagy, designed to protect cells from intracellular 
pathogens, but it may unfortunately be subverted to act as a pro-viral pathway 
facilitating the replication of certain viruses. Herpes simplex virus type I 
(HSV-1) is a neurotropic virus that remains latent in host neurons; it is the 
most common cause of sporadic viral encephalitis. Moreover, HSV-1 has been 
related to the pathogenesis of Alzheimer's disease. HSV-1 can modulate the 
autophagic process through a mechanism mediated by the viral protein ICP34.5. 
Here we report that HSV-1 induces a strong increase in GFP-LC3 and endogenous 
LC3 lipidation, and triggers the accumulation of intracellular autophagic 
compartments (mainly autophagosomes) without enhancing autophagic long-lived 
protein degradation in the late stages of infection. Autophagy inhibition 
mediated by ATG5 gene silencing had no effect on viral growth. The present 
results suggest that HSV-1 infection activates the host autophagic machinery and 
strongly controls the autophagic process, blocking the fusion of autophagosomes 
with lysosomes. These events might be important in the neurodegenerative process 
associated with HSV-1 infection.