The ins and outs of virus trafficking through acidic Ca2+stores

Many viruses exploit host-cell Ca-2+ signaling processes throughout their life cycle. This is especially relevant for viruses that translocate through the endolysosomal system, where cellular infection is keyed to the microenvi-ronment of these acidic Ca-2+ stores and Ca-2+-dependent trafficking pathways. As regulators of the endolyso-somal ionic milieu and trafficking dynamics, two families of endolysosomal Ca-2+-permeable cation channels - two pore channels (TPCs) and transient receptor potential mucolipins (TRPMLs) - have emerged as important host-cell factors in viral entry. Here, we review: (i) current evidence implicating Ca-2+ signaling in viral trans-location through the endolysosomal system, (ii) the roles of these ion channels in supporting cellular infection by different viruses, and (iii) areas for future research that will help define the potential of TPC and TRPML ligands as progressible antiviral agents.

Automated summary

Many viruses manipulate the host-cell's calcium signaling processes. Particularly, the acidic calcium stores and calcium-dependent trafficking pathways in the endolysosomal system are crucial for viral infection. Two families of calcium-permeable ion channels, two pore channels (TPCs) and transient receptor potential mucolipins (TRPMLs), have been identified as important factors for viral entry into host cells. Further research is needed to explore the potential of TPC and TRPML ligands as antiviral agents.