Abstract
Mitochondria are multifunctional organelles with diverse roles including energy production and distribution, apoptosis, eliciting host immune response, and causing diseases and aging. Mitochondria-mediated immune responses might be an evolutionary adaptation by which mitochondria might have prevented the entry of invading microorganisms thus establishing them as an integral part of the cell. This makes them a target for all the invading pathogens including viruses. Viruses either induce or inhibit various mitochondrial processes in a highly specific manner so that they can replicate and produce progeny. Some viruses encode the Bcl2 homologues to counter the proapoptotic functions of the cellular and mitochondrial proteins. Others modulate the permeability transition pore and either prevent or induce the release of the apoptotic proteins from the mitochondria. Viruses like Herpes simplex virus 1 deplete the host mitochondrial DNA and some, like human immunodeficiency virus, hijack the host mitochondrial proteins to function fully inside the host cell. All these processes involve the participation of cellular proteins, mitochondrial proteins, and virus specific proteins. This review will summarize the strategies employed by viruses to utilize cellular mitochondria for successful multiplication and production of progeny virus.
Highlights
IntroductionThe p7 protein of hepatitis C virus (HCV) forms porin-like structures [65] and causes Ca2+ influx to cytoplasm from storage organelles [66]
The R (Vpr) protein of human immunodeficiency virus (HIV), a small accessory protein, localizes to the mitochondria, interacts with adenine nucleotide translocase (ANT), modulates mitochondrial permeability transition pores (MPTP), and induces loss of membrane potential (MMP) promoting release of Cyto C [137] leading to cell death [138, 139]
The PB1-F2 protein of influenza A viruses localizes to the mitochondria [147,148,149,150] and interacts with VDAC1 and ANT3 [151] resulting in decreased MMP, which induces the release of proapoptotic proteins causing cell death
Summary
The p7 protein of HCV forms porin-like structures [65] and causes Ca2+ influx to cytoplasm from storage organelles [66] These HCV proteins disturb the Ca2+ homeostasis at different stages of the infection and help to enhance the survival of the cell. The NSP4 protein of rotavirus increases the cytosolic Ca2+ concentration by activation of phospholipase C (PLC) and the resultant ER Ca2+ depletion through IP3R [73, 74] This alteration in Ca2+ homeostasis has been attributed to an increase in the permeability of cell membrane [75]. A decrease in mitochondrial and other storage organelles (ER and golgi) Ca2+ levels causes an increase in cytosolic Ca2+ concentration, leading to the formation of vesicles and cell death, assisting in virus release [81, 84, 85]. The 6.7K protein encoded by E3 region of HAdV-2 localizes to ER and helps maintain ER Ca2+ homeostasis in transfected cells, inhibiting apoptosis [89]
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