There are four mammalian eIF2 kinases that phosphorylate eIF2α: general control non-derepressible 2 (GCN2), which is upregulated by amino acid starvation; protein kinase R (PKR), which is activated by viral infections; PKR-like endoplasmic reticulum (ER) kinase (PERK), which is upregulated by ER stress; and heme-regulated eIF2α kinase (HRI), which is induced upon oxidative stress or heme deprivation.3, 4, 5, 6 Phosphorylated eIF2α (p-eIF2α) markedly attenuates translation initiation and overall protein synthesis, allowing for conservation of cellular resources. This evidence concerns the gene EIF2A and viral infectious disease.