A
virus minimally contains a
nucleic acid genome packaged by a
protein coat. The
genome and
capsid together are known as the
nucleocapsid, which has an envelope containing a
lipid bilayer (mainly
phospholipids) originating from host
cell membranes. The
viral envelope has transmembrane
proteins that are usually
glycoproteins. The
proteins in the envelope bind to host
cell receptors, promoting
membrane fusion and
viral entry into the
cell.
Virus-infected host
cells exhibit marked increases in
glutamine utilization and
metabolism.
Glutamine metabolism generates
ATP and precursors for the synthesis of macromolecules to assemble progeny
viruses. Some compounds derived from
glutamine are used in the synthesis of
purines and
pyrimidines. These latter compounds are precursors for the synthesis of
nucleotides. Inhibitors of
glutamine transport and
metabolism are potential candidate
antiviral drugs.
Glutamine is also an essential
nutrient for the functions of
leukocytes (
lymphocyte,
macrophage, and
neutrophil), including those in
virus-infected
patients. The increased
glutamine requirement for immune
cell functions occurs concomitantly with the high
glutamine utilization by host
cells in
virus-infected
patients. The development of
antiviral drugs that target
glutamine metabolism must then be specifically directed at
virus-infected host
cells to avoid negative effects on immune functions. Therefore, the aim of this
review was to describe the landscape of cellular
glutamine metabolism to search for potential candidates to inhibit
glutamine transport or
glutamine metabolism.