M. Muroi et al., NOVEL BLOCKADE OF CELL-SURFACE EXPRESSION OF VIRUS GLYCOPROTEINS BY LEUCINOSTATIN-A, Journal of antibiotics, 49(11), 1996, pp. 1119-1126
The nonapeptide leucinostatin A (LSA) inhibited syncytium formation wi
thout profoundly affecting HN glycoprotein synthesis in Newcastle dise
ase virus (NDV)-infected BHK cells. At similar doses of LSA, cytopathi
c effect and infectious virus production were suppressed in vesicular
stomatitis virus (VSV)-infected BHK cells. Blockade by LSA of cell sur
face expression of NDV-HN and VSV-G glycoproteins was demonstrated, ac
companied by intracellular accumulation of these virus glycoproteins.
LSA acts as an inhibitor of mitochondrial F-type H+-translocating ATPa
se, a key enzyme in the generation of ATP, but its action against cell
surface expression of virus glycoproteins was independent of the depl
etion of intracellular ATP. LSA also acts as an ionophore, but its act
ion on intoxication by ricin and diphtheria toxin was different from t
hat of monensin. This novel action of LSA is expected to be useful in
investigation of the mechanism of intracellular trafficking of protein
s.