Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.6.1.3 (ATPase)
 65,361 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

During the course of screening studies to identify inhibitors of intracellular protein trafficking, we isolated efrapeptins as active principles. These compounds arrested syncytium formation (SF) and cytopathic effect (CPE) in Newcastle disease virus (NDV)- and vesicular stomatitis virus (VSV)-infected BHK cells, respectively, without profoundly affecting glycoprotein synthesis. Efrapeptins blocked cell surface expression of NDV-HN and VSV-G glycoproteins, but did not suppress intoxication by ricin or diphtheria toxin even after prolonged pretreatment. Efrapeptins are inhibitors of F-ATPase, or ATP synthase, but their inhibitory effect on SF and CPE was independent of the amount of intracellular ATP.
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PMID:Efrapeptins block exocytic but not endocytic trafficking of proteins. 888 13

The nonapeptide leucinostatin A (LSA) inhibited syncytium formation without profoundly affecting HN glycoprotein synthesis in Newcastle disease virus (NDV)-infected BHK cells. At similar doses of LSA, cytopathic effect and infectious virus production were suppressed in vesicular stomatitis virus (VSV)-infected BHK cells. Blockade by LSA of cell surface expression of NDV-HN and VSV-G glycoproteins was demonstrated, accompanied by intracellular accumulation of these virus glycoproteins. LSA acts as an inhibitor of mitochondrial F-type H(+)-translocating ATPase, a key enzyme in the generation of ATP, but its action against cell surface expression of virus glycoproteins was independent of the depletion of intracellular ATP. LSA also acts as an ionophore, but its action on intoxication by ricin and diphtheria toxin was different from that of monensin. This novel action of LSA is expected to be useful in investigation of the mechanism of intracellular trafficking of proteins.
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PMID:Novel blockade of cell surface expression of virus glycoproteins by leucinostatin A. 898 41

Dawson, C. R. (The Middlesex Hospital Medical School, London, England), M. A. Epstein, and K. Hummeler. Cytochemical and electron microscopical observations on the presence and origin of adenosine triphosphatase-like activity at the surface of two myxoviruses. J. Bacteriol. 89:1526-1532. 1965.-HeLa cells infected with either fowl plague virus (FPV) or Newcastle disease virus (NDV) were examined in thin sections by electron microscopy. Preparations were studied both after direct fixation and embedding and after the application of cytochemical staining for enzymes splitting adenosine triphosphate. Viral particles were identified by their size and characteristic structure, and were found to form at the cell surface by budding out through structurally altered plasmalemma. After cytochemical staining for adenosine triphosphatase activity, extracellular FPV or NDV particles lying close against cell membranes with enzyme activity likewise carried this function, whereas those particles which were associated with cell surfaces without reaction product were themselves free from it. This correspondence between enzyme function in cell membranes and the outer viral membranes of newly formed particles adjacent to them indicates that surface enzymatic capability of the host cell survives even when the cell membrane undergoes morphological and antigenic alteration into myxovirus outer membrane.
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PMID:CYTOCHEMICAL AND ELECTRON MICROSCOPICAL OBSERVATIONS ON THE PRESENCE AND ORIGIN OF ADENOSINE TRIPHOSPHATASE-LIKE ACTIVITY AT THE SURFACE OF TWO MYXOVIRUSES. 1429 92

Sarco/endoplasmic reticulum calcium-ATPase (SERCA) is a membrane-bound cytosolic enzyme which is known to regulate the uptake of calcium into the sarco/endoplasmic reticulum. Herein, we demonstrate for the first time that SERCA can also regulate virus replication. Treatment of Vero cells with SERCA-specific inhibitor (Thapsigargin) at a concentration that is nontoxic to the cells significantly reduced Peste des petits ruminants virus (PPRV) and Newcastle disease virus (NDV) replication. Conversely, overexpression of SERCA rescued the inhibitory effect of Thapsigargin on virus replication. PPRV and NDV infection induced SERCA expression in Vero cells, which could be blocked by Thapsigargin. Besides inducing enhanced formation of cytoplasmic foci, Thapsigargin was shown to block viral entry into the target cells as well as synthesis of viral proteins. Furthermore, NDV was shown to acquire significant resistance to Thapsigargin upon long-term passage (P) in Vero cells. As compared to the P0 and P70-Control, the fusion (F) protein of P70-Thapsigargin virus exhibited a unique mutation at amino acid residue 104 (E104K), whereas no Thapsigargin-associated mutations were observed in HN gene. To the best of our knowledge, this is the first report describing the virus-supportive role of SERCA and a rare report suggesting that viruses may acquire resistance even in the presence of an inhibitor that targets a cellular factor.
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PMID:Inhibitor of Sarco/Endoplasmic Reticulum Calcium-ATPase Impairs Multiple Steps of Paramyxovirus Replication. 3081 86