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)

It was shown that infection of E. coli cells by phage T4 is suppressed, when the cells are treated by oxidative phosphorylation uncouplers. The inhibiting effects of the uncouplers manifest themselves at the stage of phage DNA entry into the cells. Study of the E. coli cells devoid of their H+-ATPase activity due to mutation showed that the infection is suppressed by a switch-off of the respiratory chain, the only generator of the proton motive force (PMF) in mutated cells. Infection of the E. coli cells containing intact H+-ATPase occured even in the case when the respiratory chain activity was inhibited. The kinetic studies showed that generation of PMF is necessary during phage DNA transport into the cells and is indispensable for phage DNA entry into bacterial cells.
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PMID:[Role of proton motive force in the infection of E. coli K-12 cells by bacteriophage T4]. 3 41

Infection of Escherichia coli with bacteriophage T7 results in an inhibition of the host exonuclease V (recB, C DNase) activity. This inhibition is not observed when cells are infected in the presence of chloramphenicol or with a gene 1 mutant. The protein responsible for the inhibition of exonuclease V has been partially purified from T7-infected cells. The protein which does not possess nuclease or ATPase activity can inhibit all nucleolytic activities associated with exonuclease V. The protein does not, however, inhibit the DNA-dependent ATPase activity associated with exonuclease V. The inhibitory protein has a molecular weight of about 12,000, as determined from sedimentation analysis in glycerol gradients.
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PMID:Partial purification and properties of a bacteriophage T7 inhibitor of the host exonuclease V activity. 12 51

Infection by bacteriophage T4 has previously been shown to cause a rapid inhibition of the host recBC DNase, an ATP-dependent DNase that is required for genetic recombination in Escherichia coli. We report here the partial purification of a protein ("T4 rec inhibitor") from extracts of T4-infected cells and some characteristics of the in vitro inhibition reaction with purified inhibitor and recBC nuclease. This inhibitory activity could not be purified from extracts of uninfected E. coli. Both the ATP-dependent exonuclease and DNA-dependent ATPase activities of recBC DNase are inhibited by T4 rec inhibitor. Experiments suggest that the inhibitor interacts with the nuclease in a stoichiometric manner. The biological significance of this inhibition is discussed with respect to control reactions in phage-infected cells.
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PMID:Postinfection control by bacteriophage T4 of Escherichia coli recBC nuclease activity. 13 May 1

Sarcomas were induced in CFW mice by the iv inoculation of simian virus 40 (SV40) in neonatal animals. Infection with murine malaria parasites, Plasmodium berghei yoelli, decreased the latency and increased the incidence and invasiveness of the tumors. All mice given both SV40 and P. berghei yoelli had sarcomas of the liver and spleen at 9 months of age. At 11 months of age, 70% of the SV40-inoculated mice had sarcomas of the liver indistinguishable from those in the group given both pathogens. Only 1 lung metastasis was seen in the SV40-treated group. The sarcomas contained SV40 T-antigen as revealed by the indirect immunofluorescence technique. Among adult CFW mice given iv injections of SV40, only 2 tumors were found at 11 or 12 months after virus inoculation. Both tumors were in the lungs; 1 was an adenoma and 1 was a papillary adenocarcinoma. Neither gave a positive reaction with the immunofluorescence test.
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PMID:Sarcomas induced by injection of simian virus 40 into neonatal CFW mice. 22 3

The functional properties of the early antigens of simian virus 40 (SV40) and human papovavirus BK (BKV) were investigated. Infection of African green monkey kidney cells with BKV permitted the bidirectional replication of an early temperature-sensitive mutant (tsA) at a nonpermissive temperature. Conceivably, an early gene product (T-antigen) of BKV can substitute functionally for the defective SV40 T-antigen. On the other hand, SV40 DNA replication remained undetectable in human embryonic kidney cells preinfected with BKV, suggesting that BKV early antigens alone are not sufficient to provide for the replication of SV40. Preinfection of African green monkey kidney cells with BKV restored the normal pattern of late lytic SV40 transcription, suppressing the overproduction of early RNA by an SV40 tsA mutant at the nonpermissive temperature. Furthermore, preinfection of African green monkey kidney cells with BKV supported the growth of adenovirus type 2, providing a "helper function" similar to that provided by SV40 for the growth of human adenovirus in monkey kidney cells.
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PMID:Functional similarity between the early antigens of simian virus 40 and human papovavirus BK. 22 12

Infection of MA-104 cells with the OSU strain of rotavirus induced an increase in Na+ and a decrease in K+ intracellular concentrations, starting at 4 h post-infection. These changes were not related to an inhibition of the Na+/K+ pump since ouabain-sensitive 86Rb uptake was augmented in rotavirus-infected cells compared to control cells, whereas the [3H]ouabain binding and Na+/K+ ATPase activity in the cell homogenate were unaffected. Furosemide-sensitive 86Rb uptake (Na+/K+/2Cl- cotransport) was not modified by the infection. Passive 86Rb efflux and 22Na influx were augmented in infected cells suggesting an increase in the plasma membrane permeability. The increase in intracellular Na+ concentration might be responsible for the observed stimulation of the Na+/K+ pump. This effect was dependent upon the synthesis of viral proteins because it was abolished by addition of cycloheximide up to 4 h post-infection. Prevention of the increase in intracellular Na+ by the use of low Na(+)-containing media did not modify the pattern of protein synthesis. This suggests that changes in intracellular Na+ and K+ concentrations were not related to shutoff of cellular protein synthesis. Alterations of ion contents in the rotavirus-infected enterocytes might impair intestinal absorptive capacity before the appearance of histopathological lesions.
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PMID:Rotavirus infection alters Na+ and K+ homeostasis in MA-104 cells. 184 90

Infection of Vero cells with Tacaribe virus stocks containing a high ratio of standard (plaque-forming) viruses to defective interfering particles (DIP) induced inhibition of the host cell Ca2+ ATPase (Ca2+ pump) and the ouabain-sensitive Na+/K+ ATPase (Na+/K+ pump). The Mg2+ ATPase which is not involved in cation transport was not affected. The presence of DIP in the inocula protected the cells from alteration of the transport-associated ATPases induced by standard viruses.
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PMID:Tacaribe virus infection may induce inhibition of the activity of the host cell Ca2+ and Na+/K+ pumps. 283 72

Infection of cells with herpes simplex virus type 1 (HSV-1) induces high levels of deoxypyrimidine triphosphatase. The majority of the enzyme activity is found in infected cell nuclei. A similar activity is induced by HSV type 2 (HSV-2) which, in contrast to the HSV-1 enzyme, fractionates to more than 99% in the soluble cytoplasmic extract. Of a series of temperature-sensitive mutants of HSV-1 studied, only the immediate-early mutants in complementation group 1-2 (strain 17 mutants tsD and tsK and strain KOS mutant tsB2) induced reduced levels of triphosphatase at nonpermissive temperature. Of a series of temperature-sensitive mutants of HSV-2 strain HG52, ts9 and ts13 failed to induce wild-type levels of the enzyme at nonpermissive temperature; ts9 was the most defective mutant with regard to triphosphatase expression of both herpes simplex virus serotypes. After shift-up from permissive to nonpermissive temperature, triphosphatase activity in cells infected with ts9 decreased rapidly, whereas all other mutants continued to exhibit enzyme levels comparable with controls kept at the permissive temperature. The type 1-specific nuclear expression of the triphosphatase was mapped physically by the use of HSV-1 x HSV-2 intertypic recombinants, based on enzyme levels different by more than two orders of magnitude found in nuclei of HSV-1- and HSV-2-infected cells. The locus for the type-specific expression maps between 0.67 and 0.68 fractional length on the HSV genome.
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PMID:Control of expression of the herpes simplex virus-induced deoxypyrimidine triphosphatase in cells infected with mutants of herpes simplex virus types 1 and 2 and intertypic recombinants. 612 30

Infection of golden hamsters with Ancylostoma ceylanicum caused significant decrease in body weight, liver weight and the protein content of liver plasma membrane. Significant inhibition of liver plasma membrane enzymes activities-5'Nucleotidase, gamma-glutamyl transpeptidase, NADHK3Fe (CN)6 reductase, Na+/K(+)-ATPase, CA(2+)-ATPase and Mg(2+)-ATPase was observed in infected animals compared to corresponding controls. Sialic acid content and phospholipid/cholesterol ratio in liver plasma membrane of the infected group were significantly reduced. The study suggests that changes in both the structural and functional organization of membrane may be a biochemical basis of the hepatotoxic effects.
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PMID:Liver plasma membrane-bound enzymes and lipids in golden hamsters infected with Ancylostoma ceylanicum. 791 86

Infection of cultured vertebrate cells by Sindbis virus, an alphavirus, results in a reduction in the overall rate of protein synthesis and in selective termination (shutoff) of host-specified protein synthesis. The shutoff of host protein synthesis by Sindbis virus has been temporally correlated with a decrease in intracellular K+ concentration (and an increase in intracellular Na+ concentration) which occurs as a consequence of virus-mediated inhibition of the plasma membrane-associated Na+/K+ ATPase. Incubation of Sindbis virus-infected cells in medium containing an elevated concentration of K+ resulted in an increase in the intracellular concentration of K+, an increase in the overall rate of protein synthesis, and in partial reversal of the virus-induced termination of cell-specified protein synthesis. These results suggest that the virus-induced decrease in intracellular K+ concentration is required for efficient shutoff of host protein synthesis by Sindbis virus.
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PMID:Sindbis virus-induced inhibition of protein synthesis is partially reversed by medium containing an elevated potassium concentration. 811 64


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