Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:1.2.1.13 (glyceraldehyde-3-phosphate dehydrogenase)
6,511 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

8 male patients (age 65-82 years) suffering from bacterial pneumonia or erysipelas were subjected to skeletal muscle biopsies. Significantly lower activities of lactate dehydrogenase (LDH) and glyceraldehyde-3-phosphate dehydrogenase (TPD) of skeletal muscle were recorded in the acute phase of the illness as compared to after the end of the convalescent phase. For citrate synthetase (CS) a similar although non-significant tendency was observed, while cytochrome c oxidase (CYTOX) was not altered by infection. Similar results have been reported in young patients with viral and mycoplasma infections. In the old patients the activity of LDH was approximately half of that found in the young patients (and in young controls confined to bed) on all occasions of measurement.
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PMID:Human skeletal muscle in bacterial infection: enzyme activities and their relationship to age. 19 74

We report the establishment of a phylogenetic relationship between the sterol-nonrequiring mycoplasmas (Acholeplasma species) and streptococci. Three specific antisera prepared against purified Streptococcus faecalis fructose diphosphate aldolase and glyceraldehyde-3-phosphate dehydrogenase and Pediococcus cerevisiae glyceraldehyde-3-phosphate dehydrogenase were used for comparative enzyme immunological studies; the Ouchterlony double-diffusion technique and the quantitative microcomplement fixation procedure were employed. The reactions obtained provide evidence showing that all seven ACholeplasma species studied (A. laidlawii, A. granularum, A. modicum, A. oculi, A. axanthum. A. hippikon, and A. equifetale) are phylogenetically related to streptococci and that they evolved from streptococci. The data strongly suggest that the acholeplasmas comprise a distinct evolutionary group that has diverged from streptococci belonging to Lancefield group D or N. No reactions were observed between these enzyme antisera and cell extracts from six fermentative Mycoplasma species. These results support the view that mycoplasmas are derived from various bacteria.
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PMID:Origins of the mycoplasmas: sterol-nonrequiring mycoplasmas evolved from streptococci. 617 74

A summary of a survey of three genera of mycoplasmatales (Mycoplasma, Acholeplasma, and Ureaplasma) for isozyme expression is presented. Isozyme analysis of mycoplasmas has been employed in at least three distinct areas: (1) as genetic markers for identification, individualization, and taxonomic classification; (2) as markers for cell culture contamination; and (3) as a qualitative measure of the operative metabolic pathways in the diverse species. We have found five ubiquitous enzymes: purine nucleoside phosphorylase, adenylate kinase, inorganic pyrophosphatase, dipeptidase, and esterase. Three enzymes, glucose-6-phosphate dehydrogenase, phosphogluconate dehydrogenase, and superoxide dismutase, were restricted to Acholeplasma species and were not detected in Mycoplasma or Ureaplasma. Four glycolytic enzymes, glucose phosphate isomerase, triose phosphate isomerase, glyceraldehyde-3-phosphate dehydrogenase, and lactate dehydrogenase, were restricted to those species of Mycoplasma and Acholeplasma capable of glucose fermentation. Two of these glycolytic enzymes, glucose phosphate isomerase and lactate dehydrogenase, were detected in serovars I and II of U. urealyticum, which is inconsistent with the non-glycolytic activity in this genus.
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PMID:On the distribution and characteristics of isozyme expression in Mycoplasma, Acholeplasma, and Ureaplasma species. 667 51

Crude extracts of triple-cloned, purified cultures of 22 species of Mycoplasma and Acholeplasma were examined for expression of 21 isozyme systems routinely used to type mammalian cells. Nine previously described enzymes (purine nucleoside phosphorylase, adenylate kinase, dipeptidase, esterase, glyceraldehyde-3-phosphate dehydrogenase, glucose phosphate isomerase, glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, and superoxide dismutase) and three enzymes not previously reported in mycoplasma (triose phosphate isomerase, inorganic pyrophosphatase, and acid phosphatase) were detected in some or all of the species examined. These findings provide new information on the enzymatic expressions of these organisms. Three of the isozyme systems (superoxide dismutase, glucose-6-phosphate dehydrogenase, and 6-phosphogluconate dehydrogenase) were present in Acholeplasma species but not in any Mycoplasma species. The characteristic pattern of electrophoretic mobility of the 12 isozyme systems also provides a useful biochemical property for identification, characterization, and classification of these mycoplasmas. Mycoplasma isozyme expression for seven of the enzymes were readily detected in various infected-cell culture lines by using either cell extracts or concentrated cell culture fluids. Mycoplasma-specific enzymes found in infected-cell extracts had the same electrophoretic mobility patterns as enzymes obtained from broth-grown mycoplasmas of the same species. Expression of homologous mammalian enzymes was not detectably altered by infection with mycoplasmas.
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PMID:Analysis of multiple isoenzyme expression among twenty-two species of Mycoplasma and Acholeplasma. 721 1

Specific regions of adherence binding sites and epitopes of the P1 adhesin of Mycoplasma pneumoniae were synthesised as octapeptides and used as targets in a modified enzyme-linked immunosorbent assay. Acute phase and convalescent sera from 10 patients with M. pneumoniae infection were tested for antibody reactivity to these octapeptides. In convalescent sera, antibody activities were directed against octapeptides of the epitope regions, whereas no antibody activity was found in acute or convalescent sera to octapeptides of adherence-mediating binding sites could be explained partially from the results of cross-reactivity experiments with adherence-inhibiting anti-P1 adhesin monoclonal antibodies (MAbs). Two of these MAbs showed cross-reactions with intracellular antigens of eukaryotic cell lines in immunofluorescence microscopy experiments. The cross-reacting antigens were isolated and characterised as glyceraldehyde-3-phosphate dehydrogenase and 2-phospho-D-glycerate hydrolyase. Antigenic mimicry of eukaryotic structures by functional sites of the P1 adhesin of M. pneumoniae may influence the pathogenesis of M. pneumoniae infection.
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PMID:Molecular mimicry by Mycoplasma pneumoniae to evade the induction of adherence inhibiting antibodies. 747 75

Mycoplasma hominis has been previously described as a heterogeneous species, and in the present study intraspecies diversity of 20 M. hominis isolates from different individuals was analyzed using parts of the unlinked gyrase B (gyrB), elongation factor Tu (tuf), SRalpha homolog (ftsY), hitB-hitL, excinuclease ABC subunit A (uvrA) and glyceraldehyde-3-phosphate dehydrogenase (gap) genes. The level of variability of these M. hominis genes was low compared with the housekeeping genes from Helicobacter pylori and Neisseria meningitidis, but only few M. hominis isolates had identical sequences in all genes indicating the presence of recombination. In order to test for intergenic recombination, phylogenetic trees were reconstructed for each of the genes but no well-supported bifurcating phylogenetic trees could be obtained. The genes were tested for intragenic recombination using the correlation between linkage disequilibrium and distance between the segregating sites, by the homoplasy ratio (H ratio), and by compatibility matrices. The gap gene showed well-supported evidence for high levels of recombination, whereas recombination was less frequent and not significant within the other genes. The analysis revealed intergenic and intragenic recombination in M. hominis and this may explain the high intraspecies variability. The results obtained in the present study may be of importance for future population studies of Mycoplasma species.
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PMID:Recombination in Mycoplasma hominis. 1279 6

Mycoplasma genitalium is known to cause nonchlamydial, nongonococcal urethritis in men and to be associated with pelvic inflammatory disease in women. Specific and sensitive PCR methods are needed for diagnosis of this bacterium because it is very difficult to culture from patient samples. To determine the bacterial load in patients' specimens, a quantitative real-time LightCycler PCR was developed. The housekeeping gene gap encoding glyceraldehyde-3-phosphate dehydrogenase was chosen as the target gene. The assay could consistently detect five genome copies per reaction. To evaluate the PCR, we tested 246 selected urethral swab samples from men attending a clinic for sexually transmitted diseases. Eighty-two of the samples were found positive for M. genitalium by a conventional 16S rRNA gene PCR assay, whereas 164 samples were randomly chosen among those tested negative. Of the positive samples, 78 (95.1%) were found positive, whereas 6 (3.7%) of the negatives were found positive by the LightCycler assay. The patient samples were also tested with a quantitative TaqMan assay, and the bacterial load was compared to the LightCycler results. A good linear correlation between the LightCycler and the TaqMan assays was found with a correlation coefficient of 0.89 and a slope of 0.99. Significantly more M. genitalium-positive men had urethritis, discharge, and dysuria than had M. genitalium-negative men. The M. genitalium DNA load in samples from patients with urethritis was significantly higher than in samples from those without (61 and 2.9 copies/microl, respectively [P = 0.0005]). This assay may prove useful in the monitoring of treatment and for optimizing sample preparation methods.
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PMID:Development of a quantitative real-time PCR assay for detection of Mycoplasma genitalium. 1600 Apr 23

Mycoplasma suis is a member of the group of uncultivable haemoplasmas which colonise erythrocytes of a wide range of vertebrates. Adhesion to erythrocytes is the crucial step in the unique haemoplasma life cycle. Due to the lack of a cultivation system, no adhesion structures have been identified so far. In order to determine potential adhesion molecules of M. suis, we screened genomic M. suis libraries. The protein MSG1 with glyceraldehyde-3-phosphate dehydrogenase (GAPDH) similarity was identified. The encoding gene msg1 is 1011bp in size. The overall homology of the deduced amino acid sequence to GAPDHs of other pathogenic mycoplasmas ranged from 52.6% to 54.5%. Recombinant MSG1 expressed in Escherichia coli exhibited GAPDH activity. Immunoblot and immunoelectron microscopy analyses using antibodies against rMSG1 verified the membrane and surface localisation of native MSG1 in M. suis. Furthermore, we showed that rMSG1 binds to erythrocyte lysate in a dose-dependent manner. E. coli transformants which express MSG1 on their surface acquire the ability to adhere to porcine erythrocytes. This adhesion could be specifically and significantly inhibited by rMSG1 and antibodies to MSG1. In conclusion, our studies indicate that the membrane-associated MSG1 represents the first putative adhesion protein identified in the group of haemoplasmas.
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PMID:MSG1, a surface-localised protein of Mycoplasma suis is involved in the adhesion to erythrocytes. 1733 68

Diseases caused by Mycoplasma bovis are an important source of financial losses for beef and dairy cattle producers. Antigenic variation in M. bovis hinders the production of effective vaccines and although there are few vaccines available, they are prepared from bacteria obtained from few isolates potentially limiting their effectiveness. Thus, to develop a vaccine that protects against all M. bovis isolates, it is necessary to use a common antigen that shows less or no antigenic variation. We have isolated the gap gene of M. bovis encoding for glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and showed that cattle colonized with M. bovis were able to mount an immune response to GAPDH. Using restriction-fragment length polymorphism (RFLP) of several M. bovis gap genes amplified by PCR, we were able to detect small intragenic variations that allowed us to classify the genes into two groups without changing the antigenic makeup of the proteins. The immune responses detected in cattle combined with the antigenic conservation of the proteins suggest that the M. bovis GAPDH protein could be a potential target for development of a more effective vaccine against all M. bovis isolates.
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PMID:Detection of antibodies against the Mycoplasma bovis glyceraldehyde-3-phosphate dehydrogenase protein in beef cattle. 1768 21

The objective of the current study was to determine the sensitivity and specificity of real-time polymerase chain reaction (real-time PCR) for feline hemoplasmas when applied to DNA extracted from dried whole-blood smears in comparison to that for DNA extracted from liquid whole blood. Blood samples were collected into ethylenediamine tetra-acetic acid tubes from 305 cats with possible or suspected hemoplasmosis, and dried blood smears from each sample were prepared. DNA was extracted from blood smears and a 160-microl aliquot of each liquid blood sample by using a robotic extractor and was subjected to real-time PCR for feline glyceraldehyde-3-phosphate dehydrogenase (liquid blood), 18S ribosomal RNA (dried blood), and "Candidatus Mycoplasma haemominutum", Mycoplasma haemofelis, and "Candidatus Mycoplasma turicensis" DNA. When using the results for liquid whole blood as the gold standard, the sensitivity of each assay for "Ca. M. haemominutum", M. haemofelis, and "Ca. M. turicensis" was 49 of 66 (74%), 11 of 13 (85%), and 11 of 20 (55%), respectively. The specificity of each assay was 224 of 234 (96%), 287 of 287 (100%), and 280 of 280 (100%), respectively. When possible, liquid blood samples should be submitted for detection of feline hemoplasmas by using real-time PCR. The improved sensitivity of real-time PCR on blood smears for M. haemofelis compared with that of the other hemoplasma species may reflect the higher organism burdens associated with infection with this species.
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PMID:Use of dried blood smears for detection of feline hemoplasmas using real-time polymerase chain reaction. 1877 95


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