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Query: UMLS:C0026936 (Mycoplasma)
 14,761 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Attachment of washed Mycoplasma gallisepticum cells to glass was quantified with organisms in which membrane lipids were labelled with 3H. Siliconization of the test tubes decreased attachment, while centrifugation increased it. Attachment increased with temperature, decreased with increasing pH and ionic strength of the attachment mixture, but was unaffected by Ca2+, Mg2+ and EDTA. This suggests that ionic bonds, but not salt bridges, participate in the attachment process. Glycophorin, the major receptor responsible for M. gallisepticum attachment to erythrocytes, partially inhibited the attachment of the organisms to glass. However, bovine serum albumin also decreased attachment. Extensive pretreatment of the organisms with trypsin decreased their ability to attach to glass by about 35 to 40%. Trypsin and pronase failed to detach the organisms already bound to glass, suggesting that external mycoplasma cell components, other than membrane proteins, also participate in attachment of the organisms to glass.
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PMID:Adherence of Mycoplasma gallisepticum to glass. 3 84

The human pathogen Mycoplasma pneumoniae adheres to a variety of cells, including erythrocytes. A hemadsorption technique was developed to quantitate adherence by photometric measurement of lysates of erythrocytes that attached to sheets of M. pneumoniae grown in cups of Linbro plates. Attachment of sheep erythrocytes (SE) increased with higher ionic strength, was unaffected by minor pH variations (6 to 9), and was blocked by anti-M. pneumoniae antiserum, but was not inhibited by a variety of sugars, amino acids, and bovine serum albumin. The reaction was time and temperature dependent. The temperature curve showed peaks at 14 and 28 degrees C with untreated SE but only one peak at about 38 degrees C with glutaraldehyde-treated SE. The temperature dependence indicated involvement of either metabolic or membrane activities in the binding process. Trypsin treatment of the M. pneumoniae sheet abolished adherence of SE but was only partially effective with human erythrocytes and noneffective with rabbit erythrocytes. The binding capacity of the mycoplasma cells for SE was restored by incubation in growth medium for 3 to 4 h; this restoration was inhibited by 10 mug of chloramphenicol per ml. Neuraminidase treatment of SE removed their attachment capacity but had no effect on attachment of rabbit erythrocytes and only a slight effect on attachment of human erythrocytes. Pretreatment of M. pneumoniae with neuraminic acid partially blocked the adherence of SE, whereas rabbit erythrocyte attachment was not affected. Attached SE could be detached by trypsin, but not by neuraminidase. For human and rabbit erythrocytes, the results suggest binding mechanisms other than the interaction between neuraminidase-sensitive receptors and protein-containing binding sites shown for SE.
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PMID:Adherence of erythrocytes to Mycoplasma pneumoniae. 3 34

Comparisons of liver histology and serum protein characteristics from cases of oedema syndrome and from poults with Mycoplasma meleagridis induced ascites revealed that the two conditions, though presenting grossly similar post mortem appearances, are different entities. Serum albumin concentrations, but not total serum protein levels, were markedly reduced in poults with M meleagridis induced ascites and in those with turkey syndrome 65. Poults which were infected with M meleagridis but which failed to develop either of these conditions had more normal serum protein characteristics. It is argued that M meleagridis induced ascites may be an acute manifestation of a pathological process of which TS65 is the chronic form. It is also suggested that low serum albumin concentrations may play a primary role in the pathogenesis of TS65.
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PMID:Turkey syndrome 65, oedema syndrome and Mycoplasma meleagridis. 4 71

Spiroplasma citri was cultured in three different media that supplied cholesterol and fatty acids from: (i) horse serum, (ii) pleuropneumonia-like organism (PPLO) serum fraction, or (iii) bovine serum albumin-fatty acid-cholesterol. The ability of PPLO serum fraction to support growth varied by lot number. Neither PPLO serum fraction nor the bovine serum albumin medium supported growth as well as the horse serum medium. Analysis of cholesterol, lipid phosphorus, and membrane protein showed the horse serum- and PPLO-grown cells to be indistinguishable, but the bovine serum albumin-grown cells were deficient in lipid phosphorus. The three cultures did not show markedly different fatty acid compositions, but, in all cases, the cultures preferentially incorporated palmitic acid and discriminated against linoleic acid. Cultures grown for different times from logarithmic growth through a degenerative phase showed relatively constant ratios of cholesterol/protein and lipid phosphorus/protein. Fatty acid composition was also relatively constant at the different stages. Adenosine triphosphatase and p-nitrophenyl phosphatase were mainly associated with the membrane, whereas reduced nicotinamide adenine dinucleotide oxidase was either readily removed or not associated with the membrane. The reduced nicotinamide adenine dinucleotide oxidase was inactivated at temperatures above 35 degrees C.
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PMID:Composition and enzyme activities of Spiroplasma citri membranes. 19 32

A phosphoglycolipid, presumably identical to glyceryl-phosphoryldiglycosyl diglyceride, is the main component of the membrane glycolipids of Mycoplasma mycoides subsp. capri. It is immunologically active. Anti-phosphoglycolipid antibodies were induced in rabbits by intravenous injection of the flocculated complexes of methylated bovine serum albumin with a mixture of the phosphoglycolipid and the auxiliary lipids, phosphatidyl-choline and cholesterol. The specificities of the antibodies directed against the phosphoglycolipid, are due to both the phosphate and carbohydrate moieties of the lipid molecule. Anti-phosphoglycolipid antibodies were detected in the sera of rabbits intravenously immunized with intact M. mycoides subsp. capri. The intravenous method of immunization was chosen in order to select for a response to surface antigenic determinants. Anti-phosphoglycolipid antibodies specifically reacted with intact organisms and isolated membranes of M. mycoides subsp. capri, as shown by complement fixation and agglutination tests. The antigenic determinants of the phosphoglycolipid are mainly located on the outer membrane surface. It is concluded that the antigenic determinants of the phosphoglycolipid in intact M. mycoides subsp. capri significantly contribute to the surface architecture of mycoplasma membranes.
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PMID:Localization of a phosphoglycolipid in Mycoplasma membranes using specific anti-lipid-antibodies. 33 35

Mycoplasma growth factors in bovine serum fraction were separated by Sephadex G150 column chromatography and density ultracentrifugation. The major growth factor of bovine serum fraction eluted from the Sephadex column in the void volume. Its growth-supporting activity was greatly enhanced by the presence of bovine serum albumin in the mycoplasma culture media. Other investigators had previously identified the major growth factor in serum as an alpha-lipoprotein. Although density ultracentrifugation revealed the presence of traces of a high-density lipoprotein in bovine serum fraction, another, less dense component, isolated by ultracentrifugation (component 3) and containing cholesterol, cholesteryl esters, free fatty acids, triglycerides, and protein, but no lipoprotein, exhibited considerably more growth-supporting activity than did the high-density lipoprotein, thus indicating that at least two mycoplasma species do not require intact serum lipoprotein for growth. Both the high-density lipoprotein and component 3 exhibited maximum activity only in the presence of bovine serum albumin. A chloroform extract containing component 3 lipids combined with bovine serum albumin to form an effective, partially defined, less complex substitute for serum in mycoplasma culture media.
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PMID:Mycoplasma growth factors in bovine serum fraction. 69 78

Phosphatidylglycerol is the main component (87%) of the membrane phospholipids of Mycoplasma hominis. It is immunologically active. Antibodies directed against phosphatidylglycerol were detected in rabbits intravenously immunised with native M. hominis or isolated M. hominis membranes. The intravenous method of immunisation was chosen in order to select for a response to surface antigenic determinants. Anti-phosphatidylglycerol antibodies were induced in rabbits by intravenously injecting the flocculated complexes of methylated bovine serum albumin and a phosphatidylglycerol/phosphatidylcholine/cholesterol mixture. These antibodies were specifically bound to intact M. hominis, as shown by complement fixation and Coombs tests. Native M. hominis were not agglutinated by anti-phosphatidylglycerol antibodies; but after partial digestion of the membrane proteins with Pronase, the mycoplasmas were heavily agglutinated by the anti-phosphatidylglycerol antibodies. The same amount of anti-phosphatidylglycerol antibodies was bound to intact M. hominis, containing 600 mug of phosphatidylglycerol as to 6 mug of phosphatidylglycerol in the optimal configurational arrangement of a mixed phosphatidylglycerol/phosphatidylcholine/cholesterol micelle. It is concluded that the major part of the phosphatidylglycerol in native M. hominis membranes is masked, probably by membrane proteins, and is not accessible to the anti-phosphatidylglycerol antibodies.
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PMID:Immunological studies on the localization of phosphatidylglycerol in the membranes of Mycoplasma hominis. 115 31

Groups of one-day-old turkeys were infected with two isolates of Mycoplasma meleagridis and one of M gallisepticum. The experiment was terminated at three weeks of age when the incidence of TS65 in the three groups were 32, 24 and 82 per cent respectively. The development of TS65 in the M meleagridis-infected groups was not accompanied by dramatic falls of serum albumin levels thus invalidating the hypothesis that low serum albumin concentration is a primary factor in the development of TS65.
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PMID:Experimental reproduction of turkey syndrome 65 with Mycoplasma meleagridis and M gallisepticum and associated changes in serum protein characteristics. 116 25

Mycoplasma canadense and Mycoplasma verecundum were cultured in a serum-free medium containing bovine serum albumin, cholesterol, oleic acid, and palmitic acid in order to avoid the addition of horse serum. Growth was detected by measurement of A640 and by colony formation. The level of growth attained in this medium was less than that obtained in the horse serum-supplemented media, but colonies retained their distinctive morphology.
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PMID:Conditions for growing Mycoplasma canadense and Mycoplasma verecundum in a serum-free medium. 220 60

During the course of investigating the growth and differentiation of opossum kidney cells in serum-free medium, it was observed that a mycoplasma contamination (M. hyorhinis) contributed to the spreading of cells. Contaminated cells, seeded on collagen-coated plates, spread out and grew to confluency in Dulbecco's modified eagle's medium/Ham's F12 nutrient mixture containing insulin, transferrin, sodium selenite, and bovine serum albumin fraction V. In addition, differentiated characteristics, including parathyroid hormone-inhibitable, sodium-dependent phosphate transport, were expressed by these cells grown in this medium. After the infection was eradicated, the contamination-free cells would not spread out and proliferate in the same serum-free medium as they had done in the presence of mycoplasma. Normal cellular development, however, was attained after cells were plated in serum-free medium that included fetuin. Cells once again spread out, grew to confluency, and were able to express their differentiated characteristics.
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PMID:Mycoplasma provides for the spreading of opossum kidney cells in a serum-free, defined medium. 247 76


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