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

Convalescent sera from proven cases of infection with Mycoplasma pneumoniae, and rabbit antisera to M. pneumoniae and to human erythrocyte glycoprotein contained cold hemagglutinins which were reactive only for human erythrocytes. Only the human serum cold agglutinins were inhibited by soluble integral glycoproteins derived from human erythrocyte ghosts by treatment with chloroform-methanol. Rabbit antiserum to chloroform-methanol glycoprotein, as well as to M. pneumoniae, fixed complement with either M. pneumoniae or chloroform-methanol glycoprotein antigens. The findings support the hypothesis that the cold agglutinins elicited by M. pneumoniae infection represent a cross-reaction between determinants common to erythrocyte glycoprotein containing I antigen and the membrane of M. pneumoniae.
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PMID:Cold hemagglutinin cross-reactivity with Mycoplasma pneumoniae. 8 98

Respiratory infection with Mycoplasma pneumoniae evokes immunoglobulin M autoantibody which agglutinates human erythrocytes at 4 degrees C (cold agglutinin) and is specific for I antigen. Cross-reactions between surface antigens of M. pneumoniae and human erythrocytes, previously examined by serological analysis, were examined by transmission and scanning electron microscopy. Ferritin-labeled human antimycoplasmal and rabbit antisera to erythrocyte membrane components reacted with antigens on the surface of both M. pneumoniae and erythrocytes. Adsorption of human erythrocytes to M. pneumoniae was blocked by the same antisera without ferritin label. It is proposed that the cross-reactive specificity lies in peripheral areas of the mycoplasmal cell, probably in a surface carbohydrate which has antigenic identity with erythrocyte glycoprotein.
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PMID:Immune electron microscopy of cross-reactions between Mycoplasma pneumoniae and human erythrocytes. 45 71

The obligate, thermophilic, acidophilic mycoplasma, Thermoplasma acidophilum, grows optimally at 56 degrees C and pH 2.0. Its plasma membrane possessed 21--22 protein bands that were resolved by polyacrylamide gel electrophoresis. One major membrane protein, molecular weight 152 000, which stained for carbohydrate with periodic acid-Schiff reagent, accounted for 32% (w/w) of the total membrane proteins. It was isolated and further purified by concanavalin A affinity chromatography. The carbohydrate content amounted to less than 10% (w/w) compared to that of the entire glycoprotein. The carbohydrate moiety consisted mainly of mannose residues with branched alpha 1 leads to 2 linkages at the non-reducing ends of the glycopeptide as determined by permethylation followed by gas chromatography-mass spectrometry analysis. The reducing end was an N-glycosidic linkage between asparagine and N-acetylglucosamine. The amino acid composition of this glycoprotein showed 62 mol% hydrophobic residues, while the acidic amino acid content contributed 9 mol% more than that of the basic amino acids. The existence of membrane glycoproteins in the procaryotic, wall-less T. acidophilum may provide a protective coat for the plasma membrane. The stereochemistry and the conformation of the carbohydrate chains, in conjunciton with water turgor, may contribute to the rigidity of the membrane and the cation binding.
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PMID:Purification and partial characterization of a procaryotic glycoprotein from the plasma membrane of Thermoplasma acidophilum. 53 27

A glycoprotein was detected in Mycoplasma pneumoniae membranes. Its apparent molecular weight was about 60,000, as observed by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. It corresponded to the single band that was detected on the gels by the carbohydrate stain, periodic acid-Schiff reagent. The intensity of this stained band varied for membranes derived from cells harvested between 4 and 10 days, with maximal intensity found for cells grown for 6 days. The carbohydrate-containing polypeptide was extracted with lithium diiodosalicylate. The extracted fraction consisted of about 80 to 90% amino acids (mainly glycine and histidine) and about 7% carbohydrates (mainly glucose, galactose, and glucosamine). The fraction was immunologically active, as indicated by the complement fixation and precipitin tests with antisera against whole cells, membranes, and membrane proteins.
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PMID:Isolation of a glycoprotein from Mycoplasma pneumoniae membranes. 92 74

The glycoproteins in the normal pig bronchial gland are identified by the combined Alcian Blue (AB)-periodic acid Schiff (PAS) technique, with the use of sialidase digestion and AB staining either at pH 2-6 or at pH 1-0. In enzootic pneumonia (produced experimentally by infection with Mycoplasma hyorhinis) the bronchial gland hypertrophies, mucous and serous cells both increase, in number and size; hence the total glycoprotein content of the gland increases. The distribution of glycoproteins in the hypertrophied gland differs from that in the normal. Quantitative analysis of the mucous cells shows that in the hypertrophied gland the acid glycoprotein is increased relative to the neutral. There is also a relative change in the amounts of sialidase-sensitive sialomucin and sulphomucin; both are significantly increased at the expense of the sialidase-resistant sialomucin. Qualitative analysis of the serous cells shows that in the normal gland most of the glycoprotein is neutral and that the small amount of acid glycoprotein is sialidase-resistant sialomucin. In the hypertrophied gland there is relatively more acid glycoprotein which is either sialidase-resistant sialomucin or sulphomucin; in addition, in pigs with enzootic pneumonia there is an increase in the height of the bronchial epithelium and a depletion in both goblet cell number and glycoprotein content, which latter has more neutral glycoprotein and less acid glycoprotein.
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PMID:Histochemical identification of glycoproteins in pig bronchial epithelium: (a) normal and (b) hypertrophied from enzootic pneumonia. 115 72

M. gallisepticum membranes were treated with 0.3M lithium diiodosalicylate (LIS) and, on average, 43% of the original membrane proteins were extracted. The extract contained particles with a sedimentation coefficient of 13S and some aggregated proteins. This LIS extract was immunogenic, stimulating the production of haemagglutination-inhibiting, growth-inhibiting and precipitating antibodies in rabbits. It was devoid of haemagglutinating (HA) activity for chicken erythrocytes but did inhibit the HA activity of membranes of M. gallisepticum. This inhibitory activity was destroyed by periodate and trypsin, but not by heat. By sedimentation equilibrium in a caesium chloride gradient, the LIS extract was separated into a lipoprotein-like and a glycoprotein fraction. The lipoprotein-like fraction contained the majority of the proteins present in the original extract, had HA activity and blocked antibody which inhibits haemagglutination. These activities were apparently due to the protein moiety, since they were not removed by extraction with n-butanol. The lipoprotein-like fraction behaved similarly to the unfractionated LIS extract in immunodiffusion tests and polyacrylamide gel electrophoresis, producing one periodic acid-Schiff positive band in the latter. The glycoprotein fraction consisted of about 66% carbohydrate and 33% protein. The sugar components were identified as glucose, galactose, glucosamine, galactosamine, glucuronic acid. The glycorprotein fraction did not possess HA but blocked the HA activity of M. gallisepticum membranes. In immunodiffusion it produced one faint precipitation band. The possible significance of glycoprotein in mycoplasma membranes has been discussed.
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PMID:Dissociation of Mycoplasma gallisepticum membranes with lithium diiodosalicylate and isolation of glycoprotein. 121 14

Serologic evidence of anti-I and anti-Fl cold agglutinins occurring in mycoplasma infections led to the isolation of I/Fl glycoprotein from human erythrocyte membranes. Mycoplasma pneumoniae bound to purified I/Fl glycoprotein in a dose-dependent fashion depending on sialylated carbohydrate determinants. This was shown by the decreased binding of mycoplasmas to either sialidase-treated I/Fl glycoprotein (dot blot analysis) or sialidase-treated erythrocytes (hemagglutination test). Structural properties of the receptor for optimal binding could be explored by hemagglutination inhibition assays. Glycophorins were excluded as receptors. These results indicate that Fl (and I) antigens are receptors for M. pneumoniae.
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PMID:Characterization of I/F1 glycoprotein as a receptor for Mycoplasma pneumoniae. 137 Feb 78

Mycoplasma hyopneumoniae causes pneumonia in pigs. The effect of infection by this organism on histochemical characteristics of airway mucin within epithelial cells was studied. Seven- to 10-week-old pigs were inoculated intratracheally with M hyopneumoniae or culture broth, and lung tissues were collected from inoculated and control pigs at 2, 4, and 6 weeks after inoculation. Tissue sections were stained with periodic acid-Schiff/Alcian blue, pH 2.5 or high iron diamine/Alcian blue. Histologic features of randomly selected bronchi, bronchioles, and submucosal glands were compared in sections stained with periodic acid-Schiff/Alcian blue. Bronchial goblet cell sulfomucin and sialomucin were quantitated by image analysis of sections stained with high iron diamine/Alcian blue. Bronchi and bronchioles of infected pigs contained proportionately fewer goblet cells with mucin at all stages of infection than age-matched control pigs. Goblet cells in bronchi of infected pigs contained significantly less total mucin and sialomucin, and significantly more sulfomucin than goblet cells of control pigs. Increased sulfated mucin in bronchial goblet cells may reflect altered glycoprotein production or secretion in response to infection with M hyopneumoniae.
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PMID:Histochemical and morphologic changes of porcine airway epithelial cells in response to infection with Mycoplasma hyopneumoniae. 141 80

We determined serum levels of alpha 1-antitrypsin, alpha 1-acid glycoprotein, ceruloplasmin, haptoglobin, alpha 2-HS glycoprotein, C3 and fibronectin in 22 patients with acute pneumonia, 10 patients with mycoplasma pneumonia and 8 patients with exacerbation of chronic bronchitis at both acute and convalescent phases to clarify whether levels of these proteins change with inflammation. Serum levels of alpha 1-antitrypsin, alpha 1-acid glycoprotein, ceruloplasmin, haptoglobin and C3 in the patients in the acute phase were significantly higher than that in the patients in the convalescent phase. The serum level of fibronectin in the patients in the acute phase was significantly lower than that in the patients in convalescent phase. The serum level of alpha 2HS glycoprotein remained unchanged.
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PMID:[Changes in various serum protein levels between acute and convalescent phases in patients with respiratory infections]. 169 92

Multiple bands of glycoprotein, rare in procaryotes, were detected in ten human Mycoplasma species by staining with periodic acid-Schiff (PAS) reagent after sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). A major contaminant formed in Hayflick medium (H medium), corresponding to an apparent molecular weight of about 80 kD, was eliminated by using the organisms grown in PPLO broth supplemented with PPLO serum fraction (P medium), except that M. genitalium and M. pneumoniae were grown in H medium as monolayers on the glass surface. The comparison of glycoproteins among ten human Mycoplasma species indicated that their profiles were shown to be species-specific. However, those of M. buccale and M. faucium were very similar, and M. pneumoniae and M. genitalium seemed to be related.
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PMID:Comparison of glycoproteins from ten human Mycoplasma species. 181


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