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Biomedical subjects

H Brunner

Publications and source records attributed to H Brunner.

At least 307 records · Page 17Linked to original sources
PubMed1974

Asymptomatic infection of adult volunteers with a temperature sensitive mutant of Mycoplasma pneumoniae.

Temperature sensitive mutants of Mycoplasma pneumoniae were developed with the expectation that their temperature sensitive defects would restrict replication in vivo at the temperature of the lower respiratory tract, whereas such defects would not seriously impair replication in the cooler environment of the upper respiratory passages. One such ts mutant, ts-H43, which does not replicate at a temperature of 37 degrees or above, although noninfectious for hamsters, infected each of 16 seronegative adult volunteers when given by the intranasal route. The mutant remained genetically stable throughout the course of infection and stimulated a moderate systemic and local antibody response. The mutant was entirely avirulent for the volunteers but appeared to stimulate resistance to subsequent challenge with partially attenuated wild-type (ts(+)) Mycoplasma pneumoniae.

Adult↗
PubMed1974

Studies with lectins on the surface carbohydrate structures of mycoplasma membranes.

The surface carbohydrate structures on the cell membranes of various mycoplasma species have been investigated by using lectins, which are sugar-specific proteins. Carbohydrate structures presumably bound to glycolipids, with both galactose and glucose units, were found to be exposed on the surface of Mycoplasma pneumoniae and its temperature-sensitive mutants, M. mycoides var. mycoides and capri, M. pulmonis, M. gallinarum, and M. gallisepticum. Lipid-bound glucose was found on M. neurolyticum. The possible relationship of the lipid-bound surface carbohydrate groups to the known serological cross-reactions and lipid compositions of the various mycoplasma species is discussed. Intact Acholeplasma laidlawii and M. fermentans have no lectin-binding sites exposed on their surfaces; galactose groups were discovered only after Pronase digestion of the organisms, suggesting that their glycolipids are hidden under a protein layer. Neither intact nor Pronase-digested M. hominis reacted with the lectins; this is fully consistent with the lipid composition of this organism, which contains glycolipids. The lectins from Vicia cracca and Phaseolus vulgaris, which react with N-acetyl-galactosamine groups, agglutinated M. gallinarum, M. gallisepticum, M. mycoides var. capri, and M. pulmonis. The agglutinability was lost after Pronase treatment, indicating that the corresponding carbohydrates are presumably protein bound. They may be correlated with the extracellular structures observed by electron microscopy of both sectioned and negatively stained mycoplasma species.

Agglutination Tests↗