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Trypsin-sensitive, bovine serum albumin-dependent hemolysis activity in Mycoplasma pulmonis
Abstract:
Although Mycoplasma pulmonis did not lyse normal erythrocytes, it rapidly lysed erythrocytes that had cytoskeletal deficiencies which allow increased diffusion of membrane glycophorin or that had been treated with trypsin to remove surface proteins. This hemolysis occurred only in the presence of bovine serum albumin and was eliminated by trypsin treatment of the mycoplasma. Hemolytic activity was restored after such trypsin treatment when mycoplasma protein synthesis was allowed. M. pulmonis hemolytic activity was not diffusible and thus differed from the activities reported for other mycoplasmas, which involve small diffusible intermediates such as hydrogen peroxide. With the exception of the requirement for bovine serum albumin, the factors which affected hemolysis were similar to those which we have previously reported to affect M. pulmonis hemagglutination, suggesting that these two activities are functionally related.
Insights
Mycoplasma pulmonis selectively lyses erythrocytes with membrane defects or removed surface proteins. This non-diffusible hemolytic activity requires bovine serum albumin and mycoplasma protein synthesis.
Area of Science:
- Microbiology
- Cell Biology
- Immunology
Background:
- Mycoplasma pulmonis is a bacterium known to interact with host cells.
- Erythrocyte lysis by microorganisms can be mediated by various mechanisms.
- Previous studies indicated Mycoplasma pulmonis exhibits hemagglutination activity.
Purpose of the Study:
- To investigate the hemolytic activity of Mycoplasma pulmonis against erythrocytes.
- To characterize the conditions and factors influencing this hemolytic activity.
- To compare the hemolytic mechanism with other known Mycoplasma species.
Main Methods:
- Erythrocytes with induced cytoskeletal deficiencies and trypsin-treated erythrocytes were used.
- Hemolysis assays were performed in the presence of bovine serum albumin.
- Effects of trypsin treatment on Mycoplasma pulmonis and subsequent protein synthesis were assessed.
Main Results:
- Mycoplasma pulmonis did not lyse normal erythrocytes but rapidly lysed erythrocytes with cytoskeletal deficiencies or removed surface proteins.
- Hemolysis was dependent on bovine serum albumin and was inhibited by trypsin treatment of the mycoplasma.
- Hemolytic activity was restored upon mycoplasma protein synthesis post-trypsinization and was non-diffusible.
Conclusions:
- Mycoplasma pulmonis possesses a non-diffusible hemolytic activity distinct from other mycoplasmas.
- This activity is mediated by mycoplasma surface components and requires specific erythrocyte membrane properties.
- Hemolysis and hemagglutination by Mycoplasma pulmonis appear to be functionally related processes.