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Distribution of ecto 5'-nucleotidase on Mycoplasma species associated with arthritis
1Biochemistry Division, Department of Cellular and Molecular Sciences, St. George's Hospital Medical School, London, UK. sjohnson@sghms.ac.uk
Abstract:
The enzyme ecto 5'-nucleotidase (5'N) was found to be active on 8/14 strains of Mycoplasma fermentans, K(m) (+/-S.D.) 3.8+/-2.8 microM 5'-AMP, and on the type strain of Mycoplasma pulmonis, K(m) 0.63 microM 5'-AMP. The six M. fermentans strains lacking 5'N activity were related by restriction fragment length polymorphism typing. At pH 8.5, the type strains of Mycoplasma arthritidis, Mycoplasma buccale and Ureaplasma urealyticum showed a relatively non-specific phosphatase activity against 5'-AMP but no activity was shown by the type strains of Mycoplasma genitalium, Mycoplasma hominis, Mycoplasma orale, Mycoplasma penetrans, Mycoplasma pneumoniae and Mycoplasma salivarium at this pH. M. fermentans has been reported from rheumatoid joints, which show a raised 5'N activity on their synovial cells and in their fluid which may be associated directly or indirectly with the mycoplasma.
Insights
Ecto-5'-nucleotidase (5'N) activity was detected in some Mycoplasma fermentans strains and Mycoplasma pulmonis. This enzyme
Area of Science:
- Microbiology
- Enzymology
- Molecular Biology
Background:
- Ecto-5 -nucleotidase (5 N) is an enzyme involved in nucleotide metabolism.
- Mycoplasma species are known opportunistic pathogens that can colonize various host tissues.
- Previous studies suggest a potential link between Mycoplasma infections and altered 5 N activity in hosts, particularly in rheumatoid arthritis.
Purpose of the Study:
- To investigate the presence and activity of ecto-5 -nucleotidase (5 N) in various Mycoplasma and Ureaplasma species.
- To explore the potential association between Mycoplasma fermentans and elevated 5 N activity observed in rheumatoid joints.
Main Methods:
- Enzyme activity assays were performed on multiple strains of Mycoplasma fermentans, Mycoplasma pulmonis, and other Mycoplasma/Ureaplasma species using 5 -AMP as a substrate.
- Kinetic parameters (K(m)) for 5 N activity were determined.
- Restriction fragment length polymorphism (RFLP) typing was used to analyze strains of Mycoplasma fermentans.
- Phosphatase activity was assessed at pH 8.5 for various type strains.
Main Results:
- Ecto-5 -nucleotidase (5 N) activity was detected in 8 out of 14 strains of Mycoplasma fermentans and in the type strain of Mycoplasma pulmonis.
- Six Mycoplasma fermentans strains lacked 5 N activity and were related by RFLP typing.
- Type strains of Mycoplasma arthritidis, Mycoplasma buccale, and Ureaplasma urealyticum exhibited non-specific phosphatase activity, but not specific 5 N activity at pH 8.5.
- Several other Mycoplasma type strains (M. genitalium, M. hominis, M. orale, M. penetrans, M. pneumoniae, M. salivarium) showed no 5 N activity at pH 8.5.
Conclusions:
- The presence of ecto-5 -nucleotidase (5 N) varies among Mycoplasma strains, with activity found in some Mycoplasma fermentans and Mycoplasma pulmonis strains.
- The observed elevated 5 N activity in rheumatoid joints may be linked to Mycoplasma fermentans infections, either directly or indirectly.
- Further research is warranted to elucidate the precise role of mycoplasma-associated 5 N in joint inflammation and disease pathogenesis.