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Outer sheath associated proteins of the oral spirochete Treponema maltophilum
K Heuner1, U Meltzer, B K Choi
1Institut für Mikrobiologie und Hygiene, Universitätsklinikum Charité, Humboldt-Universität zu Berlin, Germany. klaus.heuner@mail-wuerburg.de
Abstract:
We recently cloned the major outer membrane protein of Treponema maltophilum [Heuner, K., Choi, B.K., Schade, R., Moter, A., Otto, A., Göbel, U.B., J. Bacteriol. 181, 1025-1029]. Here we report the localization of the major sheath protein (Msp)A protein in T. maltophilum by immunogold electron microscopy and its expression. Northern blot analysis revealed that mspA is expressed constitutively as a monocistronic unit. The transcription initiation site of the mspA gene was identified by primer extension analysis. A further screening of a genomic library of T. maltophilum with an anti-outer membrane fraction antibody was done. We were able to clone DNA regions of T. maltophilum encoding putative sugar transport operons and putative outer membrane proteins of this oral treponeme which has a high prevalence in periodontal lesions.
Insights
Researchers localized the major sheath protein (Msp)A in Treponema maltophilum using immunogold electron microscopy. This study also identified mspA gene expression and cloned other outer membrane proteins and sugar transport operons.
Area of Science:
- Microbiology
- Oral microbiology
- Molecular biology
Background:
- Treponema maltophilum is an oral treponeme frequently found in periodontal lesions.
- The major outer membrane protein (Msp)A of T. maltophilum was previously cloned.
- Understanding the outer membrane proteins of T. maltophilum is crucial for comprehending its role in periodontal disease.
Purpose of the Study:
- To determine the localization of the major sheath protein (Msp)A in T. maltophilum.
- To investigate the expression pattern of the mspA gene.
- To identify other potential outer membrane proteins and sugar transport operons in T. maltophilum.
Main Methods:
- Immunogold electron microscopy was used for protein localization.
- Northern blot analysis and primer extension were employed to study gene expression.
- Screening of a genomic library with an anti-outer membrane antibody was performed.
Main Results:
- MspA protein localization in T. maltophilum was successfully determined.
- The mspA gene is constitutively expressed as a monocistronic unit.
- DNA regions encoding putative sugar transport operons and outer membrane proteins were cloned.
Conclusions:
- The study provides insights into the expression and localization of MspA in T. maltophilum.
- The identification of additional outer membrane proteins and sugar operons contributes to understanding the molecular mechanisms of this oral pathogen.
- Further research on these identified components may reveal new targets for therapeutic intervention in periodontal disease.