Related Experiment Video
Updated: Sep 23, 2026

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking
Published on: December 17, 2013
Phase variation of the multiple banded protein in Ureaplasma urealyticum and Ureaplasma parvum
Stefan Monecke1, Jürgen H Helbig, Enno Jacobs
1Institute for Medical Microbiology and Hygiene, Medical Faculty, Technical University of Dresden, Germany. monecke@rocketmail.com
Abstract:
Ureaplasma urealyticum and U. parvum are common commensals and, possibly, pathogens of the human urogenital tract. Like other Mycoplasmatales they possess variable surface proteins. The multiple banded (MB) protein shows a striking variability of its molecular weight. This is caused by changes of the number of C-terminal repeating units. In this study, selective pressure was imposed against cytadherence of U. urealyticum and U. parvum. Ureaplasmas were co-incubated with either erythrocytes or HeLa cells and the cell-bound fraction was removed. Additionally, U. urealyticum populations were transferred serially through broth containing specific polyclonal antibodies. Both approaches led to the emergence of escape variants in which no MB protein was detectable. PCR studies with several primers on different parts of the mba gene indicated major differences between wild-type strains and MB-negative escape variants. In experiments with clonal lineages, however, the loss of the MB protein was shown to be reversible. Therefore, it is proposed that the multiple banded proteins of U. urealyticum and U. parvum are subjected to a phase-switching mechanism as it has already been described for several other Mycoplasmatales.
Insights
Ureaplasma urealyticum and U. parvum can lose their multiple banded (MB) proteins under selective pressure. This loss is reversible, suggesting a phase-switching mechanism for MB protein expression in these common urogenital tract bacteria.
Area of Science:
- Microbiology
- Bacterial Pathogenesis
- Molecular Biology
Background:
- Ureaplasma urealyticum and U. parvum are common inhabitants of the human urogenital tract, acting as both commensals and potential pathogens.
- These bacteria possess variable surface proteins, including the multiple banded (MB) protein, which exhibits significant molecular weight variations due to changes in C-terminal repeating units.
Purpose of the Study:
- To investigate the mechanisms underlying the variability of the multiple banded (MB) protein in Ureaplasma urealyticum and U. parvum.
- To determine if selective pressures can induce changes in MB protein expression and to characterize the nature of these changes.
Main Methods:
- Selective pressure was applied by co-incubating Ureaplasma species with erythrocytes or HeLa cells to inhibit cytadherence.
- Serial passage in broth containing polyclonal antibodies was used to select for variants with altered surface protein expression.
- PCR analysis was performed on wild-type and variant strains to examine the mba gene structure.
Main Results:
- Exposure to selective pressures, including antibody treatment and cell co-incubation, resulted in the emergence of Ureaplasma variants lacking detectable MB protein.
- PCR studies revealed significant genetic differences in the mba gene between wild-type strains and MB-negative escape variants.
- Experiments with clonal lineages demonstrated that the loss of MB protein expression is a reversible phenomenon.
Conclusions:
- The findings suggest that the multiple banded proteins of Ureaplasma urealyticum and U. parvum are regulated by a phase-switching mechanism.
- This reversible phase-switching likely contributes to the adaptability and persistence of Ureaplasma in the urogenital tract.
- The study provides insights into the dynamic nature of bacterial surface protein expression in response to environmental cues.
More Related Videos
Related Concept Videos
Position-effect Variegation
Regulation of Bacterial Virulence

