In Mycoplasma hoministhe OppA-mediated cytoadhesion depends on its ATPase activity

BMC Microbiology

Research Article

Birgit Henrich¹  Miriam Hopfe¹  Theresa Dahlmanns¹ 

[1] Institute of Medical Microbiology and Hospital Hygiene, Heinrich-Heine-University Duesseldorf, Moorenstrasse 5, 40225, Duesseldorf, Germany;

关键词: HeLa Cell;    ATPase Activity;    Suramin;    Oligomycin;    ATPase Domain;   

DOI  :  10.1186/1471-2180-11-185

 received in 2011-04-28, accepted in 2011-08-19,  发布年份 2011

来源: Springer

【 摘 要 】

BackgroundIn Mycoplasma hominis, a facultative human pathogen of the human genital tract, OppA, the substrate-binding domain of the oligopeptide permease, is a multifunctional protein involved in nutrition uptake, cytoadhesion and hydrolysis of extracellular ATP.ResultsTo map the function-related protein regions the ATPase activity and adhesive behavior of OppA mutants were analyzed. Mutations of the Walker BA motifs resulted in an inhibition of up to 8% of the OppA ATPase activity, whereas deletion of the N-terminal CS1 or the CS2 region, structural motifs that are conserved in bacterial OppA proteins, reduced ATPase activity to 60% and deletion of CS3, the third conserved region adjacent to the Walker B motif led to a reduction to 42% ATPase activity.Interestingly, adhesion of the OppA mutants to immobilized HeLa cells demonstrated that two distal regions are mainly involved in adherence of OppA: the CS1 region, deletion of which led to 35% of the cytoadhesion, and the Walker BA with the adjacent upstream region CS3, deletion of which led to 25% of the cytoadhesion. The influence of the ATPase activity on the adherence of M. hominis to HeLa cells was confirmed by the use of ATPase inhibitors which reduced mycoplasmal cytoadhesion to 50%.ConclusionsThese findings suggest that the OppA-mediated cytoadherence of Mycoplasma hominis depends on both, the topology of the neighbouring CS1 and ATPase domain regions and the functionality of the ecto-ATPase activity in addition.

【 授权许可】

Unknown   
© Hopfe et al; licensee BioMed Central Ltd. 2011. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.