Document Detail

OppA, the ecto-ATPase of Mycoplasma hominis induces ATP release and cell death in HeLa cells.
MedLine Citation:
PMID:  18394151     Owner:  NLM     Status:  MEDLINE    
BACKGROUND: In the facultative human pathogen Mycoplasma hominis, which belongs to the cell wall-less Mollicutes, the surface-localised substrate-binding domain OppA of the oligopeptide permease was characterised as the main ecto-ATPase.
RESULTS: With the idea that extra-cellular ATP could only be provided by the infected host cells we analysed the ATP release of HeLa cells after incubation with different preparations of Mycoplasma hominis: intact bacterial cells, the membrane fraction with or without OppA, recombinant OppA as well as an ATPase-deficient OppA mutant. Release of ATP into the supernatant of the HeLa cells was primarily determined in all samples lacking ecto-ATPase activity of OppA. In the presence of the ATPase inhibitor DIDS the amount of ATP in the OppA-containing samples increased. This increase was maximal after incubation with fractions containing OppA protein indicating that OppA is involved in ATP release and subsequent hydrolysis. Real-time PCR analyses revealed that the proliferation of HeLa cells is reduced after infection with M. hominis and flow cytometry experiments established that OppA induces greater apoptosis than necrosis of HeLa cells whereas the preservation of ecto-ATPase activity of OppA induces apoptosis.
CONCLUSION: The OppA induced ATP-release and -hydrolysis induced cell death of M. hominis infected HeLa cells was predominantly due to apoptosis rather than necrosis. Future work will elucidate whether the induction of apoptosis is indispensable for survival of these non-invasive pathogen.
Miriam Hopfe; Birgit Henrich
Publication Detail:
Type:  Journal Article     Date:  2008-04-04
Journal Detail:
Title:  BMC microbiology     Volume:  8     ISSN:  1471-2180     ISO Abbreviation:  BMC Microbiol.     Publication Date:  2008  
Date Detail:
Created Date:  2008-04-18     Completed Date:  2008-05-13     Revised Date:  2013-06-05    
Medline Journal Info:
Nlm Unique ID:  100966981     Medline TA:  BMC Microbiol     Country:  England    
Other Details:
Languages:  eng     Pagination:  55     Citation Subset:  IM    
Institute of Medical Microbiology and Center for Biological Medical Research, Heinrich-Heine-University, Moorenstrasse 5, 40225 Duesseldorf, Germany.
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MeSH Terms
Adenosine Triphosphatases / metabolism*
Adenosine Triphosphate / metabolism*
Bacterial Proteins / metabolism*
Carrier Proteins / metabolism*
Cell Death
HeLa Cells / metabolism,  pathology
Lipoproteins / metabolism*
Mycoplasma hominis / enzymology*
Oligopeptides / metabolism*
Reg. No./Substance:
0/Bacterial Proteins; 0/Carrier Proteins; 0/Lipoproteins; 0/Oligopeptides; 0/oligopeptide-binding protein, bacteria; 56-65-5/Adenosine Triphosphate; EC 3.6.1.-/Adenosine Triphosphatases; EC 3.6.1.-/ectoATPase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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