Amyloid-beta peptide degradation in cell cultures by mycoplasma contaminants
<p>Abstract</p> <p>Background</p> <p>Cell cultures have become an indispensable tool in Alzheimer's disease research for studying amyloid-β (Aβ) metabolism. It is estimated that up to 35% of cell cultures in current use are infected with various mycoplasma species....
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doaj-4bddea3d79d54a8a9c4156da2f0eed632020-11-25T03:27:50ZengBMCBMC Research Notes1756-05002008-06-01113810.1186/1756-0500-1-38Amyloid-beta peptide degradation in cell cultures by mycoplasma contaminantsDavies PeterDreses-Werringloer UteZhao HaitianMarambaud Philippe<p>Abstract</p> <p>Background</p> <p>Cell cultures have become an indispensable tool in Alzheimer's disease research for studying amyloid-β (Aβ) metabolism. It is estimated that up to 35% of cell cultures in current use are infected with various mycoplasma species. In contrast with common bacterial and fungal infections, contaminations of cell cultures with mycoplasmas represent a challenging issue in terms of detectability and prevention. Mycoplasmas are the smallest and simplest self-replicating bacteria and the consequences of an infection for the host cells are variable, ranging from no apparent effect to induction of apoptosis.</p> <p>Findings</p> <p>Here we present evidence that mycoplasmas from a cell culture contamination are able to efficiently and rapidly degrade extracellular Aβ. As a result, we observed no accumulation of Aβ in the conditioned medium of mycoplasma-positive cells stably transfected with the amyloid-β precursor protein (APP). Importantly, eradication of the mycoplasma contaminant – identified as <it>M. hyorhinis </it>– by treatments with a quinolone-based antibiotic, restored extracellular Aβ accumulation in the APP-transfected cells.</p> <p>Conclusion</p> <p>These data show that mycoplasmas degrade Aβ and thus may represent a significant source of variability when comparing extracellular Aβ levels in different cell lines. On the basis of these results, we recommend assessment of mycoplasma contaminations prior to extracellular Aβ level measurements in cultured cells.</p> http://www.biomedcentral.com/1756-0500/1/38 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Davies Peter Dreses-Werringloer Ute Zhao Haitian Marambaud Philippe |
spellingShingle |
Davies Peter Dreses-Werringloer Ute Zhao Haitian Marambaud Philippe Amyloid-beta peptide degradation in cell cultures by mycoplasma contaminants BMC Research Notes |
author_facet |
Davies Peter Dreses-Werringloer Ute Zhao Haitian Marambaud Philippe |
author_sort |
Davies Peter |
title |
Amyloid-beta peptide degradation in cell cultures by mycoplasma contaminants |
title_short |
Amyloid-beta peptide degradation in cell cultures by mycoplasma contaminants |
title_full |
Amyloid-beta peptide degradation in cell cultures by mycoplasma contaminants |
title_fullStr |
Amyloid-beta peptide degradation in cell cultures by mycoplasma contaminants |
title_full_unstemmed |
Amyloid-beta peptide degradation in cell cultures by mycoplasma contaminants |
title_sort |
amyloid-beta peptide degradation in cell cultures by mycoplasma contaminants |
publisher |
BMC |
series |
BMC Research Notes |
issn |
1756-0500 |
publishDate |
2008-06-01 |
description |
<p>Abstract</p> <p>Background</p> <p>Cell cultures have become an indispensable tool in Alzheimer's disease research for studying amyloid-β (Aβ) metabolism. It is estimated that up to 35% of cell cultures in current use are infected with various mycoplasma species. In contrast with common bacterial and fungal infections, contaminations of cell cultures with mycoplasmas represent a challenging issue in terms of detectability and prevention. Mycoplasmas are the smallest and simplest self-replicating bacteria and the consequences of an infection for the host cells are variable, ranging from no apparent effect to induction of apoptosis.</p> <p>Findings</p> <p>Here we present evidence that mycoplasmas from a cell culture contamination are able to efficiently and rapidly degrade extracellular Aβ. As a result, we observed no accumulation of Aβ in the conditioned medium of mycoplasma-positive cells stably transfected with the amyloid-β precursor protein (APP). Importantly, eradication of the mycoplasma contaminant – identified as <it>M. hyorhinis </it>– by treatments with a quinolone-based antibiotic, restored extracellular Aβ accumulation in the APP-transfected cells.</p> <p>Conclusion</p> <p>These data show that mycoplasmas degrade Aβ and thus may represent a significant source of variability when comparing extracellular Aβ levels in different cell lines. On the basis of these results, we recommend assessment of mycoplasma contaminations prior to extracellular Aβ level measurements in cultured cells.</p> |
url |
http://www.biomedcentral.com/1756-0500/1/38 |
work_keys_str_mv |
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1724586849537622016 |