Helicobacter pylori secretes the chaperonin GroEL (HSP60), which binds iron

Published on Jun 19, 2013in FEBS Letters3.057
· DOI :10.1016/J.FEBSLET.2013.04.048
Marco Antonio González-López4
Estimated H-index: 4
(UACM: Universidad Autónoma de la Ciudad de México),
Norma Velázquez-Guadarrama9
Estimated H-index: 9
+ 1 AuthorsJosé de Jesús Olivares-Trejo13
Estimated H-index: 13
(UACM: Universidad Autónoma de la Ciudad de México)
Helicobacter pylori is a bacterium that can use multiple iron sources. However, it is unknown whether this bacterium secretes molecules such as siderophores or haemophores to scavenge iron. Here, we report the first secreted iron-binding protein of H. pylori, which we purified by haem-affinity chromatography. Mass spectrometry analysis revealed its identity as chaperonin (HpGroEL). When we compared HpGroEL with EcGroEL from Escherichia coli, they were homologous, showing 60% similarity. Additionally, purified cytoplasmic HpGroEL could also bind iron. Perhaps H. pylori secretes HpGroEL to maintain the appropriate folding of extracellular proteins and to bind iron.
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