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Helicobacter pylori secretes the chaperonin GroEL (HSP60), which binds iron
Author(s) -
GonzálezLópez Marco Antonio,
VelázquezGuadarrama Norma,
RomeroEspejel María Elena,
de Jesús OlivaresTrejo José
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.04.048
Subject(s) - chaperonin , groel , helicobacter pylori , hsp60 , chemistry , groes , microbiology and biotechnology , biochemistry , biology , virology , protein folding , heat shock protein , genetics , escherichia coli , hsp70 , gene
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.