title: Surface-associated GroEL facilitates the adhesion of Escherichia coli to macrophages through lectin-like oxidized low-density lipoprotein receptor-1.
abstract: The Escherichia coli homolog of GroEL, a 60 kDa heat shock protein (HSP), is a dominant protein produced not only in response to heat stress but also under in vitro growth condition. Beside its traditional cytoplasmic location, the surface exposures of GroEL have been observed in many pathogenic bacteria. To investigate the role of the surface-associated GroEL in the binding of E. coli to macrophages, we constructed a new strain of E. coli displaying GroEL on the outer membrane. We found that surface-associated GroEL increases the clearance ratio of E. coli by macrophages. It has been previously demonstrated that lectin-like oxidized low-density lipoprotein receptor-1 (LOX-1) is the receptor for Hsp60 from different species. Our present results showed that GroEL on E. coli was recognized by LOX-1 on macrophages, leading to the phagocytosis of pathogen by macrophages. In addition, surface-associated GroEL made mice more susceptible to E. coli-induced peritonitis. These findings add to the research that clarifies the factors mediating bacterial adherence to host cells. Our results suggest that GroEL is a novel therapeutic target for modulating the immune response in infectious and inflammatory conditions.
authors.affiliation: Department of Biochemistry, Shanghai Medical School, Fudan University, and Department of Thoracic Surgery, Huashan Hospital, Shanghai 200032, PR China.
authors.forename: Haiyan
authors.initials: H
authors.lastname: Zhu
authors.forename: Chiayu
authors.initials: C
authors.lastname: Lee
authors.forename: Dongmei
authors.initials: D
authors.lastname: Zhang
authors.forename: Weicheng
authors.initials: W
authors.lastname: Wu
authors.forename: Lan
authors.initials: L
authors.lastname: Wang
authors.forename: Xiaoyun
authors.initials: X
authors.lastname: Fang
authors.forename: Xiaolin
authors.initials: X
authors.lastname: Xu
authors.forename: Dongli
authors.initials: D
authors.lastname: Song
authors.forename: Jianhui
authors.initials: J
authors.lastname: Xie
authors.forename: Shifang
authors.initials: S
authors.lastname: Ren
authors.forename: Jianxin
authors.initials: J
authors.lastname: Gu
mesh_terms: D000818:Animals; D001422:Bacterial Adhesion / Q000235:genetics / Q000502:physiology; D002478:Cells, Cultured; D018834:Chaperonin 60 / Q000235:genetics / Q000378:metabolism*; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism / Q000472:pathogenicity / Q000502:physiology*; D029968:Escherichia coli Proteins / Q000235:genetics / Q000378:metabolism*; D005260:Female; D005434:Flow Cytometry; D008264:Macrophages / Q000378:metabolism* / Q000382:microbiology*; D051379:Mice; D008810:Mice, Inbred C57BL; D010538:Peritonitis / Q000378:metabolism / Q000382:microbiology; D051127:Scavenger Receptors, Class E / Q000378:metabolism*; D016019:Survival Analysis
chemical_list: D018834:Chaperonin 60; D029968:Escherichia coli Proteins; C495138:Olr1 protein, mouse; D051127:Scavenger Receptors, Class E