{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Biedzka-Sarek M"],"funding":["NHLBI NIH HHS"],"pagination":["38211-38219"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3207405"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["286(44)"],"pubmed_abstract":["Apolipoprotein A-I (apoA-I), the main protein component of high density lipoprotein (HDL), is well recognized for its antiatherogenic, antioxidant, and antiinflammatory properties. Here, we report a novel role for apoA-I as a host defense molecule that contributes to the complement-mediated killing of an important gastrointestinal pathogen, Gram-negative bacterium Yersinia enterocolitica. We specifically show that the C-terminal domain of apoA-I is the effector site providing the bactericidal activity. Although the presence of the lipopolysaccharide O-antigen on the bacterial surface is absolutely required for apoA-I to kill the bacteria, apoA-I does not interact with the bacteria directly. To the contrary, exposure of the bacteria by serum proteins triggers apoA-I deposition on the bacterial surface. As our data show that both purified lipid-free and HDL-associated apoA-I displays anti-bacterial potential, apoA-I mimetic peptides may be a promising therapeutic agent for the treatment of certain Gram-negative infections."],"journal":["The Journal of biological chemistry"],"pubmed_title":["Apolipoprotein A-I exerts bactericidal activity against Yersinia enterocolitica serotype O:3."],"pmcid":["PMC3207405"],"funding_grant_id":["R01 HL048739","HL48739"],"pubmed_authors":["Kateifides A","Radziejewska-Lebrecht J","Metso J","Biedzka-Sarek M","Skurnik M","Meri T","Jokiranta TS","Muszynski A","Jauhiainen M","Zannis V"],"additional_accession":[]},"is_claimable":false,"name":"Apolipoprotein A-I exerts bactericidal activity against Yersinia enterocolitica serotype O:3.","description":"Apolipoprotein A-I (apoA-I), the main protein component of high density lipoprotein (HDL), is well recognized for its antiatherogenic, antioxidant, and antiinflammatory properties. Here, we report a novel role for apoA-I as a host defense molecule that contributes to the complement-mediated killing of an important gastrointestinal pathogen, Gram-negative bacterium Yersinia enterocolitica. We specifically show that the C-terminal domain of apoA-I is the effector site providing the bactericidal activity. Although the presence of the lipopolysaccharide O-antigen on the bacterial surface is absolutely required for apoA-I to kill the bacteria, apoA-I does not interact with the bacteria directly. To the contrary, exposure of the bacteria by serum proteins triggers apoA-I deposition on the bacterial surface. As our data show that both purified lipid-free and HDL-associated apoA-I displays anti-bacterial potential, apoA-I mimetic peptides may be a promising therapeutic agent for the treatment of certain Gram-negative infections.","dates":{"release":"2011-01-01T00:00:00Z","publication":"2011 Nov","modification":"2024-10-17T17:15:53.996Z","creation":"2019-03-27T00:45:37Z"},"accession":"S-EPMC3207405","cross_references":{"pubmed":["21896489"],"doi":["10.1074/jbc.m111.249482","10.1074/jbc.M111.249482"]}}