Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 286, Issue 44, Pages 38211-38219Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M111.249482
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Funding
- National Institutes of Health [HL48739]
- Finnish Cultural Foundation
- Paulo Foundation
- Aarne Koskelon Foundation
- Orion Farmos
- Alfred Kordelin Foundation
- Research Council for Biosciences and Environment, Academy of Finland [114075]
- Finnish Foundation for Cardiovascular Research
- Research Council for Health, Academy of Finland [132629]
- Academy of Finland (AKA) [132629, 132629] Funding Source: Academy of Finland (AKA)
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Apolipoprotein A-I (apoA-I), the main protein component of high density lipoprotein (HDL), is well recognized for its anti-atherogenic, 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.
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