Apolipoprotein A-I exerts bactericidal activity against Yersinia enterocolitica serotype O:3.
J Biol Chem
; 286(44): 38211-38219, 2011 Nov 04.
Article
em En
| MEDLINE
| ID: mdl-21896489
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.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Yersinia enterocolitica
/
Apolipoproteína A-I
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Antígenos O
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Antibacterianos
Limite:
Humans
Idioma:
En
Ano de publicação:
2011
Tipo de documento:
Article