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Am J Physiol Lung Cell Mol Physiol 281: L776-L785, 2001;
1040-0605/01 $5.00
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Vol. 281, Issue 4, L776-L785, October 2001

Interaction of bacterial lipopolysaccharide with mouse surfactant protein C inserted into lipid vesicles

Luis Augusto1, Karine Le Blay1, Genevieve Auger2, Didier Blanot2, and Richard Chaby1

1 Endotoxin Group and 2 Laboratory of Bacterial Envelopes and Antibiotics, Unité Mixte de Recherche-8619 of the National Center for Scientific Research, University of Paris-Sud, 91405 Orsay, France

Infection of the respiratory tract is a frequent cause of lung pathologies, morbidity, and death. When bacterial endotoxin [lipopolysaccharide (LPS)] reaches the alveolar spaces, it encounters the lipid-rich surfactant that covers the epithelium. Although binding of hydrophilic surfactant protein (SP) A and SP-D with LPS has been established, nothing has been reported to date on possible cross talks between LPS and hydrophobic SP-B and SP-C. We designed a new binding technique based on the incorporation of surfactant components to lipid vesicles and the separation of unbound from vesicle-bound LPS on a density gradient. We found that among the different hydrophobic components of mouse surfactant separated by gel filtration or reverse-phase HPLC, only SP-C exhibited the capacity to bind to a tritium-labeled LPS. The binding of LPS to vesicles containing SP-C was saturable, temperature dependent, related to the concentrations of SP-C and LPS, and inhibitable by distinct unlabeled LPSs. Unlike SP-A and SP-D, the binding of SP-C to LPS did not require calcium ions. This LPS binding capacity of SP-C may represent another antibacterial defense mechanism of the lung.

endotoxin; surfactant protein A; surfactant protein B; surfactant protein D


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