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  • Title: Membrane pore formation by pentraxin proteins from Limulus, the American horseshoe crab.
    Author: Harrington JM, Chou HT, Gutsmann T, Gelhaus C, Stahlberg H, Leippe M, Armstrong PB.
    Journal: Biochem J; 2008 Jul 15; 413(2):305-13. PubMed ID: 18370931.
    Abstract:
    The pentraxins are a family of highly conserved plasma proteins of metazoans known to function in immune defence. The canonical members, C-reactive protein and serum amyloid P component, have been identified in arthropods and humans. Mammalian pentraxins are known to bind lipid bilayers, and a pentraxin representative from the American horseshoe crab, Limulus polyphemus, binds and permeabilizes mammalian erythrocytes. Both activities are Ca(2+)-dependent. Utilizing model liposomes and planar lipid bilayers, in the present study we have investigated the membrane-active properties of the three pentraxin representatives from Limulus and show that all of the Limulus pentraxins permeabilize lipid bilayers. Mechanistically, Limulus C-reactive protein forms transmembrane pores in asymmetric planar lipid bilayers that mimic the outer membrane of Gram-negative bacteria and exhibits a Ca(2+)-independent form of membrane binding that may be sufficient for pore formation.
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