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- W1970258298 abstract "Cholesterol binds to streptolysin O and related bacterial toxins. In normal serum, only a fraction of the cholesterol attached to lipoprotein is available for binding, probably as a cholesterol-peptide complex formed during catabolic breakdown of the lipoprotein. Cholesterol esterase produced by certain organisms—e.g., Staphylococcus pyogenes and Pseudomonas œruginosa—augments this fraction both in vitro and in vivo. Endogenous esterase similarly increases the amount of cholesterol-peptide complex, a mechanism which may be activated as a feedback process following binding of toxin to the cholesterol component of the complex. These complexes will thus supply a readily available means of binding bacterial toxins before antibody formation begins. Cholesterol-peptide complexes, either alone or modified by binding to toxin, may function as autoantigens. It is postulated that immune complexes so formed may be involved in atherosclerosis either by directly damaging vessels walls or by cross-reaction of antibody with cell-membrane-bound lipoproteins which equilibrate with plasma-lipoproteins." @default.
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- W1970258298 date "1975-02-01" @default.
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- W1970258298 title "FUNCTIONAL ROLE OF CHOLESTEROL IN INFECTION AND AUTOIMMUNITY" @default.
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- W1970258298 doi "https://doi.org/10.1016/s0140-6736(75)91211-8" @default.
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