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Control of malaria virulence by alpha 1-acid glycoprotein (orosomucoid), an acute-phase (inflammatory) reactant

M J Friedman

    Proceedings of the National Academy of Sciences of the United States of America
    |September 1, 1983
    PubMed

    Insights

    Alpha 1-acid glycoprotein (AGP) concentration during malaria significantly inhibits parasite multiplication. This protective effect is linked to AGP's sialic acid content and structure, blocking parasite invasion.

    Area of Science:

    • Immunology
    • Infectious Diseases
    • Biochemistry

    Background:

    • Plasma concentrations of alpha 1-acid glycoprotein (AGP) elevate during infections like malaria.
    • The precise function of AGP in host defense during malaria has remained largely unknown.

    Purpose of the Study:

    • To elucidate the functional role of alpha 1-acid glycoprotein (AGP) in the context of malaria infection.
    • To investigate the mechanism by which AGP influences Plasmodium falciparum multiplication.

    Main Methods:

    • In vitro culture of Plasmodium falciparum.
    • Quantification of AGP's sialic acid content and analysis of its higher-order structure.
    • Assessment of AGP's effect on parasite multiplication rates.

    Main Results:

    • AGP concentrations observed during malaria inhibit Plasmodium falciparum multiplication by up to 80%.
    • The inhibitory activity of AGP is dependent on its sialic acid content (12-16 mol/mol) and structural integrity.
    • AGP functions by preventing the interaction between the malaria parasite and host erythrocytes during invasion.

    Conclusions:

    • Alpha 1-acid glycoprotein (AGP) plays a significant protective role against malaria by inhibiting parasite multiplication.
    • AGP's mechanism involves interfering with parasite-erythrocyte binding, highlighting its in vivo relevance.
    • These findings suggest AGP is a key component of the host's protective response to malaria and potentially other infections.

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