Cytophilic antibodies to are thought to be protective against pregnancy-associated malaria in part by promoting phagocytosis of infected erythrocytes (IE). The effect of opsonisation by such antibodies on pro-inflammatory cytokine (PIC) production is not clear. We studied the effect of opsonization of IE with immune serum on cytokine responses using human monocyte-derived macrophages (MDM) exposed to E infected with the CS2 strain of Plasmodium falciparum. Since HIV infection increases the risk and severity of pregnancy-associated malaria by poorly defined mechanisms, we measured the effect of HIV infection of macrophages on cytokine production.
Unopsonised IE induced secretion of IL-6 (median=622pg/ml [IQR=1,250-240], n=9), but not IL-1b or TNFa, whereas opsonised IE induced secretion of IL-1b (18.6 pg/mL [34.2-14.4]), TNFa (113pg/ml [421-17.0]) and increased IL-6 (2195 pg/mL [4,658-1,095]) by MDM. Both IE and opsonised IE, however, induced similar robust IL-6, TNF and IL-1â mRNA expression and activated NF-kB to a similar extent, suggesting opsonization affects post-transcriptional events. IgG-opsonized, but not unopsonized, CS2 IE activated caspase-1 cleavage and enzymatic activity in MDM showing that Fcγ receptor-mediated phagocytosis activates the inflammasome. MDM attached to IgG-coated surfaces however secreted IL-1b in response to unopsonized IE, suggesting that internalization of IE is not an absolute requirement for inflammasome activation and IL-1b secretion. IgG-opsonised CS2 did not induce cytokine production from MyD88-/- mouse macrophages suggesting a MyD88-dependent receptor recognizes IE on the surface of macrophages. HIV-1 infection significantly inhibited phagocytosis of opsinised-IE, decreased secretion of IL-6 and IL-1β.
We conclude that a MyD88 dependent surface receptor activates NFkB in response to IE and stimulates PIC mRNA expression. IgG opsonization is required for inflammasome activity and IL-1b secretion. HIV infection of macrophages inhibits IE clearance and innate immune responses to IE.