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Role of complement and Fc receptors in the pathogenesis of HIV-1 infection

1997; Springer Science+Business Media; Volume: 18; Issue: 3 Linguagem: Inglês

10.1007/bf00813504

1432-2196

David C. Montefiori,

Hepatitis C virus research

The Fc portion of immunoglobulin is important for complement activation and for targeting antigens to complement receptors (CR) and Fc receptors (FcR) on the surface of many cell types. Interactions with complement, CR and FcR can play both beneficial and pathological roles during viral infection. Activation of the classical or alternative complement pathways by epitopes and antibodies on microbial surfaces generates cleavage fragments of early complement component C3 that deposit on microbial surfaces and act as opsonins [104, 125]. Further activation of the terminal complement pathway can lead to assembly of the C5b-9 membrane attack complex (MAC) that forms transmembrane channels and eventually kills many targeted microbes, including certain viruses [48]. Opsonized virus particles that are not destroyed by the MAC may go on to bind CR on a variety of cell types. CR-binding can have consequences such as infection enhancement, virus clearance through the mononuclear phagocytic system, virus trapping in lymphoid tissues and B cell activation. Infection enhancement or phagocytosis also occurs when immune-complexed virus engages FcR on monocytes and macrophages.