Abstract
In recent years, there has been a renewed interest in utilizing antibody fragment crystallizable (Fc) functions to prevent and control viral infections. The protective and therapeutic potential of Fc-mediated antibody functions have been assessed for some clinically important human viruses, including HIV, hemorrhagic fever viruses and influenza virus. There is mounting evidence that influenza-specific antibodies with Fc-mediated functions, such as antibody-dependent cellular cytotoxicity and antibody-dependent phagocytosis, can aid in the clearance of influenza virus infection. Recent influenza challenge studies and intravenous immunoglobulin G therapy studies in humans suggest a protective role for Fc effector functions in vivo. Broadly reactive influenza antibodies with Fc-mediated functions are prevalent in the human population and could inform the development of a universally protective influenza vaccine or therapy. In this review, we explore the utility of antibodies with Fc-mediated effector functions against viral infections with a focuson influenza virus.
Highlights
Structural features of antibodies allow them to mediate a diverse array of antiviral effector functions
The fragment crystallizable (Fc) domain is historically considered to be the invariant region of the antibody, but it displays significant heterogeneity owing to variation in the antibody isotypes [immunoglobulin G (IgG), IgA, IgM, IgE and IgD], subclasses (IgG1, IgG2, IgG3 and IgG4), allotypes and modifications.[1,2]
We showed that humans who succumbed to H7N9 infection had reduced Fc-functional antibodies, in magnitude and breadth, compared with those who survived infection.[68]
Summary
Structural features of antibodies allow them to mediate a diverse array of antiviral effector functions.
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