Journal
FUTURE VIROLOGY
Volume 9, Issue 4, Pages 397-414Publisher
FUTURE MEDICINE LTD
DOI: 10.2217/fvl.14.19
Keywords
ADCC; antibody; antibody-dependent cellular phagocytosis; antibody-dependent cellular viral inhibition; antibody-dependent complement-dependent cytotoxicity; Fc; Fc effector function; glycosylation; HIV; IgG; subclass
Categories
Funding
- Bill and Melinda Gates Collaboration for AIDS Vaccine Discovery [OPP1032817]
- National Health and Medical Research Center [APP1036470]
- Massachusetts General Hospital
- [NIH1R01AI102660-02]
- [5R01Al080289-03]
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RV144 vaccine immune-correlates analysis has generated a renewed interest in understanding the potentially protective role of non-neutralizing antibodies in HIV infection and vaccine design. Antibodies consist of a variable region involved in antigen binding and a constant region. While both ends of the antibody collaborate to induce protective immunity, it is through the constant portion that an antibody provides instructions to the innate immune system on how the recognized antigen should be processed, contributing directly to antiviral immunity. Antibody constant regions, despite their name, are not uniform structures, but can vary both in protein sequence and glycosylation, together modulating antibody functionality via conformational changes that alter antibody affinity for Fc receptors, complement and so on. This review will focus on how the immune system naturally modulates the Fc domain of antibodies to achieve optimum protective Fc effector responses for vaccine and monoclonal therapeutic design efforts aimed at preventing or curing HIV infection.
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