PMID- 28133801
OWN - NLM
STAT- MEDLINE
DCOM- 20170814
LR  - 20200725
IS  - 1600-065X (Electronic)
IS  - 0105-2896 (Print)
IS  - 0105-2896 (Linking)
VI  - 275
IP  - 1
DP  - 2017 Jan
TI  - Anti-retroviral antibody FcgammaR-mediated effector functions.
PG  - 285-295
LID - 10.1111/imr.12482 [doi]
AB  - The antiviral activity of antibodies reflects the bifunctional properties of 
      these molecules. While the Fab domains mediate highly specific antigenic 
      recognition to block virus entry, the Fc domain interacts with diverse types of 
      Fcgamma receptors (FcgammaRs) expressed on the surface of effector leukocytes to induce 
      the activation of distinct immunomodulatory pathways. Fc-FcgammaR interactions are 
      tightly regulated to control IgG-mediated inflammation and immunity and are 
      largely determined by the structural heterogeneity of the IgG Fc domain, stemming 
      from differences in the primary amino acid sequence of the various subclasses, as 
      well as the structure and composition of the Fc-associated N-linked glycan. 
      Engagement of specific FcgammaR types on effector leukocytes has diverse consequences 
      that affect several aspects of innate and adaptive immunity. In this review, we 
      provide an overview of the complexity of FcgammaR-mediated pathways, discussing their 
      role in the in vivo protective activity of anti-HIV-1 antibodies. We focus on 
      recent studies on broadly neutralizing anti-HIV-1 antibodies that revealed that 
      Fc-FcgammaR interactions are required to achieve full therapeutic activity through 
      clearance of IgG-opsonized virions and elimination of HIV-infected cells. 
      Manipulation of Fc-FcgammaR interactions to specifically activate distinct 
      FcgammaR-mediated pathways has the potential to affect downstream effector responses, 
      influencing thereby the in vivo protective activity of anti-HIV-1 antibodies; a 
      strategy that has already been successfully applied to other IgG-based 
      therapeutics, substantially improving their clinical efficacy.
CI  - (c) 2017 John Wiley & Sons A/S. Published by John Wiley & Sons Ltd.
FAU - Bournazos, Stylianos
AU  - Bournazos S
AD  - The Laboratory of Molecular Genetics and Immunology, The Rockefeller University, 
      New York, NY, USA.
FAU - Ravetch, Jeffrey V
AU  - Ravetch JV
AD  - The Laboratory of Molecular Genetics and Immunology, The Rockefeller University, 
      New York, NY, USA.
LA  - eng
GR  - P01 AI100148/AI/NIAID NIH HHS/United States
GR  - R01 CA080757/CA/NCI NIH HHS/United States
GR  - R56 AI034662/AI/NIAID NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, Non-U.S. Gov't
PT  - Review
PL  - England
TA  - Immunol Rev
JT  - Immunological reviews
JID - 7702118
RN  - 0 (Antibodies, Neutralizing)
RN  - 0 (HIV Antibodies)
RN  - 0 (Immunoglobulin Fab Fragments)
RN  - 0 (Receptors, IgG)
SB  - IM
MH  - Animals
MH  - Antibodies, Neutralizing/*therapeutic use
MH  - HIV Antibodies/*immunology/therapeutic use
MH  - HIV Infections/immunology/*therapy
MH  - HIV-1/*immunology
MH  - Humans
MH  - Immunoglobulin Fab Fragments/immunology
MH  - Immunomodulation
MH  - Immunotherapy/*methods
MH  - Phagocytosis
MH  - Receptors, IgG/immunology
MH  - Viral Load
PMC - PMC7379163
MID - NIHMS1610680
OTO - NOTNLM
OT  - AIDS
OT  - Fc receptors
OT  - antibodies
OT  - cytotoxicity
OT  - immunotherapies
OT  - inflammation
EDAT- 2017/01/31 06:00
MHDA- 2017/08/15 06:00
PMCR- 2020/07/24
CRDT- 2017/01/31 06:00
PHST- 2017/01/31 06:00 [entrez]
PHST- 2017/01/31 06:00 [pubmed]
PHST- 2017/08/15 06:00 [medline]
PHST- 2020/07/24 00:00 [pmc-release]
AID - 10.1111/imr.12482 [doi]
PST - ppublish
SO  - Immunol Rev. 2017 Jan;275(1):285-295. doi: 10.1111/imr.12482.