LIVIVO - Search results -

Search results

Result 1 - 10 of total 76

Search options

Article ; Online: Engineering strategies of Anti-HIV antibody therapeutics in clinical development.

Pihlstrom, Nicole / Bournazos, Stylianos

2023 Volume 18, Issue 4, Page(s) 184–190

Abstract: Purpose of review: Anti-human immunodeficiency virus (HIV) antibody-based therapeutics offer an alternative treatment option to current antiretroviral drugs. This review aims to provide an overview of the Fc- and Fab-engineering strategies that have ... ...

Abstract	Purpose of review: Anti-human immunodeficiency virus (HIV) antibody-based therapeutics offer an alternative treatment option to current antiretroviral drugs. This review aims to provide an overview of the Fc- and Fab-engineering strategies that have been developed to optimize broadly neutralizing antibodies and discuss recent findings from preclinical and clinical studies. Recent findings: Multispecific antibodies, including bispecific and trispecific antibodies, DART molecules, and BiTEs, as well as Fc-optimized antibodies, have emerged as promising therapeutic candidates for the treatment of HIV. These engineered antibodies engage multiple epitopes on the HIV envelope protein and human receptors, resulting in increased potency and breadth of activity. Additionally, Fc-enhanced antibodies have demonstrated extended half-life and improved effector function. Summary: The development of Fc and Fab-engineered antibodies for the treatment of HIV continues to show promising progress. These novel therapies have the potential to overcome the limitations of current antiretroviral pharmacologic agents by more effectively suppressing viral load and targeting latent reservoirs in individuals living with HIV. Further studies are needed to fully understand the safety and efficacy of these therapies, but the growing body of evidence supports their potential as a new class of therapeutics for the treatment of HIV.
MeSH term(s)	Humans ; HIV Infections/drug therapy ; Antibodies, Neutralizing/therapeutic use ; HIV-1 ; Antibodies, Bispecific/therapeutic use ; Antibodies, Bispecific/pharmacology ; HIV Antibodies
Chemical Substances	Antibodies, Neutralizing ; Antibodies, Bispecific ; HIV Antibodies
Language	English
Publishing date	2023-05-04
Publishing country	United States
Document type	Review ; Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2502511-9
ISSN	1746-6318 ; 1746-630X
ISSN (online)	1746-6318
ISSN	1746-630X
DOI	10.1097/COH.0000000000000796
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 6812: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Details ▾
- See ZB MED holdings
- Order with fees

Article: IgG Fc Receptors: Evolutionary Considerations.

Bournazos, Stylianos

Current topics in microbiology and immunology

2019 Volume 423, Page(s) 1–11

Abstract: Immunoglobulins (Ig), a critical component of the adaptive immune system, are present in all jawed vertebrates and through sophisticated diversification mechanisms are able to recognize antigens of almost infinite diversity. During mammalian evolution, ... ...

Abstract	Immunoglobulins (Ig), a critical component of the adaptive immune system, are present in all jawed vertebrates and through sophisticated diversification mechanisms are able to recognize antigens of almost infinite diversity. During mammalian evolution, IgG has emerged as the predominant Ig isotype that is elicited upon antigenic challenge, representing the most abundant isotype present in circulation. Along with the IgG molecule, a family of specialized receptors has evolved in mammalian species that specifically recognize the Fc domain of IgG. These receptors, termed Fcγ receptors (FcγRs), are expressed on the surface of effector leukocytes and upon crosslinking by the IgG Fc domain mediate diverse immunomodulatory processes with profound impact on several aspects of innate and adaptive immunity. FcγRs share a high degree of sequence homology among mammalian species and the ancestral locus, where the genes that encode for FcγRs are mapped, can be traced back early in mammalian evolution. FcγRs also share a number of common structural and functional properties among mammalian species and utilize highly conserved motifs for transducing signals upon engagement. Despite the high homology of FcγRs in diverse mammalian species, human FcγRs exhibit unique features relating to the gene organization, expression pattern in the various leukocyte populations, as well as affinity for human IgGs. Such inter-species differences in FcγRs biology between humans and other mammalian species represents a major limitation for the interpretation of in vivo studies on human IgG function using conventional animal models.
MeSH term(s)	Animals ; Humans ; Immunoglobulin G/chemistry ; Immunoglobulin G/immunology ; Models, Animal ; Receptors, Fc/immunology ; Receptors, IgG/immunology
Chemical Substances	Immunoglobulin G ; Receptors, Fc ; Receptors, IgG
Language	English
Publishing date	2019-02-07
Publishing country	Germany
Document type	Journal Article ; Review
ISSN	0070-217X
ISSN	0070-217X
DOI	10.1007/82_2019_149
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾
- Full text online
- Order with fees

Article ; Online: A novel mouse strain optimized for chronic human antibody administration.

Gupta, Aaron / Smith, Patrick / Bournazos, Stylianos / Ravetch, Jeffrey V

Proceedings of the National Academy of Sciences of the United States of America

2022 Volume 119, Issue 10, Page(s) e2123002119

Abstract: Therapeutic human IgG antibodies are routinely tested in mouse models of oncologic, infectious, and autoimmune diseases. However, assessing the efficacy and safety of long-term administration of these agents has been limited by endogenous anti-human IgG ... ...

Abstract	Therapeutic human IgG antibodies are routinely tested in mouse models of oncologic, infectious, and autoimmune diseases. However, assessing the efficacy and safety of long-term administration of these agents has been limited by endogenous anti-human IgG immune responses that act to clear human IgG from serum and relevant tissues, thereby reducing their efficacy and contributing to immune complex–mediated pathologies, confounding evaluation of potential toxicity. For this reason, human antibody treatment in mice is generally limited in duration and dosing, thus failing to recapitulate the potential clinical applications of these therapeutics. Here, we report the development of a mouse model that is tolerant of chronic human antibody administration. This model combines both a human IgG1 heavy chain knock-in and a full recapitulation of human Fc receptor (FcγR) expression, providing a unique platform for in vivo testing of human monoclonal antibodies with relevant receptors beyond the short term. Compared to controls, hIgG1 knock-in mice mount minimal anti-human IgG responses, allowing for the persistence of therapeutically active circulating human IgG even in the late stages of treatment in chronic models of immune thrombocytopenic purpura and metastatic melanoma.
MeSH term(s)	Animals ; Antibodies, Monoclonal, Humanized/administration & dosage ; Antibodies, Monoclonal, Humanized/therapeutic use ; Antibodies, Monoclonal, Humanized/toxicity ; Antibody Formation/genetics ; Chronic Disease ; Humans ; Immune Tolerance ; Immunoglobulin G/administration & dosage ; Immunoglobulin G/genetics ; Immunoglobulin G/immunology ; Immunoglobulin Heavy Chains/genetics ; Melanoma, Experimental/immunology ; Melanoma, Experimental/therapy ; Mice ; Mice, Transgenic ; Models, Animal ; Purpura, Thrombocytopenic, Idiopathic/immunology ; Purpura, Thrombocytopenic, Idiopathic/therapy
Chemical Substances	Antibodies, Monoclonal, Humanized ; Immunoglobulin G ; Immunoglobulin Heavy Chains
Language	English
Publishing date	2022-03-02
Publishing country	United States
Document type	Journal Article
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.2123002119
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 1148: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Human FcγRIIIa activation on splenic macrophages drives dengue pathogenesis in mice.

Yamin, Rachel / Kao, Kevin S / MacDonald, Margaret R / Cantaert, Tineke / Rice, Charles M / Ravetch, Jeffrey V / Bournazos, Stylianos

Nature microbiology

2023 Volume 8, Issue 8, Page(s) 1468–1479

Abstract: Although dengue virus (DENV) infection typically causes asymptomatic disease, DENV-infected patients can experience severe complications. A risk factor for symptomatic disease is pre-existing anti-DENV IgG antibodies. Cellular assays suggested that these ...

Abstract	Although dengue virus (DENV) infection typically causes asymptomatic disease, DENV-infected patients can experience severe complications. A risk factor for symptomatic disease is pre-existing anti-DENV IgG antibodies. Cellular assays suggested that these antibodies can enhance viral infection of Fcγ receptor (FcγR)-expressing myeloid cells. Recent studies, however, revealed more complex interactions between anti-DENV antibodies and specific FcγRs by demonstrating that modulation of the IgG Fc glycan correlates with disease severity. To investigate the in vivo mechanisms of antibody-mediated dengue pathogenesis, we developed a mouse model for dengue disease that recapitulates the unique complexity of human FcγRs. In in vivo mouse models of dengue disease, we discovered that the pathogenic activity of anti-DENV antibodies is exclusively mediated through engagement of FcγRIIIa on splenic macrophages, resulting in inflammatory sequelae and mortality. These findings highlight the importance of IgG-FcγRIIIa interactions in dengue, with important implications for the design of safer vaccination approaches and effective therapeutic strategies.
MeSH term(s)	Humans ; Animals ; Mice ; Receptors, IgG ; Dengue ; Dengue Virus ; Macrophages ; Immunoglobulin G
Chemical Substances	Receptors, IgG ; Immunoglobulin G
Language	English
Publishing date	2023-07-10
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ISSN	2058-5276
ISSN (online)	2058-5276
DOI	10.1038/s41564-023-01421-y
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article ; Online: The role of IgG Fc receptors in antibody-dependent enhancement.

Bournazos, Stylianos / Gupta, Aaron / Ravetch, Jeffrey V

Nature reviews. Immunology

2020 Volume 20, Issue 10, Page(s) 633–643

Abstract: Antibody-dependent enhancement (ADE) is a mechanism by which the pathogenesis of certain viral infections is enhanced in the presence of sub-neutralizing or cross-reactive non-neutralizing antiviral antibodies. In vitro modelling of ADE has attributed ... ...

Abstract	Antibody-dependent enhancement (ADE) is a mechanism by which the pathogenesis of certain viral infections is enhanced in the presence of sub-neutralizing or cross-reactive non-neutralizing antiviral antibodies. In vitro modelling of ADE has attributed enhanced pathogenesis to Fcγ receptor (FcγR)-mediated viral entry, rather than canonical viral receptor-mediated entry. However, the putative FcγR-dependent mechanisms of ADE overlap with the role of these receptors in mediating antiviral protection in various viral infections, necessitating a detailed understanding of how this diverse family of receptors functions in protection and pathogenesis. Here, we discuss the diversity of immune responses mediated upon FcγR engagement and review the available experimental evidence supporting the role of FcγRs in antiviral protection and pathogenesis through ADE. We explore FcγR engagement in the context of a range of different viral infections, including dengue virus and SARS-CoV, and consider ADE in the context of the ongoing SARS-CoV-2 pandemic.
MeSH term(s)	Antibodies, Monoclonal/administration & dosage ; Antibodies, Monoclonal/adverse effects ; Antibodies, Monoclonal/biosynthesis ; Antibodies, Neutralizing/administration & dosage ; Antibodies, Neutralizing/adverse effects ; Antibodies, Neutralizing/biosynthesis ; Antibodies, Viral/administration & dosage ; Antibodies, Viral/adverse effects ; Antibodies, Viral/biosynthesis ; Antibody-Dependent Enhancement/drug effects ; Betacoronavirus/drug effects ; Betacoronavirus/immunology ; Betacoronavirus/pathogenicity ; COVID-19 ; Coronavirus Infections/drug therapy ; Coronavirus Infections/immunology ; Coronavirus Infections/virology ; Dengue/drug therapy ; Dengue/immunology ; Dengue/virology ; Dengue Virus/drug effects ; Dengue Virus/immunology ; Dengue Virus/pathogenicity ; Gene Expression Regulation ; Host-Pathogen Interactions/drug effects ; Host-Pathogen Interactions/immunology ; Humans ; Leukocytes/drug effects ; Leukocytes/immunology ; Leukocytes/virology ; Pandemics ; Pneumonia, Viral/drug therapy ; Pneumonia, Viral/immunology ; Pneumonia, Viral/virology ; Receptors, IgG/antagonists & inhibitors ; Receptors, IgG/genetics ; Receptors, IgG/immunology ; SARS Virus/drug effects ; SARS Virus/immunology ; SARS Virus/pathogenicity ; SARS-CoV-2 ; Severe Acute Respiratory Syndrome/drug therapy ; Severe Acute Respiratory Syndrome/immunology ; Severe Acute Respiratory Syndrome/virology ; Signal Transduction ; Virus Internalization/drug effects
Chemical Substances	Antibodies, Monoclonal ; Antibodies, Neutralizing ; Antibodies, Viral ; Receptors, IgG
Keywords	covid19
Language	English
Publishing date	2020-08-11
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	2062776-2
ISSN	1474-1741 ; 1474-1733
ISSN (online)	1474-1741
ISSN	1474-1733
DOI	10.1038/s41577-020-00410-0
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 5565: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 34: Show issues

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Features and protective efficacy of human mAbs targeting Mycobacterium tuberculosis arabinomannan.

Liu, Yanyan / Chen, Tingting / Zhu, Yongqi / Furey, Aisha / Lowary, Todd L / Chan, John / Bournazos, Stylianos / Ravetch, Jeffrey V / Achkar, Jacqueline M

JCI insight

2023 Volume 8, Issue 20

Abstract: A better understanding of the epitopes most relevant for antibody-mediated protection against tuberculosis (TB) remains a major knowledge gap. We have shown that human polyclonal IgG against the Mycobacterium tuberculosis (M. tuberculosis) surface glycan ...

Abstract	A better understanding of the epitopes most relevant for antibody-mediated protection against tuberculosis (TB) remains a major knowledge gap. We have shown that human polyclonal IgG against the Mycobacterium tuberculosis (M. tuberculosis) surface glycan arabinomannan (AM) and related lipoarabinomannan (LAM) is protective against TB. To investigate the impact of AM epitope recognition and Fcγ receptor (FcγR) binding on antibody functions against M. tuberculosis, we isolated a high-affinity human monoclonal antibody (mAb; P1AM25) against AM and showed its binding to oligosaccharide (OS) motifs we previously found to be associated with in vitro functions of human polyclonal anti-AM IgG. Human IgG1 P1AM25, but not 2 other high-affinity human IgG1 anti-AM mAbs reactive with different AM OS motifs, enhanced M. tuberculosis phagocytosis by macrophages and reduced intracellular growth in an FcγR-dependent manner. P1AM25 in murine IgG2a, but neither murine IgG1 nor a non-FcγR-binding IgG, given intraperitoneally prior to and after aerosolized M. tuberculosis infection, was protective in C57BL/6 mice. Moreover, we demonstrated the protective efficacy of human IgG1 P1AM25 in passive transfer with M. tuberculosis-infected FcγR-humanized mice. These data enhance our knowledge of the important interplay between both antibody epitope specificity and Fc effector functions in the defense against M. tuberculosis and could inform development of vaccines against TB.
MeSH term(s)	Humans ; Animals ; Mice ; Mycobacterium tuberculosis ; Receptors, IgG/metabolism ; Mice, Inbred C57BL ; Tuberculosis/prevention & control ; Antibodies, Monoclonal/pharmacology ; Immunoglobulin G ; Epitopes
Chemical Substances	arabinomannan (53026-40-7) ; Receptors, IgG ; Antibodies, Monoclonal ; Immunoglobulin G ; Epitopes
Language	English
Publishing date	2023-10-23
Publishing country	United States
Document type	Journal Article
ISSN	2379-3708
ISSN (online)	2379-3708
DOI	10.1172/jci.insight.167960
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article ; Online: Antibodies elicited in humans upon chimeric hemagglutinin-based influenza virus vaccination confer FcγR-dependent protection in vivo.

Edgar, Julia E / Trezise, Stephanie / Anthony, Robert M / Krammer, Florian / Palese, Peter / Ravetch, Jeffrey V / Bournazos, Stylianos

Proceedings of the National Academy of Sciences of the United States of America

2023 Volume 120, Issue 44, Page(s) e2314905120

Abstract: Antibody responses against highly conserved epitopes on the stalk domain of influenza virus hemagglutinin (HA) confer broad protection; however, such responses are limited. To effectively induce stalk-specific immunity against conserved HA epitopes, ... ...

Abstract	Antibody responses against highly conserved epitopes on the stalk domain of influenza virus hemagglutinin (HA) confer broad protection; however, such responses are limited. To effectively induce stalk-specific immunity against conserved HA epitopes, sequential immunization strategies have been developed based on chimeric HA (cHA) constructs featuring different head domains but the same stalk regions. Immunogenicity studies in small animal models, as well as in humans, revealed that cHA immunogens elicit stalk-specific IgG responses with broad specificity against heterologous influenza virus strains. However, the mechanisms by which these antibodies confer in vivo protection and the contribution of their Fc effector function remain unclear. To characterize the role of Fc-FcγR (Fcγ receptor) interactions to the in vivo protective activity of IgG antibodies elicited in participants in a phase I trial of a cHA vaccine candidate, we performed passive transfer studies of vaccine-elicited IgG antibodies in mice humanized for all classes of FcγRs, as well as in mice deficient for FcγRs. IgG antibodies elicited upon cHA vaccination completely protected FcγR humanized mice against lethal influenza virus challenge, while no protection was evident in FcγR-deficient mice, suggesting a major role for FcγR pathways in the protective function of vaccine-elicited IgG antibodies. These findings have important implications for influenza vaccine development, guiding the design of vaccination approaches with the capacity to elicit IgG responses with optimal Fc effector function.
MeSH term(s)	Humans ; Animals ; Mice ; Hemagglutinins ; Receptors, IgG/genetics ; Receptors, IgG/metabolism ; Antibodies, Viral ; Hemagglutinin Glycoproteins, Influenza Virus/genetics ; Influenza Vaccines ; Orthomyxoviridae/metabolism ; Influenza, Human/prevention & control ; Orthomyxoviridae Infections ; Vaccination ; Immunoglobulin G ; Epitopes
Chemical Substances	Hemagglutinins ; Receptors, IgG ; Antibodies, Viral ; Hemagglutinin Glycoproteins, Influenza Virus ; Influenza Vaccines ; Immunoglobulin G ; Epitopes
Language	English
Publishing date	2023-10-23
Publishing country	United States
Document type	Journal Article
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.2314905120
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 1148: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Attenuated Vaccines for Augmented Immunity.

Bournazos, Stylianos / Ravetch, Jeffrey V

Cell host & microbe

2017 Volume 21, Issue 3, Page(s) 314–315

Abstract: Live attenuated vaccines are more immunogenic and have the capacity to elicit long-lasting immune responses. In two recent studies, Wang et al. (2017) and Si et al. (2016) describe strategies for the generation of live attenuated influenza viruses, which ...

Abstract	Live attenuated vaccines are more immunogenic and have the capacity to elicit long-lasting immune responses. In two recent studies, Wang et al. (2017) and Si et al. (2016) describe strategies for the generation of live attenuated influenza viruses, which elicited robust humoral, mucosal, and cellular immunity against diverse virus strains.
MeSH term(s)	Antibody Formation ; Humans ; Immunity, Cellular ; Influenza Vaccines/immunology ; Orthomyxoviridae/immunology ; Vaccines, Attenuated/immunology
Chemical Substances	Influenza Vaccines ; Vaccines, Attenuated
Language	English
Publishing date	2017-03-09
Publishing country	United States
Document type	Journal Article ; Comment
ZDB-ID	2278004-X
ISSN	1934-6069 ; 1931-3128
ISSN (online)	1934-6069
ISSN	1931-3128
DOI	10.1016/j.chom.2017.02.016
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 6578: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Fcγ Receptor Function and the Design of Vaccination Strategies.

Bournazos, Stylianos / Ravetch, Jeffrey V

Immunity

2017 Volume 47, Issue 2, Page(s) 224–233

Abstract: Through specific interactions with distinct types of Fcγ receptors (FcγRs), the Fc domain of immunoglobulin G (IgG) mediates a wide spectrum of immunological functions that influence both innate and adaptive responses. Recent studies indicate that IgG Fc- ...

Abstract	Through specific interactions with distinct types of Fcγ receptors (FcγRs), the Fc domain of immunoglobulin G (IgG) mediates a wide spectrum of immunological functions that influence both innate and adaptive responses. Recent studies indicate that IgG Fc-FcγR interactions are dynamically regulated during an immune response through the control of the Fc-associated glycan structure and Ig subclass composition on the one hand and selective FcγR expression on immune cells on the other, which together determine the capacity of IgG to interact in a cell-type-specific manner with specific members of the FcγR family. Here, we present a framework that synthesizes the current understanding of the contribution of FcγR pathways to the induction and regulation of antibody and T cell responses. Within this context, we discuss vaccination strategies to elicit broad and potent immune responses based on the immunomodulatory properties of Fc-FcγR interactions.
MeSH term(s)	Animals ; Humans ; Immunoglobulin Fc Fragments/metabolism ; Immunoglobulin Isotypes/immunology ; Immunoglobulin Isotypes/metabolism ; Immunomodulation ; Receptors, IgG/immunology ; Receptors, IgG/metabolism ; Signal Transduction ; T-Lymphocytes, Regulatory/immunology ; Vaccination ; Vaccines/immunology
Chemical Substances	Immunoglobulin Fc Fragments ; Immunoglobulin Isotypes ; Receptors, IgG ; Vaccines
Language	English
Publishing date	2017-08-29
Publishing country	United States
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	1217235-2
ISSN	1097-4180 ; 1074-7613
ISSN (online)	1097-4180
ISSN	1074-7613
DOI	10.1016/j.immuni.2017.07.009
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 4227: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 69: Show issues

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Anti-retroviral antibody FcγR-mediated effector functions.

Bournazos, Stylianos / Ravetch, Jeffrey V

Immunological reviews

2017 Volume 275, Issue 1, Page(s) 285–295

Abstract: 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 Fcγ receptors (FcγRs) ... ...

Abstract	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 Fcγ receptors (FcγRs) expressed on the surface of effector leukocytes to induce the activation of distinct immunomodulatory pathways. Fc-FcγR 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 FcγR 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 FcγR-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-FcγR interactions are required to achieve full therapeutic activity through clearance of IgG-opsonized virions and elimination of HIV-infected cells. Manipulation of Fc-FcγR interactions to specifically activate distinct FcγR-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.
MeSH term(s)	Animals ; Antibodies, Neutralizing/therapeutic use ; HIV Antibodies/immunology ; HIV Antibodies/therapeutic use ; HIV Infections/immunology ; HIV Infections/therapy ; HIV-1/immunology ; Humans ; Immunoglobulin Fab Fragments/immunology ; Immunomodulation ; Immunotherapy/methods ; Phagocytosis ; Receptors, IgG/immunology ; Viral Load
Chemical Substances	Antibodies, Neutralizing ; HIV Antibodies ; Immunoglobulin Fab Fragments ; Receptors, IgG
Language	English
Publishing date	2017-01-16
Publishing country	England
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	391796-4
ISSN	1600-065X ; 0105-2896
ISSN (online)	1600-065X
ISSN	0105-2896
DOI	10.1111/imr.12482
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Se 160: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾

To top

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito