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Article ; Online: The next frontier in vaccine design: blending immune correlates of protection into rational vaccine design.

Britto, Carl / Alter, Galit

2022 Volume 78, Page(s) 102234

Abstract: Despite the extraordinary speed and success in SARS-Cov-2 vaccine development, the emergence of variants of concern perplexed the vaccine development community. Neutralizing antibodies waned antibodies waned and were evaded by viral variants, despite the ...

Abstract	Despite the extraordinary speed and success in SARS-Cov-2 vaccine development, the emergence of variants of concern perplexed the vaccine development community. Neutralizing antibodies waned antibodies waned and were evaded by viral variants, despite the preservation of protection against severe disease and death across vaccinated populations. Similar to other vaccine design efforts, the lack of mechanistic correlates of immunity against Coronavirus Disease 2019, raised questions related to the need for vaccine redesign and boosting. Hence, our limited understanding of mechanistic correlates of immunity - across pathogens - remains a major obstacle in vaccine development. The identification and incorporation of mechanistic correlates of immunity are key to the accelerated design of highly impactful globally relevant vaccines. Systems-biology tools can be applied strategically to define a complete understanding of mechanistic correlates of immunity. Embedding immunological dissection and target immune profile identification, beyond canonical antibody binding and neutralization, may accelerate the design and success of durable protective vaccines.
MeSH term(s)	Humans ; Viral Vaccines ; COVID-19 Vaccines ; COVID-19/prevention & control ; SARS-CoV-2 ; Antibodies, Neutralizing ; Antibodies, Viral
Chemical Substances	Viral Vaccines ; COVID-19 Vaccines ; Antibodies, Neutralizing ; Antibodies, Viral
Language	English
Publishing date	2022-08-13
Publishing country	England
Document type	Journal Article ; Review ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1035767-1
ISSN	1879-0372 ; 0952-7915
ISSN (online)	1879-0372
ISSN	0952-7915
DOI	10.1016/j.coi.2022.102234
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Article ; Online: Humoral immune responses against SARS-CoV-2 in transplantation: Actionable biomarker or misplaced trust?

Fishman, Jay A / Alter, Galit

American journal of transplantation : official journal of the American Society of Transplantation and the American Society of Transplant Surgeons

2022 Volume 22, Issue 5, Page(s) 1291–1292

MeSH term(s)	Antibodies, Viral ; Biomarkers ; COVID-19 ; Humans ; Immunity, Humoral ; SARS-CoV-2 ; Trust ; Vaccination
Chemical Substances	Antibodies, Viral ; Biomarkers
Language	English
Publishing date	2022-03-10
Publishing country	United States
Document type	Editorial ; Comment
ZDB-ID	2060594-8
ISSN	1600-6143 ; 1600-6135
ISSN (online)	1600-6143
ISSN	1600-6135
DOI	10.1111/ajt.17018
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Book: The multi-faceted role of the IgG glycan

Alter, Galit

(Immunology Interest Group seminar series)

2017

Abstract: CIT): Immunology Interest Group Seminar Series Beyond their role in pathogen neutralization, antibodies mediate pathogen control and clearance via the recruitment of innate immune effector functions including phagocytosis and cytotoxicity but also via ... ...

Institution	National Institutes of Health (U.S.). / Immunology Interest Group,
Author's details	Galit Alter
Series title	Immunology Interest Group seminar series
Abstract	(CIT): Immunology Interest Group Seminar Series Beyond their role in pathogen neutralization, antibodies mediate pathogen control and clearance via the recruitment of innate immune effector functions including phagocytosis and cytotoxicity but also via the homeostatic regulation of the immune activation. Two modifications to the constant domain of the IgG antibody control this biological activity: 1) the irreversible genomic selection of isotype/subclass and 2) a more subtle alteration in Fc-glycosylation, that together provide instructions to the innate immune system . Because glycosylation alters the affinity of antibodies for Fc-receptors on innate immune cells, mounting evidence suggests that glycosylation may be actively exploited by the immune system to tune antibody biological activity far beyond pathogen control and clearance. While many monoclonal therapeutics have exploited glycosylation, its in vivo control and whether it may be selectively harnessed to target pathogens and/or tumors is unknown. Two distinct functional roles of antibodies will be discussed in this presentation including the role of antibodies the regulation of the induction of the fhumoral immune response as well as in the regulation of antibody transfer from mother to child. Galit Alter received her PhD in experimental medicine from McGill University, and is currently an Associate Professor in Medicine at Harvard Medical School. Over the past 8 years her research has focused on understanding the role of the innate immune response to chronic viral infections, including HIV and HCV, with a focus on defining the role of Natural Killer (NK) cells in antiviral control. Recently, these studies have shifted gears to begin to define the mechanism by which these innate immune effector cells may be harnessed through vaccination to gain more effective control over viral replication. To do this, her current research interests lie in defining the role of innate immune recruiting antibodies in providing protection from infection. Specifically, she is working towards defining the pathways that result in the targeted production of "protective" antibody glycans to enhance the production of antibodies that can potently block infections. Advancement in understanding how to manipulate the antibody glycan in a targeted manner through vaccination will also lead to the generation of vaccines with broader applications by extending to the improvement of therapeutic vaccines for the treatment of malignancies and autoimmune diseases as well. This knowledge will provide insights into natural antibody glycovariation, and lead to the development of novel approaches to strategically tailor vaccines to induce innate immune cell-recruiting antibodies, with the hope that these findings will ultimately revolutionize the application of vaccines to treat and prevent a remarkably larger range of diseases.
MeSH term(s)	Immunoglobulin G/immunology ; Antibodies, Viral/immunology ; Immunoglobulin Fc Fragments/immunology ; Glycosylation ; Polysaccharides/immunology ; Antibodies, Neutralizing/immunology
Language	English
Size	1 online resource (1 streaming video file (1 hr., 9 min.)) :, color, sound.
Document type	Book
Note	Closed-captioned.
Database	Catalogue of the US National Library of Medicine (NLM)

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Article ; Online: The multifaceted roles of breast milk antibodies.

Atyeo, Caroline / Alter, Galit

Cell

2021 Volume 184, Issue 6, Page(s) 1486–1499

Abstract: Neonates are born with an immature immune system and rely on the transfer of immunity from their mothers. Maternal antibodies are transferred via the placenta and breast milk. Although the role of placentally transferred immunoglobulin G (IgG) is ... ...

Abstract	Neonates are born with an immature immune system and rely on the transfer of immunity from their mothers. Maternal antibodies are transferred via the placenta and breast milk. Although the role of placentally transferred immunoglobulin G (IgG) is established, less is known about the selection of antibodies transferred via breast milk and the mechanisms by which they provide protection against neonatal disease. Evidence suggests that breast milk antibodies play multifaceted roles, preventing infection and supporting the selection of commensals and tolerizing immunity during infancy. Here, we discuss emerging data related to the importance of breast milk antibodies in neonatal immunity and development.
MeSH term(s)	Animals ; Antibodies/metabolism ; Homeostasis ; Humans ; Immunity ; Immunologic Factors/pharmacology ; Microbiota ; Milk, Human/immunology
Chemical Substances	Antibodies ; Immunologic Factors
Language	English
Publishing date	2021-03-31
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	187009-9
ISSN	1097-4172 ; 0092-8674
ISSN (online)	1097-4172
ISSN	0092-8674
DOI	10.1016/j.cell.2021.02.031
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Article ; Online: The Power of Antibody-Based Surveillance.

Alter, Galit / Seder, Robert

The New England journal of medicine

2020 Volume 383, Issue 18, Page(s) 1782–1784

MeSH term(s)	Betacoronavirus ; COVID-19 ; Coronavirus Infections ; Humans ; Iceland ; Immunity, Humoral ; Pandemics ; Pneumonia, Viral ; SARS-CoV-2
Keywords	covid19
Language	English
Publishing date	2020-09-01
Publishing country	United States
Document type	Editorial ; Comment
ZDB-ID	207154-x
ISSN	1533-4406 ; 0028-4793
ISSN (online)	1533-4406
ISSN	0028-4793
DOI	10.1056/NEJMe2028079
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Article ; Online: Understanding the role of antibody glycosylation through the lens of severe viral and bacterial diseases.

Irvine, Edward B / Alter, Galit

Glycobiology

2020 Volume 30, Issue 4, Page(s) 241–253

Abstract: Abundant evidence points to a critical role for antibodies in protection and pathology across infectious diseases. While the antibody variable domain facilitates antibody binding and the blockade of infection, the constant domain (Fc) mediates cross talk ...

Abstract	Abundant evidence points to a critical role for antibodies in protection and pathology across infectious diseases. While the antibody variable domain facilitates antibody binding and the blockade of infection, the constant domain (Fc) mediates cross talk with the innate immune system. The biological activity of the Fc region is controlled genetically via class switch recombination, resulting in the selection of distinct antibody isotypes and subclasses. However, a second modification is made to all antibodies, via post-translational changes in antibody glycosylation. Studies from autoimmunity and oncology have established the role of immunoglobulin G (IgG) Fc glycosylation as a key regulator of humoral immune activity. However, a growing body of literature, exploring IgG Fc glycosylation through the lens of infectious diseases, points to the role of inflammation in shaping Fc-glycan profiles, the remarkable immune plasticity in antibody glycosylation across pathogen-exposed populations, the canonical and noncanonical functions of glycans and the existence of antigen-specific control over antibody Fc glycosylation. Ultimately, this work provides critical new insights into the functional roles for antibody glycosylation as well as lays the foundation for leveraging antibody glycosylation to drive prevention or control across diseases.
MeSH term(s)	Animals ; Antibodies/immunology ; Bacterial Infections/immunology ; Glycosylation ; Humans ; Immunoglobulin Fc Fragments/immunology ; Polysaccharides/immunology ; Virus Diseases/immunology
Chemical Substances	Antibodies ; Immunoglobulin Fc Fragments ; Polysaccharides
Language	English
Publishing date	2020-02-26
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	1067689-2
ISSN	1460-2423 ; 0959-6658
ISSN (online)	1460-2423
ISSN	0959-6658
DOI	10.1093/glycob/cwaa018
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Article ; Online: Dissecting antibody-mediated protection against SARS-CoV-2.

Zohar, Tomer / Alter, Galit

Nature reviews. Immunology

2020 Volume 20, Issue 7, Page(s) 392–394

MeSH term(s)	Animals ; Antibodies, Neutralizing/immunology ; Antibodies, Viral/blood ; Antibodies, Viral/immunology ; Antibody-Dependent Cell Cytotoxicity ; Antibody-Dependent Enhancement ; COVID-19 ; COVID-19 Vaccines ; Coronavirus Infections/immunology ; Coronavirus Infections/prevention & control ; Humans ; Pandemics ; Pneumonia, Viral/immunology ; Viral Vaccines/immunology
Chemical Substances	Antibodies, Neutralizing ; Antibodies, Viral ; COVID-19 Vaccines ; Viral Vaccines
Keywords	covid19
Language	English
Publishing date	2020-06-08
Publishing country	England
Document type	Journal Article
ZDB-ID	2062776-2
ISSN	1474-1741 ; 1474-1733
ISSN (online)	1474-1741
ISSN	1474-1733
DOI	10.1038/s41577-020-0359-5
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Article ; Online: Extra-Neutralizing FcR-Mediated Antibody Functions for a Universal Influenza Vaccine.

Boudreau, Carolyn M / Alter, Galit

Frontiers in immunology

2019 Volume 10, Page(s) 440

Abstract: While neutralizing antibody titers measured by hemagglutination inhibition have been proposed as a correlate of protection following influenza vaccination, neutralization alone is a modest predictor of protection against seasonal influenza. Instead, ... ...

Abstract	While neutralizing antibody titers measured by hemagglutination inhibition have been proposed as a correlate of protection following influenza vaccination, neutralization alone is a modest predictor of protection against seasonal influenza. Instead, emerging data point to a critical role for additional extra-neutralizing functions of antibodies in protection from infection. Specifically, beyond binding and neutralization, antibodies mediate a variety of additional immune functions via their ability to recruit and deploy innate immune effector function. Along these lines, antibody-dependent cellular cytotoxicity, antibody-mediated macrophage phagocytosis and activation, antibody-driven neutrophil activation, antibody-dependent complement deposition, and non-classical Fc-receptor antibody trafficking have all been implicated in protection from influenza infection. However, the precise mechanism(s) by which the immune system actively tunes antibody functionality to drive protective immunity has been poorly characterized. Here we review the data related to Fc-effector functional protection from influenza and discuss prospects to leverage this humoral immune activity for the development of a universal influenza vaccine.
MeSH term(s)	Adjuvants, Immunologic ; Antibodies, Neutralizing/immunology ; Antibodies, Viral/immunology ; Antibody-Dependent Cell Cytotoxicity ; Complement Activation/immunology ; Epitopes/immunology ; Glycosylation ; Hemagglutinin Glycoproteins, Influenza Virus/chemistry ; Hemagglutinin Glycoproteins, Influenza Virus/immunology ; Humans ; Immunity, Innate ; Immunoglobulin Fab Fragments/immunology ; Immunoglobulin Fc Fragments/immunology ; Immunoglobulin Isotypes/immunology ; Influenza Vaccines/immunology ; Influenza, Human/immunology ; Influenza, Human/prevention & control ; Killer Cells, Natural/immunology ; Macrophage Activation/immunology ; Models, Molecular ; Neuraminidase/immunology ; Neutrophil Activation/immunology ; Orthomyxoviridae/immunology ; Phagocytosis ; Protein Processing, Post-Translational ; Receptors, Fc/immunology
Chemical Substances	Adjuvants, Immunologic ; Antibodies, Neutralizing ; Antibodies, Viral ; Epitopes ; Hemagglutinin Glycoproteins, Influenza Virus ; Immunoglobulin Fab Fragments ; Immunoglobulin Fc Fragments ; Immunoglobulin Isotypes ; Influenza Vaccines ; Receptors, Fc ; Neuraminidase (EC 3.2.1.18)
Language	English
Publishing date	2019-03-18
Publishing country	Switzerland
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	2606827-8
ISSN	1664-3224 ; 1664-3224
ISSN (online)	1664-3224
ISSN	1664-3224
DOI	10.3389/fimmu.2019.00440
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Article ; Online: Tissues: the unexplored frontier of antibody mediated immunity.

Webb, Nicholas E / Bernshtein, Biana / Alter, Galit

Current opinion in virology

2021 Volume 47, Page(s) 52–67

Abstract: Pathogen-specific immunity evolves in the context of the infected tissue. However, current immune correlates analyses and vaccine efficacy metrics are based on immune functions from peripheral cells. Less is known about tissue-resident mechanisms of ... ...

Abstract	Pathogen-specific immunity evolves in the context of the infected tissue. However, current immune correlates analyses and vaccine efficacy metrics are based on immune functions from peripheral cells. Less is known about tissue-resident mechanisms of immunity. While antibodies represent the primary correlate of immunity following most clinically approved vaccines, how antibodies interact with localized, compartment-specific immune functions to fight infections, remains unclear. Emerging data demonstrate a unique community of immune cells that reside within different tissues. These tissue-specific immunological communities enable antibodies to direct both expected and unexpected local attack strategies to control, disrupt, and eliminate infection in a tissue-specific manner. Defining the full breadth of antibody effector functions, how they selectively contribute to control at the site of infection may provide clues for the design of next-generation vaccines able to direct the control, elimination, and prevention of compartment specific diseases of both infectious and non-infectious etiologies.
MeSH term(s)	Animals ; Antibodies/immunology ; Brain/immunology ; Brain/pathology ; Brain/physiology ; Humans ; Immunity, Innate ; Immunoglobulin Fc Fragments/immunology ; Intestines/immunology ; Intestines/microbiology ; Liver/immunology ; Liver/microbiology ; Organ Specificity ; Receptors, Complement/immunology ; Skin/immunology ; Skin/microbiology ; Vaccines/immunology
Chemical Substances	Antibodies ; Immunoglobulin Fc Fragments ; Receptors, Complement ; Vaccines
Language	English
Publishing date	2021-02-10
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	2611378-8
ISSN	1879-6265 ; 1879-6257
ISSN (online)	1879-6265
ISSN	1879-6257
DOI	10.1016/j.coviro.2021.01.001
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Article ; Online: Antibodies for Human Immunodeficiency Virus-1 Cure Strategies.

Rossignol, Evan / Alter, Galit / Julg, Boris

The Journal of infectious diseases

2021 Volume 223, Issue 12 Suppl 2, Page(s) 22–31

Abstract: Human immunodeficiency virus (HIV) infection leads to the establishment of a long-lived latent cellular reservoir. One strategy to eliminate quiescent reservoir cells is to reactivate virus replication to induce HIV envelope glycoprotein (Env) expression ...

Abstract	Human immunodeficiency virus (HIV) infection leads to the establishment of a long-lived latent cellular reservoir. One strategy to eliminate quiescent reservoir cells is to reactivate virus replication to induce HIV envelope glycoprotein (Env) expression on the cell surface exposing them to subsequent antibody targeting. Via the interactions between the antibody Fc domain and Fc-γ receptors (FcγRs) that are expressed on innate effector cells, such as natural killer cells, monocytes, and neutrophils, antibodies can mediate the elimination of infected cells. Over the last decade, a multitude of human monoclonal antibodies that are broadly neutralizing across many HIV-1 subtypes have been identified and are currently being explored for HIV eradication strategies. Antibody development also includes novel Fc engineering approaches to increase engagement of effector cells and optimize antireservoir efficacy. In this review, we discuss the usefulness of antibodies for HIV eradication approaches specifically focusing on antibody-mediated strategies to target latently infected cells and options to increase antibody efficacy.
MeSH term(s)	Animals ; Antibodies, Neutralizing/administration & dosage ; Antibodies, Neutralizing/immunology ; Antibody-Dependent Cell Cytotoxicity ; HIV Antibodies/administration & dosage ; HIV Antibodies/immunology ; HIV Infections/drug therapy ; HIV Infections/immunology ; HIV Infections/virology ; HIV-1/genetics ; HIV-1/immunology ; HIV-1/physiology ; Humans ; Virus Latency
Chemical Substances	Antibodies, Neutralizing ; HIV Antibodies
Language	English
Publishing date	2021-02-14
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	3019-3
ISSN	1537-6613 ; 0022-1899
ISSN (online)	1537-6613
ISSN	0022-1899
DOI	10.1093/infdis/jiaa165
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