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Article ; Online: Immunoglobulin isotype knowledge and application to Fc engineering.

Brezski, Randall J / Georgiou, George

2016 Volume 40, Page(s) 62–69

Abstract: Monoclonal antibody-based drugs continue to be one of the most rapidly growing classes of therapeutic molecules. At present, the majority of approved therapeutic antibodies are of the human IgG1 format, which can elicit immune effector functions (e.g., ... ...

Abstract	Monoclonal antibody-based drugs continue to be one of the most rapidly growing classes of therapeutic molecules. At present, the majority of approved therapeutic antibodies are of the human IgG1 format, which can elicit immune effector functions (e.g., antibody-dependent cellular cytotoxicity, antibody-dependent cellular phagocytosis, and complement-dependent cytotoxicity). However, there is a wealth of functional diversity that is present in other isotypes and IgG subclasses that can be exploited to improve clinical safety and performance by increasing stability, reduction of adverse events, modulation of effector functions, and by the engagement of two antigens by a single antibody. This review presents an overview of the different antibody isotypes and subclasses and details how exchanging amino acids between different isotypes (i.e., 'cross-isotypes') can be exploited to generate novel therapeutic platforms.
MeSH term(s)	Animals ; Antibodies, Bispecific/genetics ; Antibodies, Bispecific/therapeutic use ; Antibodies, Monoclonal/genetics ; Antibodies, Monoclonal/therapeutic use ; Antibody-Dependent Cell Cytotoxicity ; Genetic Engineering ; Humans ; Immunoglobulin Fc Fragments/genetics ; Immunoglobulin Isotypes/genetics ; Immunotherapy/methods ; Immunotherapy/trends ; Phagocytosis
Chemical Substances	Antibodies, Bispecific ; Antibodies, Monoclonal ; Immunoglobulin Fc Fragments ; Immunoglobulin Isotypes
Language	English
Publishing date	2016-06
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	1035767-1
ISSN	1879-0372 ; 0952-7915
ISSN (online)	1879-0372
ISSN	0952-7915
DOI	10.1016/j.coi.2016.03.002
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Article ; Online: IgG Fc engineering to modulate antibody effector functions.

Wang, Xinhua / Mathieu, Mary / Brezski, Randall J

Protein & cell

2017 Volume 9, Issue 1, Page(s) 63–73

Abstract: Therapeutic monoclonal antibodies are among the most effective biotherapeutics to date. An important aspect of antibodies is their ability to bind antigen while at the same time recruit immune effector functions. The majority of approved recombinant ... ...

Abstract	Therapeutic monoclonal antibodies are among the most effective biotherapeutics to date. An important aspect of antibodies is their ability to bind antigen while at the same time recruit immune effector functions. The majority of approved recombinant monoclonal antibody therapies are of the human IgG1 subclass, which can engage both humoral and cellular components of the immune system. The wealth of information generated about antibodies has afforded investigators the ability to molecularly engineer antibodies to modulate effector functions. Here, we review various antibody engineering efforts intended to improve efficacy and safety relative to the human IgG isotype. Further, we will discuss proposed mechanisms by which engineering approaches led to modified interactions with immune components and provide examples of clinical studies using next generation antibodies.
MeSH term(s)	Animals ; Antibodies, Monoclonal/metabolism ; Antigens/metabolism ; Complement System Proteins/metabolism ; Humans ; Immunoglobulin G/metabolism ; Protein Engineering ; Receptors, Fc/metabolism
Chemical Substances	Antibodies, Monoclonal ; Antigens ; Immunoglobulin G ; Receptors, Fc ; Complement System Proteins (9007-36-7)
Language	English
Publishing date	2017-10-06
Publishing country	Germany
Document type	Journal Article ; Review
ISSN	1674-8018
ISSN (online)	1674-8018
DOI	10.1007/s13238-017-0473-8
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Article ; Online: Cleavage of IgGs by proteases associated with invasive diseases: an evasion tactic against host immunity?

Brezski, Randall J / Jordan, Robert E

mAbs

2010 Volume 2, Issue 3, Page(s) 212–220

Abstract: The effective functioning of immunoglobulins and IgG mAbs in removing pathological cells requires that the antigen binding regions and the Fc (effector) domain act in concert. The hinge region that connects these domains itself presents motifs that ... ...

Abstract	The effective functioning of immunoglobulins and IgG mAbs in removing pathological cells requires that the antigen binding regions and the Fc (effector) domain act in concert. The hinge region that connects these domains itself presents motifs that engage Fc receptors on immune effector cells to achieve cell lysis. In addition, sequences in the lower hinge/CH2 and further down the CH2 region are involved in C1q binding and complement-mediated cell killing. Proteolytic enzymes of little relevance to human physiology were successfully used for decades to generate fragments of IgGs for reagent and therapeutic use. It was subsequently noted that tumor-related and microbial proteases also cleaved human IgG specifically in the hinge region. We have shown previously that the "nick" of just one of the lower hinge heavy chains of IgG unexpectedly prevented many effector functions without impacting antigen binding. Of interest, related single-cleaved IgG breakdown products were detected in breast carcinoma extracts. This suggested a pathway by which tumors might avoid host immune surveillance under a cloak of proteolytically-generated, dysfunctional antibodies that block competent IgG binding. The host immune system cannot be blind to this pathway since there exists a widespread, low-titer incidence of anti-hinge (cleavage-site) antibodies in the healthy population. The prevalence of anti-hinge reactivity may reflect an ongoing immune recognition of normal IgG catabolism. Tumor growth and bacterial infections potentially generate hostile proteolytic environments that may pose harsh challenges to host immunity. Recent findings involving physiologically-relevant proteases suggest that the potential loss of key effector functions of host IgGs may result from subtle and limited proteolytic cleavage of IgGs and that such events may facilitate the incursion of invasive cells in local proteolytic settings.
MeSH term(s)	Amino Acid Sequence ; Animals ; Antibodies, Monoclonal/metabolism ; Autoantibodies/immunology ; Bacterial Infections/enzymology ; Bacterial Infections/immunology ; Bacterial Infections/therapy ; Bacterial Proteins/metabolism ; Hinge Exons/genetics ; Hinge Exons/immunology ; Humans ; Immune Evasion ; Immunoglobulin G/immunology ; Immunoglobulin G/metabolism ; Molecular Sequence Data ; Neoplasms/enzymology ; Neoplasms/immunology ; Neoplasms/therapy ; Peptide Hydrolases/metabolism ; Tumor Escape
Chemical Substances	Antibodies, Monoclonal ; Autoantibodies ; Bacterial Proteins ; Immunoglobulin G ; Peptide Hydrolases (EC 3.4.-)
Language	English
Publishing date	2010-05-23
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	2537838-7
ISSN	1942-0870 ; 1942-0870
ISSN (online)	1942-0870
ISSN	1942-0870
DOI	10.4161/mabs.2.3.11780
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Article: B-cell receptor.

Brezski, Randall J / Monroe, John G

Advances in experimental medicine and biology

2008 Volume 640, Page(s) 12–21

Abstract: The subunit structure of the B-cell antigen receptor (BCR) and its associated compartmentalization of function confer enormous flexibility for generating signals and directing these toward specific and divergent cell fate decisions. Like all the ... ...

Abstract	The subunit structure of the B-cell antigen receptor (BCR) and its associated compartmentalization of function confer enormous flexibility for generating signals and directing these toward specific and divergent cell fate decisions. Like all the multichain immune recognition receptors discussed in this volume, assembly of these multi-unit complexes sets these receptors apart from almost all other cell surface signal transduction proteins and affords them the ability to participate in almost all of the diverse aspects of, in this case, B-cell biology. We discuss here the structural aspects of the BCR and its associated coreceptors and relate these mechanistically to how BCR signaling can be directed towards specific fate decisions. By doing so, the BCR plays a pivotal role in ensuring the effective and appropriate B-cell response to antigen.
MeSH term(s)	Animals ; B-Lymphocytes/cytology ; Cell Compartmentation ; Cell Membrane/immunology ; Humans ; Ligands ; Receptors, Antigen, B-Cell/chemistry ; Receptors, Antigen, B-Cell/immunology ; Signal Transduction
Chemical Substances	Ligands ; Receptors, Antigen, B-Cell
Language	English
Publishing date	2008
Publishing country	United States
Document type	Journal Article ; Review
ISSN	2214-8019 ; 0065-2598
ISSN (online)	2214-8019
ISSN	0065-2598
DOI	10.1007/978-0-387-09789-3_2
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Article ; Online: Multivalent human antibody-centyrin fusion protein to prevent and treat Staphylococcus aureus infections.

Buckley, Peter T / Chan, Rita / Fernandez, Jeffrey / Luo, Jinquan / Lacey, Keenan A / DuMont, Ashley L / O'Malley, Aidan / Brezski, Randall J / Zheng, Songmao / Malia, Thomas / Whitaker, Brian / Zwolak, Adam / Payne, Angela / Clark, Desmond / Sigg, Martin / Lacy, Eilyn R / Kornilova, Anna / Kwok, Debra / McCarthy, Steve /

Wu, Bingyuan / Morrow, Brian / Nemeth-Seay, Jennifer / Petley, Ted / Wu, Sam / Strohl, William R / Lynch, Anthony Simon / Torres, Victor J

Cell host & microbe

2023 Volume 31, Issue 5, Page(s) 751–765.e11

Abstract: Treating and preventing infections by antimicrobial-resistant bacterial pathogens is a worldwide problem. Pathogens such as Staphylococcus aureus produce an array of virulence determinants, making it difficult to identify single targets for the ... ...

Abstract	Treating and preventing infections by antimicrobial-resistant bacterial pathogens is a worldwide problem. Pathogens such as Staphylococcus aureus produce an array of virulence determinants, making it difficult to identify single targets for the development of vaccines or monoclonal therapies. We described a human-derived anti-S. aureus monoclonal antibody (mAb)-centyrin fusion protein ("mAbtyrin") that simultaneously targets multiple bacterial adhesins, resists proteolysis by bacterial protease GluV8, avoids Fc engagement by S. aureus IgG-binding proteins SpA and Sbi, and neutralizes pore-forming leukocidins via fusion with anti-toxin centyrins, while maintaining Fc- and complement-mediated functions. Compared with the parental mAb, mAbtyrin protected human phagocytes and boosted phagocyte-mediated killing. The mAbtyrin also reduced pathology, reduced bacterial burden, and protected from different types of infections in preclinical animal models. Finally, mAbtyrin synergized with vancomycin, enhancing pathogen clearance in an animal model of bacteremia. Altogether, these data establish the potential of multivalent mAbs for treating and preventing S. aureus diseases.
MeSH term(s)	Animals ; Humans ; Staphylococcus aureus ; Staphylococcal Infections/drug therapy ; Staphylococcal Infections/prevention & control ; Staphylococcal Infections/microbiology ; Antibodies, Monoclonal/therapeutic use ; Phagocytes/metabolism ; Leukocidins/metabolism ; Leukocidins/therapeutic use ; Methicillin-Resistant Staphylococcus aureus
Chemical Substances	Antibodies, Monoclonal ; Leukocidins
Language	English
Publishing date	2023-04-24
Publishing country	United States
Document type	Journal Article
ZDB-ID	2278004-X
ISSN	1934-6069 ; 1931-3128
ISSN (online)	1934-6069
ISSN	1931-3128
DOI	10.1016/j.chom.2023.04.004
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Article ; Online: Domain-Specific Antibodies Reveal Differences in the Membrane Topologies of Apolipoprotein L1 in Serum and Podocytes.

Gupta, Nidhi / Wang, Xinhua / Wen, Xiaohui / Moran, Paul / Paluch, Maciej / Hass, Philip E / Heidersbach, Amy / Haley, Benjamin / Kirchhofer, Daniel / Brezski, Randall J / Peterson, Andrew S / Scales, Suzie J

Journal of the American Society of Nephrology : JASN

2020 Volume 31, Issue 9, Page(s) 2065–2082

Abstract: Background: Circulating APOL1 lyses trypanosomes, protecting against human sleeping sickness. Two common African gene variants of : Methods: APOL1 topology in serum (HDL particles) and in kidney podocytes was mapped with flow cytometry, ... ...

Abstract	Background: Circulating APOL1 lyses trypanosomes, protecting against human sleeping sickness. Two common African gene variants of Methods: APOL1 topology in serum (HDL particles) and in kidney podocytes was mapped with flow cytometry, immunoprecipitation, and trypanolysis assays that tracked 170 APOL1 domain-specific monoclonal antibodies. Results: APOL1 localizes to the surface of podocytes, with most of the pore-forming domain (PFD) and C terminus of the Serum Resistance Associated-interacting domain (SRA-ID), but not the membrane-addressing domain (MAD), being exposed. In contrast, differential trypanolytic blocking activity reveals that the MAD is exposed in serum APOL1, with less of the PFD accessible. Low pH did not detectably alter the gross topology of APOL1, as determined by antibody accessibility, in serum or on podocytes. Conclusions: Our antibodies highlighted different conformations of native APOL1 topology in serum (HDL particles) and at the podocyte surface. Our findings support the surface ion channel model for APOL1 risk variant-mediated podocyte injury, as well as providing domain accessibility information for designing APOL1-targeted therapeutics.
MeSH term(s)	Animals ; Antibodies/immunology ; Antibody Specificity ; Apolipoprotein L1/analysis ; Apolipoprotein L1/blood ; Apolipoprotein L1/chemistry ; Apolipoprotein L1/immunology ; CHO Cells ; Cell Membrane/chemistry ; Cricetulus ; Humans ; Hydrogen-Ion Concentration ; Podocytes/chemistry ; Podocytes/ultrastructure ; Protein Domains
Chemical Substances	Antibodies ; Apolipoprotein L1
Keywords	covid19
Language	English
Publishing date	2020-08-06
Publishing country	United States
Document type	Journal Article
ZDB-ID	1085942-1
ISSN	1533-3450 ; 1046-6673
ISSN (online)	1533-3450
ISSN	1046-6673
DOI	10.1681/ASN.2019080830
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Article: BCR-linked factors in developmental fate decisions.

Brezski, Randall J / Monroe, John G

Advances in experimental medicine and biology

2007 Volume 596, Page(s) 47–55

MeSH term(s)	Animals ; B-Lymphocytes/cytology ; Cell Lineage ; Cholesterol/metabolism ; Humans ; NF-kappa B/metabolism ; Phospholipase C gamma/metabolism ; Proto-Oncogene Proteins c-myc/metabolism ; Receptors, Antigen, B-Cell/physiology ; Signal Transduction
Chemical Substances	NF-kappa B ; Proto-Oncogene Proteins c-myc ; Receptors, Antigen, B-Cell ; Cholesterol (97C5T2UQ7J) ; Phospholipase C gamma (EC 3.1.4.3)
Language	English
Publishing date	2007
Publishing country	United States
Document type	Journal Article ; Review
ISSN	2214-8019 ; 0065-2598
ISSN (online)	2214-8019
ISSN	0065-2598
DOI	10.1007/0-387-46530-8_4
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Article: B cell antigen receptor-induced Rac1 activation and Rac1-dependent spreading are impaired in transitional immature B cells due to levels of membrane cholesterol.

Brezski, Randall J / Monroe, John G

Journal of immunology (Baltimore, Md. : 1950)

2007 Volume 179, Issue 7, Page(s) 4464–4472

Abstract: The BCR-triggered responses of mature and transitional immature B cells differ at both the biochemical and functional level. In this study, we show that in mature B cells, BCR signaling triggers Vav phosphorylation and Rac1 activation. Furthermore, we ... ...

Abstract	The BCR-triggered responses of mature and transitional immature B cells differ at both the biochemical and functional level. In this study, we show that in mature B cells, BCR signaling triggers Vav phosphorylation and Rac1 activation. Furthermore, we demonstrate that although downstream actin-dependent BCR capping is independent of Rac1 activation, actin-dependent membrane ruffling and cell spreading are Rac1-dependent processes. In contrast, BCR-induced Vav phosphorylation and Rac1 activation is impaired in transitional immature B cells, resulting in defects in actin polymerization-dependent spreading and membrane ruffling while Rac1-independent BCR capping remains intact. Because transitional immature murine B cells maintain lower steady-state levels of plasma membrane cholesterol, we augmented their levels to that of mature B cells and found that BCR-induced Rac1 activation and Rac1-dependent membrane ruffling and cell spreading were restored. These studies provide a direct link between B cell cholesterol levels and downstream cellular signaling processes.
MeSH term(s)	Animals ; Antibodies/immunology ; B-Lymphocytes/cytology ; B-Lymphocytes/immunology ; B-Lymphocytes/metabolism ; Cell Differentiation ; Cell Membrane/metabolism ; Cells, Cultured ; Cholesterol/metabolism ; Enzyme Activation ; JNK Mitogen-Activated Protein Kinases/metabolism ; Mice ; Mice, Inbred BALB C ; Phenotype ; Proto-Oncogene Proteins c-vav/metabolism ; Receptors, Antigen, B-Cell/immunology ; Receptors, Antigen, B-Cell/metabolism ; Signal Transduction ; rac1 GTP-Binding Protein/metabolism
Chemical Substances	Antibodies ; Proto-Oncogene Proteins c-vav ; Receptors, Antigen, B-Cell ; Cholesterol (97C5T2UQ7J) ; JNK Mitogen-Activated Protein Kinases (EC 2.7.11.24) ; rac1 GTP-Binding Protein (EC 3.6.5.2)
Language	English
Publishing date	2007-08-12
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	3056-9
ISSN	1550-6606 ; 0022-1767 ; 1048-3233 ; 1047-7381
ISSN (online)	1550-6606
ISSN	0022-1767 ; 1048-3233 ; 1047-7381
DOI	10.4049/jimmunol.179.7.4464
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Article ; Online: The origins, specificity, and potential biological relevance of human anti-IgG hinge autoantibodies.

Brezski, Randall J / Knight, David M / Jordan, Robert E

TheScientificWorldJournal

2011 Volume 11, Page(s) 1153–1167

Abstract: Human anti-IgG hinge (HAH) autoantibodies constitute a class of immunoglobulins that recognize cryptic epitopes in the hinge region of antibodies exposed after proteolytic cleavage, but do not bind to the intact IgG counterpart. Detailed molecular ... ...

Abstract	Human anti-IgG hinge (HAH) autoantibodies constitute a class of immunoglobulins that recognize cryptic epitopes in the hinge region of antibodies exposed after proteolytic cleavage, but do not bind to the intact IgG counterpart. Detailed molecular characterizations of HAH autoantibodies suggest that they are, in some cases, distinct from natural autoantibodies that arise independent of antigenic challenge. Multiple studies have attempted to define the specificity of HAH autoantibodies, which were originally detected as binding to fragments possessing C-terminal amino acid residues exposed in either the upper or lower hinge regions of IgGs. Numerous investigators have provided information on the isotype profiles of the HAH autoantibodies, as well as correlations among protease cleavage patterns and HAH autoantibody reactivity. Several biological functions have been attributed to HAH autoantibodies, ranging from house-cleaning functions to an immunosuppressive role to restoring function to cleaved IgGs. In this review, we discuss both the historic and current literature regarding HAH autoantibodies in terms of their origins, specificity, and proposed biological relevance.
MeSH term(s)	Antibodies, Anti-Idiotypic/immunology ; Antibodies, Anti-Idiotypic/physiology ; Autoantibodies/immunology ; Autoantibodies/physiology ; B-Lymphocytes/immunology ; B-Lymphocytes/physiology ; Hinge Exons/immunology ; Humans ; Immunoglobulin Fab Fragments/immunology ; Immunoglobulin G/chemistry ; Immunoglobulin G/immunology ; Immunoglobulin G/metabolism ; Models, Immunological
Chemical Substances	Antibodies, Anti-Idiotypic ; Autoantibodies ; Immunoglobulin Fab Fragments ; Immunoglobulin G ; anti-IgG
Language	English
Publishing date	2011-05-26
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	2075968-X
ISSN	1537-744X ; 1537-744X
ISSN (online)	1537-744X
ISSN	1537-744X
DOI	10.1100/tsw.2011.107
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Article ; Online: An Fc engineering approach that modulates antibody-dependent cytokine release without altering cell-killing functions.

Kinder, Michelle / Greenplate, Allison R / Strohl, William R / Jordan, Robert E / Brezski, Randall J

mAbs

2015 Volume 7, Issue 3, Page(s) 494–504

Abstract: Cytotoxic therapeutic monoclonal antibodies (mAbs) often mediate target cell-killing by eliciting immune effector functions via Fc region interactions with cellular and humoral components of the immune system. Key functions include antibody-dependent ... ...

Abstract	Cytotoxic therapeutic monoclonal antibodies (mAbs) often mediate target cell-killing by eliciting immune effector functions via Fc region interactions with cellular and humoral components of the immune system. Key functions include antibody-dependent cell-mediated cytotoxicity (ADCC), antibody-dependent cellular phagocytosis (ADCP), and complement-dependent cytotoxicity (CDC). However, there has been increased appreciation that along with cell-killing functions, the induction of antibody-dependent cytokine release (ADCR) can also influence disease microenvironments and therapeutic outcomes. Historically, most Fc engineering approaches have been aimed toward modulating ADCC, ADCP, or CDC. In the present study, we describe an Fc engineering approach that, while not resulting in impaired ADCC or ADCP, profoundly affects ADCR. As such, when peripheral blood mononuclear cells are used as effector cells against mAb-opsonized tumor cells, the described mAb variants elicit a similar profile and quantity of cytokines as IgG1. In contrast, although the variants elicit similar levels of tumor cell-killing as IgG1 with macrophage effector cells, the variants do not elicit macrophage-mediated ADCR against mAb-opsonized tumor cells. This study demonstrates that Fc engineering approaches can be employed to uncouple macrophage-mediated phagocytic and subsequent cell-killing functions from cytokine release.
MeSH term(s)	Antibodies, Monoclonal/genetics ; Antibodies, Monoclonal/immunology ; Antibodies, Monoclonal/pharmacology ; Antibodies, Neoplasm/genetics ; Antibodies, Neoplasm/immunology ; Antibodies, Neoplasm/pharmacology ; Antibody-Dependent Cell Cytotoxicity/drug effects ; Antibody-Dependent Cell Cytotoxicity/genetics ; Cell Line, Tumor ; Cytokines/immunology ; Humans ; Immunoglobulin Fc Fragments/genetics ; Immunoglobulin Fc Fragments/immunology ; Immunoglobulin Fc Fragments/pharmacology ; Macrophages/immunology ; Neoplasms/drug therapy ; Neoplasms/immunology ; Protein Engineering ; Tumor Microenvironment/drug effects ; Tumor Microenvironment/immunology
Chemical Substances	Antibodies, Monoclonal ; Antibodies, Neoplasm ; Cytokines ; Immunoglobulin Fc Fragments
Language	English
Publishing date	2015
Publishing country	United States
Document type	Journal Article
ISSN	1942-0870
ISSN (online)	1942-0870
DOI	10.1080/19420862.2015.1022692
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