• AGI-134
• APC recruitment
• anti-Gal antibody
• cancer immunotherapy
• tumor antigens
• α-gal epitope
• α-gal glycolipids
• α-gal micelles
• α-gal therapy

• Adaptive immunity
• Immunology

• Animals
• Mice
• Complement C3
• Lymphoid Tissue
• B-Lymphocytes
• Erythrocytes
• Immunoglobulin G
• Interferon-alpha

• P01 HL132819 NHLBI NIH HHS
• National Heart, Lung, and Blood Institute

• B-cell epitope
• factor VIII
• hemophilia
• humoral response
• immune complex

• Animals
• Mice
• Factor VIII
• Antigen-Antibody Complex
• Hemophilia A
• Epitopes
• Hemostatics
• Immunoglobulin G

• K12 HD072245 NICHD NIH HHS
• K99 HL150595 NHLBI NIH HHS
• U54 HL141981 NHLBI NIH HHS
• National Institutes of Health
• Hemophilia of Georgia
• Hemostasis and Thrombosis Research Society

Vidutolimod, also known as CMP-001, is a virus-like particle composed of the Qβ bacteriophage coat protein encasing a TLR9 agonist. Vidutolimod injected intratumorally is showing promise in early phase clinical trials based on its ability to alter the tumor microenvironment and induce an anti-tumor immune response. We previously demonstrated that the in vivo efficacy of vidutolimod is dependent on the presence of anti-Qβ antibodies that enhance opsonization and uptake of vidutolimod by TLR9-expressing plasmacytoid dendritic cells (pDCs). Here, we evaluated the effect of immune complexes, including anti-Qβ-coated vidutolimod, on induction of Type 1 Interferon production by peripheral blood mononuclear cells in response to vidutolimod and soluble TLR9 agonists. Immune complexes, including but not limited to anti-Qβ-coated vidutolimod, indirectly suppressed TLR9-mediated Type 1 Interferon production by pDCs in a monocyte-dependent manner. These findings indicate that anti-Qβ-coated vidutolimod has effects in addition to those mediated by TLR9 that could have important clinical implications for understanding the mechanism of action of this exciting new approach to in situ immunization and cancer immunotherapy.

• Fc gamma receptor
• TLR9
• Type 1 Interferon
• monocytes
• pDCs
• vidutolimod

Immune complexes (ICs) made of antibody-bound antigens exhibit immunomodulatory activities exploitable in a vaccination strategy to optimize vaccine efficacy. The modulatory effects of ICs are typically attributed to the Fc fragments of the antibody components, which engage Fc receptors, complement and complement receptors on various immune cells. These Fc-mediated functions facilitate the critical interplay between innate and adaptive immune systems to impact the quality and quantity of the elicited adaptive responses. In addition to the Fc contribution, the Fab fragment also plays an immunoregulation role. The antigen-binding domains of the Fab fragment can bind their specific epitopes at high affinity to sterically occlude these antigenic sites from recognition by other antibodies. Moreover, the Fab-mediated binding has been demonstrated to induce allosteric alterations at nearby or distant antigenic sites. In this review article, we survey published studies to illuminate how the immunomodulatory functions of ICs have been investigated or utilized in a vaccination strategy to fight against an array of infectious pathogens, culminating with IC vaccine designs aimed at preventing HIV-1 infection. In particular, we highlight IC vaccine candidates that exploit Fab-mediated steric and allosteric effects to direct antibody responses away or toward the V1V2 domain, the V3 loop, and other antigenic sites on the HIV-1 envelope gp120 glycoprotein. Like other HIV-1 vaccine approaches, the path for IC-based vaccines to reach the clinic faces major hurdles yet to be overcome; however, investigations into this vaccine strategy have provided insights into the multifaceted activities of antibodies beyond their conventional roles in the host defense against HIV-1 and other microbial pathogens.

• Fab
• Fc
• HIV-1
• allosteric
• antibodies
• immune complex
• steric
• vaccine

• Covid-19 vaccine
• Glycan shield
• S-protein
• SARS-CoV-2
• anti-Gal
• α-gal epitopes

• Animals
• Antibodies, Viral/biosynthesis
• Antigens, Viral/genetics
• Antigens, Viral/immunology
• Antigens, Viral/metabolism
• Betacoronavirus/drug effects
• Betacoronavirus/immunology
• Betacoronavirus/pathogenicity
• COVID-19
• COVID-19 Vaccines
• Coronavirus Infections/genetics
• Coronavirus Infections/immunology
• Coronavirus Infections/prevention & control
• Coronavirus Infections/virology
• Dendritic Cells/drug effects
• Dendritic Cells/immunology
• Dendritic Cells/virology
• Genetic Engineering
• HIV Core Protein p24/chemistry
• HIV Core Protein p24/genetics
• HIV Core Protein p24/immunology
• HIV Envelope Protein gp120/chemistry
• HIV Envelope Protein gp120/genetics
• HIV Envelope Protein gp120/immunology
• Humans
• Immunogenicity, Vaccine
• Macrophages/drug effects
• Macrophages/immunology
• Macrophages/virology
• Mice
• Pandemics/prevention & control
• Pneumonia, Viral/immunology
• Pneumonia, Viral/prevention & control
• Pneumonia, Viral/virology
• Recombinant Fusion Proteins/chemistry
• Recombinant Fusion Proteins/genetics
• Recombinant Fusion Proteins/immunology
• SARS-CoV-2
• Spike Glycoprotein, Coronavirus/genetics
• Spike Glycoprotein, Coronavirus/immunology
• Spike Glycoprotein, Coronavirus/metabolism
• Trisaccharides/chemistry
• Trisaccharides/immunology
• Viral Vaccines/administration & dosage
• Viral Vaccines/biosynthesis
• Viral Vaccines/genetics
• Viral Vaccines/immunology

• Hepatitis B virus
• chronic hepatitis B
• dendritic cells
• fusion protein
• immunotherapy

• Immunotherapy
• dendritic cells
• fusion protein
• hepatitis B virus
• immune responses
• vaccine

Dendritic cells (DCs) express Fcγ receptors (FcγRs) for the binding immune complexes (ICs) consisting of IgG and antigens (Ags). IC–FcγR interactions have been demonstrated to enhance activation and antigen-presenting functions of DCs. Utilizing Friend virus (FV), an oncogenic mouse retrovirus, we investigated the effect of IgG-opsonization of retroviral particles on the infection of DCs and the subsequent presentation of viral antigens by DCs to virus-specific CD8 T cells. We found that opsonization by virus-specific non-neutralizing IgG abrogated DC infection and as a consequence significantly reduced the capacity of DCs to activate virus-specific CD8 T cells. Effects of IgG-opsonization were mediated by the high-affinity FcγR type I, CD64, expressed on DCs. Our results suggest that different opsonization patterns on the retroviral surface modulate infection and antigen-presenting functions of DCs, whereby, in contrast to complement, IgG reduces the capacity of DCs to activate cytotoxic T cell (CTL) responses.

• CD8 T cells
• Fcγ receptors
• IgG-opsonization
• dendritic cells
• friend virus

• B cells · T cells · μMT−/− mice · memory precursor effector cells · TLR4 agonist

• Adoptive Transfer
• Animals
• Antigen Presentation
• B-Lymphocytes/physiology
• B-Lymphocytes/transplantation
• Cell Differentiation
• Cells, Cultured
• Humans
• Immunoglobulin mu-Chains/genetics
• Immunologic Factors/immunology
• Immunologic Memory
• Lymphocyte Activation
• Mice
• Mice, Knockout
• T-Lymphocyte Subsets/immunology
• T-Lymphocyte Subsets/transplantation
• Th1 Cells/immunology
• Toll-Like Receptor 4/agonists
• Tuberculosis/immunology
• Tuberculosis/prevention & control
• Tuberculosis Vaccines/immunology

• HHSN272200800045C NIAID NIH HHS
• U01 AI078054 NIAID NIH HHS

In the pathogenesis of central nervous system (CNS) demyelinating disorders, antigen-specific B cells are implicated to act as potent antigen-presenting cells (APC), eliciting waves of inflammatory CNS infiltration. Here, we provide the first evidence that CNS-reactive antibodies (Ab) are similarly capable of initiating an encephalitogenic immune response by targeting endogenous CNS antigen to otherwise inert myeloid APC. In a transgenic mouse model, constitutive production of Ab against myelin oligodendrocyte glycoprotein (MOG) was sufficient to promote spontaneous experimental autoimmune encephalomyelitis (EAE) in the absence of B cells, when mice endogenously contained MOG-recognizing T cells. Adoptive transfer studies corroborated that anti-MOG Ab triggered activation and expansion of peripheral MOG-specific T cells in an Fc-dependent manner, subsequently causing EAE. To evaluate the underlying mechanism, anti-MOG Ab were added to a co-culture of myeloid APC and MOG-specific T cells. At otherwise undetected concentrations, anti-MOG Ab enabled Fc-mediated APC recognition of intact MOG; internalized, processed and presented MOG activated naïve T cells to differentiate in an encephalitogenic manner. In a series of translational experiments, anti-MOG Ab from two patients with an acute flare of CNS inflammation likewise facilitated detection of human MOG. Jointly, these observations highlight Ab-mediated opsonization of endogenous CNS auto-antigen as a novel disease- and/or relapse-triggering mechanism in CNS demyelinating disorders.

• Auto-antibodies
• Experimental autoimmune encephalomyelitis
• Fc receptor
• Multiple sclerosis
• Myeloid antigen-presenting cells
• Opsonization

• Animals
• Autoantibodies/immunology
• B-Lymphocytes/immunology
• Coculture Techniques
• Encephalomyelitis, Autoimmune, Experimental/immunology
• Female
• HEK293 Cells
• Humans
• Immunoglobulin G/metabolism
• Mice, Inbred C57BL
• Mice, Transgenic
• Middle Aged
• Multiple Sclerosis/immunology
• Myelin-Oligodendrocyte Glycoprotein/antagonists & inhibitors
• Myelin-Oligodendrocyte Glycoprotein/genetics
• Myelin-Oligodendrocyte Glycoprotein/immunology
• Myelin-Oligodendrocyte Glycoprotein/metabolism
• Neuromyelitis Optica/immunology
• Receptors, IgG/deficiency
• Receptors, IgG/genetics
• T-Lymphocytes/immunology

• National Multiple Sclerosis Society
• Deutsche Forschungsgemeinschaft
• Universitätsmedizin Göttingen
• National Health and Medical Research Council of Australia
• Department of Industry, Commonwealth of Australia
• Fundació la Marató de TV3

• B cells
• EAE
• autoantibodies
• autoimmunity
• multiple sclerosis

The α-Gal epitope (Galα1,3Galα1,4GlcNAc-R) is ubiquitously presented in non-primate mammals, marsupials and New World Monkeys, but it is absent in humans, apes and Old World monkeys. However, the anti-Gal antibody (~1% of immunoglobulins) is naturally generated in human, and is found as the immunoglobulin G (IgG), IgM and IgA isotypes. Owing to the specific binding of the anti-Gal antibody with the α-Gal epitope, humans have a distinct anti-α-gal reactivity, which is responsible for hyperacute rejection of organs transplanted from α-gal donors. In addition, the α1,3 galactosyltransferases (α1,3GT) can catalyze the synthesis of the α-Gal epitope. Therefore, the α1,3GT gene, which encodes the α1,3GT, is developed profoundly. The distributions of the α-Gal epitope and anti-Gal antibody, and the activation of α1,3GT, reveal that the enzyme of α1,3GT in ancestral primates is ineffective. Comparison of the nucleotide sequence of the human α1,3-GT pseudogene to the corresponding different species sequence, and according to the evolutionary tree of different species, the results of evolutionary inactivation of the α1,3GT gene in ancestral primates attribute to the mutations under a stronger selective pressure. However, on the basis of the structure, the mechanism and the specificity of the α-Gal epitope and anti-Gal antibody, they can be applied to clinical exploitation. Knocking out the α1,3GT gene will eliminate the xenoantigen, Gal(α1,3)Gal, so that the transplantation of α1,3GT gene knockout pig organ into human becomes a potential clinically acceptable treatment for solving the problem of organ shortage. By contrast, the α-Gal epitope expressed through the application of chemical, biochemical and genetic engineering can be exploited for the clinical use. Targeting anti-Gal-mediated autologous tumor vaccines, which express α-Gal epitope to antigen-presenting cells, would increase their immunogenicity and elicit an immune response, which will be potent enough to eradicate the residual tumor cells. For tumor vaccines, the way of increasing immunogenicity of certain viral vaccines, including flu vaccines and human immunodeficiency virus vaccines, can also be used in the elderly. Recently, α-Gal epitope nanoparticles have been applied to accelerate wound healing and further directions on regeneration of internally injured tissues.

Specific immune suppression in newly hatched chicks induced by specific maternal antibodies has been reported. Laying hens were immunized with dinitrophenyl-keyhole limpet hemocyanin (DNP-KLH). Purified maternal anti-DNP and non-specific immunoglobulin (Ig) Y antibodies were transferred by yolk sac inoculation to newly hatched chicks, and then, they were immunized with an optimum immunogenic dose of DNP-KLH at 1 and 4 weeks of age. Concentrations of anti-DNP antibodies in serum samples of these chicks were measured by using Enzyme-linked immunosorbent assay (ELISA). Proportions of T-cell subsets in peripheral blood of these chicks were also measured by flow cytometric analysis at 5 weeks of age (one week after the second immunization). Suppression of anti-DNP antibody response and down-regulation of CD3⁺CD4⁺ cells were observed in the chicks received high dose of maternal anti-DNP antibodies and immunized with DNP-KLH. On the other hand, normal anti-DNP antibody response and normal proportion of CD3⁺CD4⁺ cells were observed in the chicks received high dose of non-specific IgY antibodies and immunized with DNP-KLH. Furthermore, when chicks received high dose of maternal anti-DNP antibodies and immunized with DNP-KLH at 1 and 4 weeks of age and then with rabbit serum albumin (RSA) at 5 and 8 weeks of age, their primary anti-RSA response was also significantly suppressed. We indicate here that specific maternal antibodies can affect both B and T cell responses and induce non-specific suppression against different antigens. However, this non-specific suppression does not continue for a long time.

• Antibiotic resistance
• antibody
• antitoxin
• clinical
• disease
• gastrointestinal
• immunoglobulin
• monoclonal
• peroral
• polyclonal

• myelin basic protein
• autoimmune thyroid disease
• pulmonary alveolar proteinosis
• thyroid peroxidase

• Antigen-Presenting Cells/immunology
• Autoantibodies/immunology
• Autoantibodies/metabolism
• Autoantigens/immunology
• Autoimmune Diseases/immunology
• Communicable Diseases/immunology
• Complement Activation
• Complement System Proteins/immunology
• Cytokines/immunology
• Cytokines/metabolism
• Humans
• Inflammation/immunology
• Protein Binding
• Receptors, Complement/immunology
• Receptors, Complement/metabolism
• Receptors, Fc/immunology
• Receptors, Fc/metabolism
• T-Lymphocytes/immunology
• Thyroglobulin/immunology

• R01 DK026190 NIDDK NIH HHS

AIM: To evaluate the safety and clinical efficacy of a new immunotherapy using both α-Gal epitope-pulsed dendritic cells (DCs) and cytokine-induced killer cells.

METHODS: Freshly collected hepatocellular carcinoma (HCC) tumor tissues were incubated with a mixture of neuraminidase and recombinant α1,3-galactosyltransferase (α1,3GT) to synthesize α-Gal epitopes on carbohydrate chains of the glycoproteins of tumor membranes. The subsequent incubation of the processed membranes in the presence of human natural anti-Gal IgG resulted in the effective phagocytosis to the tumor membrane by DCs. Eighteen patients aged 38-78 years with stage III primary HCC were randomLy chosen for the study; 9 patients served as controls, and 9 patients were enrolled in the study group.

RESULTS: The evaluation demonstrated that the procedure was safe; no serious side effects or autoimmune diseases were observed. The therapy significantly prolonged the survival of treated patients as compared with the controls (17.1 ± 2.01 mo vs 10.1 ± 4.5 mo, P = 0.00121). After treatment, all patients in the study group had positive delayed hypersensitivity and robust systemic cytotoxicity in response to tumor lysate as measured by interferon-γ-expression in peripheral blood mononuclear cells using enzyme-linked immunosorbent spot assay. They also displayed increased numbers of CD8-, CD45RO- and CD56-positive cells in the peripheral blood and decreased α-fetoprotein level in the serum.

CONCLUSION: This new tumor-specific immunotherapy is safe, effective and has a great potential for the treatment of tumors.

• Hepatocellular carcinoma
• α-Gal epitope
• Dendritic cell
• Tumor-associated antigen
• Dendritic cell-activated cytokine-induced killer cell

Anti-Gal is the most abundant antibody in humans, constituting 1% of immunoglobulins. Anti-Gal binds specifically α-gal epitopes (Galα1-3Galβ1-4GlcNAc-R). Immunogenicity of autologous tumor associated antigens (TAA) is greatly increased by manipulating tumor cells to express α-gal epitopes and bind anti-Gal. Glycolipids with αgal epitopes (α-gal glycolipids) injected into tumors insert into the tumor cell membrane. Anti-Gal binding to the multiple α-gal epitopes de novo presented on the tumor cells results in targeting of these cells to APC via the interaction between the Fc portion of the bound anti-Gal and Fcγ; receptors on APC. The APC process and present immunogenic TAA peptides and thus, effectively activate tumor specific CD4+ helper T cells and CD8+ cytotoxic T cells which destroy tumor cells in micrometastases. The induced immune response is potent enough to overcome immunosuppression by Treg cells. A phase I clinical trial indicated that α-gal glycolipid treatment has no adverse effects. In addition to achieving destruction of micrometastases in cancer patients with advance disease, α-gal glycolipid treatment may be effective as neo-adjuvant immunotherapy. Injection of α-gal glycolipids into primary tumors few weeks prior to resection can induce a protective immune response capable of destroying micrometastases expressing autologous TAA, long after primary tumor resection.

Autologous melanoma associated antigens (MAA) on murine melanoma cells can elicit a protective anti-tumor immune response following a variety of vaccine strategies. Most require effective uptake by antigen presenting cells (APC). APC transport and process internalized MAA for activation of anti-tumor T cells. One potential problem with clinical melanoma vaccines against autologous tumors may be that often tumor cells do not express surface markers that label them for uptake by APC. Effective uptake of melanoma cells by APC might be achieved by exploiting the natural anti-Gal antibody which constitutes ~1% of immunoglobulins in humans. This approach has been developed in a syngeneic mouse model using mice capable of producing anti-Gal. Anti-Gal binds specifically to α-gal epitopes (Galα1-3Galβ1-4GlcNAc-R). Injection of glycolipids carrying α-gal epitopes (α-gal glycolipids) into melanoma lesions results in glycolipid insertion into melanoma cell membranes, expression of α-gal epitopes on the tumor cells and binding of anti-Gal to these epitopes. Interaction between the Fc portions of bound anti-Gal and Fcγ receptors on APC induces effective uptake of tumor cells by APC. The resulting anti-MAA immune response can be potent enough to destroy distant micrometastases. A clinical trial is now open testing effects of intratumoral α-gal glycolipid injections in melanoma patients.

HIV-1 exposure causes several dramatic unbalances in the immune system homeostasis. Here, we will focus on the paradox whereby CD4 specific autoimmune responses, which are expected to contribute to the catastrophic loss of most part of the T helper lymphocyte subset in infected patients, may display the characteristics of an unconventional protective immunity in individuals naturally resistant to HIV-1 infection. Reference to differences in fine epitope mapping of these two oppositely polarized outcomes will be presented, with particular reference to partially or totally CD4-gp120 complex-specific antibodies. The fine tuning of the anti-self immune response to the HIV-1 receptor may determine whether viral exposure will result in infection or, alternatively, protective immunity.

Along this line, an efficacious anti-HIV strategy can rely on the active (i.e., through immunization) or passive targeting of cryptic epitopes of the CD4-gp120 complex, including those harboured within the CD4 molecule. Such epitopes are expected to be safe from genetic drift and thus allow for broad spectrum of efficacy. Moreover, since these epitopes are not routinely exposed in uninfected individuals, they are expected to become targets of neutralizing antibodies or other specifically designed molecules only after viral exposure, with a predictable low impact in terms of potentially harmful anti-CD4 self-reactivity.

The experimentum naturae of naturally resistant individuals indicates a strategy to design innovative strategies to neutralize HIV-1 by acting on the sharp edge between harmful and protective self-reactivity.

• Animals
• Antibodies, Monoclonal/adverse effects
• Antibodies, Monoclonal/pharmacology
• Antibodies, Monoclonal/therapeutic use
• Antibodies, Monoclonal, Murine-Derived
• Antigen-Presenting Cells/drug effects
• Autoantibodies/blood
• Autoimmune Diseases/drug therapy
• B-Lymphocytes/drug effects
• B-Lymphocytes/physiology
• Graves Disease/drug therapy
• Graves Ophthalmopathy/drug therapy
• Graves Ophthalmopathy/immunology
• Humans
• Immunoglobulins/blood
• Lymphocyte Depletion
• Receptors, Thyrotropin/immunology
• Rituximab
• T-Lymphocytes/drug effects

• Adhesins, Bacterial/immunology
• Animals
• Antibodies, Bacterial/immunology
• Antibodies, Monoclonal/immunology
• Antigen-Antibody Complex/immunology
• Bacterial Adhesion
• Complement Activation
• Female
• Immunization
• Mice
• Mice, Inbred BALB C
• Phagocytosis
• Streptococcus mutans/immunology

• DE013882 NIDCR NIH HHS

• Animals
• Antibodies, Viral/blood
• Antigen-Presenting Cells/immunology
• CD4-Positive T-Lymphocytes/immunology
• CD8-Positive T-Lymphocytes/immunology
• Cytokines/biosynthesis
• Disease Models, Animal
• Drug Delivery Systems/methods
• Enzyme-Linked Immunosorbent Assay
• Flow Cytometry
• Hemagglutination Inhibition Tests
• Humans
• Influenza A Virus, H1N1 Subtype/chemistry
• Influenza A Virus, H1N1 Subtype/immunology
• Influenza Vaccines/administration & dosage
• Influenza Vaccines/immunology
• Influenza, Human/prevention & control
• Mice
• Mice, Inbred C57BL
• Mice, Knockout
• Survival Analysis
• Trisaccharides/immunology

• R01 CA034461 NCI NIH HHS
• AI07439 NIAID NIH HHS
• CA34461 NCI NIH HHS

• Adjuvants, Immunologic/administration & dosage
• Adjuvants, Immunologic/biosynthesis
• Adjuvants, Immunologic/genetics
• Adjuvants, Immunologic/metabolism
• Animals
• Antigens/immunology
• Antigens/metabolism
• Cell Line, Tumor
• Humans
• Immunoglobulin G/administration & dosage
• Immunoglobulin G/biosynthesis
• Immunoglobulin G/genetics
• Ligands
• Mice
• Peptide Fragments/immunology
• Peptide Fragments/metabolism
• Receptors, IgG/administration & dosage
• Receptors, IgG/genetics
• Receptors, IgG/metabolism
• Serum Albumin/biosynthesis
• Serum Albumin/genetics
• Serum Albumin/metabolism
• Serum Albumin/physiology
• Spodoptera
• U937 Cells

• 1 R21 AI058003 NIAID NIH HHS
• 1 R41 AI060257 NIAID NIH HHS

• Animals
• Antibodies, Bacterial/biosynthesis
• Female
• Immunity, Cellular
• Liver/immunology
• Liver/microbiology
• Male
• Mice
• Mice, Inbred C57BL
• Receptors, IgG/immunology
• Salmonella Infections/immunology
• Salmonella Infections/microbiology
• Salmonella Infections/prevention & control
• Salmonella Vaccines/immunology
• Salmonella typhimurium/growth & development
• Salmonella typhimurium/immunology
• Salmonella typhimurium/pathogenicity
• Spleen/immunology
• Spleen/microbiology
• T-Lymphocyte Subsets/immunology
• Virulence

• G0001245 Medical Research Council

• Antibodies, Bacterial/analysis
• Antigens, Bacterial/analysis
• Antigens, CD/analysis
• B-Lymphocytes/immunology
• Cytokines/analysis
• Histocytochemistry
• Humans
• Leprosy
• Macrophages/immunology
• Mycobacterium leprae/immunology
• Skin/immunology
• T-Lymphocytes/immunology
• Tissue Culture Techniques

• dendritic cells
• macrophages
• antigen presentation/processing
• fc receptors

• Animals
• Antigen Presentation/immunology
• Antigen-Antibody Complex/metabolism
• B-Lymphocytes/immunology
• CD4-Positive T-Lymphocytes/immunology
• Cell Proliferation
• Dendritic Cells/immunology
• Histocompatibility Antigens Class II/metabolism
• Immunoglobulin G/immunology
• Lymphocyte Activation/immunology
• Macrophages/immunology
• Mice
• Mice, Inbred BALB C

• Animals
• Antibody Formation
• Feedback, Physiological
• Humans
• Immune Tolerance
• Immunoglobulin G/immunology
• Immunoglobulin M/immunology
• Models, Immunological

• AIDS Vaccines/genetics
• AIDS Vaccines/immunology
• AIDS Vaccines/pharmacology
• Animals
• Antibody Formation/drug effects
• Antibody Formation/immunology
• Antigen-Antibody Complex/immunology
• Antigen-Presenting Cells/immunology
• CHO Cells
• Cricetinae
• Cricetulus
• Gene Expression
• HIV Antibodies/immunology
• HIV Envelope Protein gp120/genetics
• HIV Envelope Protein gp120/immunology
• HIV Envelope Protein gp120/pharmacology
• HIV Infections/immunology
• HIV Infections/prevention & control
• Humans
• Immunization
• Immunoglobulin G/immunology
• Mice
• Mice, Knockout
• Polysaccharides/genetics
• Polysaccharides/immunology
• Polysaccharides/pharmacology
• Protein Engineering
• Receptors, IgG/immunology

• R21 AI058749 NIAID NIH HHS
• AI58749 NIAID NIH HHS

• Animals
• Antigen Presentation/drug effects
• Antigen Presentation/immunology
• Antigen-Antibody Complex/immunology
• Antigen-Antibody Complex/pharmacology
• CD8-Positive T-Lymphocytes/cytology
• CD8-Positive T-Lymphocytes/immunology
• Cell Proliferation/drug effects
• Cells, Cultured
• Complement C3/deficiency
• Complement C3/immunology
• Mice
• Mice, Knockout
• Receptors, Complement/immunology
• Receptors, IgG/deficiency
• Receptors, IgG/immunology

• Adoptive Transfer
• Animals
• Antibody Formation/drug effects
• Antibody Formation/immunology
• Antigen Presentation/drug effects
• Antigen Presentation/immunology
• CD4-Positive T-Lymphocytes/immunology
• Hemocyanins/immunology
• Immunoglobulin G/immunology
• Immunoglobulin G/pharmacology
• Lymphocyte Activation/drug effects
• Lymphocyte Activation/immunology
• Mice
• Mice, Inbred BALB C
• Mice, Knockout
• Mice, Transgenic
• Ovalbumin/immunology
• Picrates/immunology
• Receptors, IgG/genetics
• Receptors, IgG/immunology
• Vaccination