scholarly journals Correction: High Affinity IgG Antibodies Develop Naturally in Ig-Knockout Rats Carrying Germline Human IgH/Igκ/Igλ Loci Bearing the Rat CH Region

2013 ◽  
Vol 190 (12) ◽  
pp. 6707-6707 ◽  
Author(s):  
Michael J. Osborn ◽  
Biao Ma ◽  
Suzanne Avis ◽  
Ashleigh Binnie ◽  
Jeanette Dilley ◽  
...  
Keyword(s):  
Igg Antibodies ◽  
High Affinity

scholarly journals Deficiency in Serum Immunoglobulin (Ig)m Predisposes to Development of Igg Autoantibodies

2000 ◽  
Vol 191 (7) ◽  
pp. 1253-1258 ◽  
Author(s):  
Michael R. Ehrenstein ◽  
H. Terence Cook ◽  
Michael S. Neuberger
Keyword(s):  
Immune Response ◽  
Initial Response ◽  
Regulatory Role ◽  
Serum Immunoglobulin ◽  
Igg Antibodies ◽  
Foreign Antigen ◽  
High Affinity ◽  
Serum Igg ◽  
Dna Antibodies ◽  
Self Antigens

Serum immunoglobulin (Ig)M provides the initial response to foreign antigen and plays a regulatory role in subsequent immune response development, accelerating the production of high-affinity IgG. Here we show that mice deficient in serum IgM have an increased propensity to spontaneous autoimmunity as judged by the development with age of serum IgG anti-DNA antibodies and the renal deposition of IgG and complement. They also exhibit augmented anti-DNA IgG production on exposure to lipopolysaccharide. Thus, deficiency in serum IgM leads to diminished responsiveness to foreign antigens but increased responsiveness to self—a paradoxical association reminiscent of that described in humans deficient in complement or IgA. We wondered whether serum IgM might play an analogous role with regard to the response to self-antigens. However, here—in contrast to the sluggish response to foreign antigens—we find that deficiency in serum IgM actually predisposes to the development of IgG antibodies to autoantigens.

scholarly journals Serologic profile of alphamethyldopa-induced hemolytic anemia: correlation between cell-bound IgM and hemolysis

Blood ◽  
1982 ◽  
Vol 59 (1) ◽  
pp. 61-68
Author(s):  
P Lalezari ◽  
JE Louie ◽  
N Fadlallah
Keyword(s):  
Hemolytic Anemia ◽  
Complement Activation ◽  
Hemolytic Activity ◽  
Igg Antibodies ◽  
Cold Agglutinins ◽  
High Affinity ◽  
Igm Antibodies ◽  
Antiglobulin Test ◽  
Complement C1q ◽  
Classic Pathway

Erythrocyte-bound immunoglobulins have been characterized by a PVP- potentiated antiglobulin test in 11 patients who had developed antibodies after treatment with alpha-methyldopa. Serologic profiles were recognized that could distinguish between the hemolyzing and nonhemolyzing patients: IgM antibodies together with the first component of complement (C1q) were demonstrated on erythrocytes of all eight hemolyzing patients. By contrast, these immunoproteins were absent from the cells of nonhemolyzing patients and became undetectable when the hemolyzing patients recovered. IgG and its subclasses were variably present on erythrocytes of all patients regardless of hemolytic activity. Eluates prepared from erythrocytes of the hemolyzing patients were shown to contain both IgG and IgM, and fixes C1q, C3, and C4. Eluates from the nonhemolyzing patients contained only IgG. The IgM antibodies differed from the commonly occurring cold agglutinins in that they were warm-reactive and were mainly concentrated on the patients' cells rather than being free in the serum. Because of their nonagglutinating property, it is suggested that they are monomeric IgM. It is concluded that the high affinity, warm- reactive IgM and not the IgG antibodies are primarily responsible for clinically manifest anemia in patients receiving alphamethyldopa and that the hemolytic activity is probably mediated by the classic pathway of complement activation.

High-Affinity Anti-Ganglioside IgG Antibodies Raised in Complex Ganglioside Knockout Mice

2001 ◽  
Vol 75 (1) ◽  
pp. 404-412 ◽  
Author(s):  
Michael P. T. Lunn ◽  
L'Aurelle A. Johnson ◽  
Susan E. Fromholt ◽  
Saki Itonori ◽  
Jian Huang ◽  
...  
Keyword(s):  
Knockout Mice ◽  
Igg Antibodies ◽  
High Affinity ◽  
Complex Ganglioside

scholarly journals High-Affinity IgG Antibodies Develop Naturally in Ig-Knockout Rats Carrying Germline Human IgH/Igκ/Igλ Loci Bearing the Rat CHRegion

2013 ◽  
Vol 190 (4) ◽  
pp. 1481-1490 ◽  
Author(s):  
Michael J. Osborn ◽  
Biao Ma ◽  
Suzanne Avis ◽  
Ashleigh Binnie ◽  
Jeanette Dilley ◽  
...  
Keyword(s):  
Igg Antibodies ◽  
High Affinity

scholarly journals Serologic profile of alphamethyldopa-induced hemolytic anemia: correlation between cell-bound IgM and hemolysis

Blood ◽  
1982 ◽  
Vol 59 (1) ◽  
pp. 61-68 ◽  
Author(s):  
P Lalezari ◽  
JE Louie ◽  
N Fadlallah
Keyword(s):  
Hemolytic Anemia ◽  
Complement Activation ◽  
Hemolytic Activity ◽  
Igg Antibodies ◽  
Cold Agglutinins ◽  
High Affinity ◽  
Igm Antibodies ◽  
Antiglobulin Test ◽  
Complement C1q ◽  
Classic Pathway

Abstract Erythrocyte-bound immunoglobulins have been characterized by a PVP- potentiated antiglobulin test in 11 patients who had developed antibodies after treatment with alpha-methyldopa. Serologic profiles were recognized that could distinguish between the hemolyzing and nonhemolyzing patients: IgM antibodies together with the first component of complement (C1q) were demonstrated on erythrocytes of all eight hemolyzing patients. By contrast, these immunoproteins were absent from the cells of nonhemolyzing patients and became undetectable when the hemolyzing patients recovered. IgG and its subclasses were variably present on erythrocytes of all patients regardless of hemolytic activity. Eluates prepared from erythrocytes of the hemolyzing patients were shown to contain both IgG and IgM, and fixes C1q, C3, and C4. Eluates from the nonhemolyzing patients contained only IgG. The IgM antibodies differed from the commonly occurring cold agglutinins in that they were warm-reactive and were mainly concentrated on the patients' cells rather than being free in the serum. Because of their nonagglutinating property, it is suggested that they are monomeric IgM. It is concluded that the high affinity, warm- reactive IgM and not the IgG antibodies are primarily responsible for clinically manifest anemia in patients receiving alphamethyldopa and that the hemolytic activity is probably mediated by the classic pathway of complement activation.

Isolation of high-affinity human IgE and IgG antibodies recognising Bet v 1 and Humicola lanuginosa lipase from combinatorial phage libraries

2004 ◽  
Vol 41 (10) ◽  
pp. 941-953 ◽  
Author(s):  
Charlotte G Jakobsen ◽  
Uffe Bodtger ◽  
Peter Kristensen ◽  
Lars K Poulsen ◽  
Erwin L Roggen
Keyword(s):  
Igg Antibodies ◽  
High Affinity ◽  
Bet V 1 ◽  
Humicola Lanuginosa ◽  
Phage Libraries ◽  
Humicola Lanuginosa Lipase

scholarly journals Demonstration of a natural antigalactosyl IgG antibody on thalassemic red blood cells

Blood ◽  
1983 ◽  
Vol 61 (6) ◽  
pp. 1258-1264 ◽  
Author(s):  
U Galili ◽  
A Korkesh ◽  
I Kahane ◽  
EA Rachmilewitz
Keyword(s):  
Sialic Acid ◽  
Myeloid Cell ◽  
Reticuloendothelial System ◽  
Igg Antibodies ◽  
Igg Antibody ◽  
High Affinity ◽  
Rbc Membrane ◽  
Antiglobulin Test ◽  
Normal Human ◽  
Galactosyl Residues

A modified antiglobulin test, based on the high affinity between the Fc portion of the red blood cell (RBC) bound IgG and the Fc receptor on the myeloid cell K-562, was utilized for demonstration of immunoglobulins (Ig) on thalassemic RBC. Ig was found on the RBC of 73 out of 80 patients with thalassemia. The immunoglobulins on the thalassemic RBC belonged to the IgG subclass and were autoreactive. Elution studies utilizing various carbohydrates, or by thermal stripping, indicated that at least part of the IgG molecules found on the thalassemic RBC were specifically reactive with terminal galactosyl residues on the RBC membrane. IgG antibodies with similar reactivity were also demonstrated in normal human serum. These natural antigalactosyl IgG antibodies from normal sera could bind to IgG- depleted thalassemic RBC. Thalassemic RBC and normal senescent RBC were previously found to contain reduced amounts of membrane sialic acid (SA). It is suggested that the antigalactosyl IgG antibodies interact with newly exposed galactosyl residues underlying the sialic acid units. Such interaction may lead to the shortened lifespan of thalassemic RBC and may result in sequestration of senescent normal RBC by the reticuloendothelial system.

scholarly journals Demonstration of a natural antigalactosyl IgG antibody on thalassemic red blood cells

Blood ◽  
1983 ◽  
Vol 61 (6) ◽  
pp. 1258-1264 ◽  
Author(s):  
U Galili ◽  
A Korkesh ◽  
I Kahane ◽  
EA Rachmilewitz
Keyword(s):  
Sialic Acid ◽  
Myeloid Cell ◽  
Reticuloendothelial System ◽  
Igg Antibodies ◽  
Igg Antibody ◽  
High Affinity ◽  
Rbc Membrane ◽  
Antiglobulin Test ◽  
Normal Human ◽  
Galactosyl Residues

Abstract A modified antiglobulin test, based on the high affinity between the Fc portion of the red blood cell (RBC) bound IgG and the Fc receptor on the myeloid cell K-562, was utilized for demonstration of immunoglobulins (Ig) on thalassemic RBC. Ig was found on the RBC of 73 out of 80 patients with thalassemia. The immunoglobulins on the thalassemic RBC belonged to the IgG subclass and were autoreactive. Elution studies utilizing various carbohydrates, or by thermal stripping, indicated that at least part of the IgG molecules found on the thalassemic RBC were specifically reactive with terminal galactosyl residues on the RBC membrane. IgG antibodies with similar reactivity were also demonstrated in normal human serum. These natural antigalactosyl IgG antibodies from normal sera could bind to IgG- depleted thalassemic RBC. Thalassemic RBC and normal senescent RBC were previously found to contain reduced amounts of membrane sialic acid (SA). It is suggested that the antigalactosyl IgG antibodies interact with newly exposed galactosyl residues underlying the sialic acid units. Such interaction may lead to the shortened lifespan of thalassemic RBC and may result in sequestration of senescent normal RBC by the reticuloendothelial system.

scholarly journals Potential Mechanisms of Age Related Severity of COVID-19 Infection: Implications for Development of Vaccines, Convalescent Serum, and Antibody Therapies

2020 ◽  
Author(s):  
Martin Zand ◽  
Jiong Wang
Keyword(s):  
Viral Entry ◽  
Vaccine Development ◽  
Surface Proteins ◽  
Igg Antibodies ◽  
Dengue Virus Infection ◽  
Younger Adults ◽  
High Affinity ◽  
Age Related ◽  
Coronavirus Infection ◽  
Viral Surface

There is an urgent need for vaccines to induce immunity to the 2019 coronavirus strain (COVID-19; CoV-SARS-2). Vaccine development may not be straightforward, in part due to the the phenomenon of antibody-dependent enhancement (ADE). The immune response to coronavirus infection or vaccination generates a mixture of IgG antibodies against viral surface proteins. Many of these antibodies block viral infection. However, in some cases IgG:virus complexes can facilitate viral entry and infection of cells by ADE, increasing the the risk and severity of infection. This phenomenon occurs in SARS, MERS, HIV, Zika and dengue virus infection and vaccination; it has been a serious barrier to vaccine development for these infections. Lack of high-affinity anti-COVID-19 IgG antibodies in children and younger adults may explain, in part, the decreased severity of infection in these groups. Here, we discuss the evidence for ADE in the context of COVID-19 infection, and how it may affect development of a vaccine and convalescent serum therapies. Here we discuss ADE in the context of COVID-19 infection, and how this may affect vaccine development, convalescent serum, and targeted monoclonal antibody therapies. We caution that this work is a hypothesis, and should be taken as such.

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