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The Inducible Defense System: Antibody Molecules and Antigen-Antibody Reactions
Published in Julius P. Kreier, Infection, Resistance, and Immunity, 2022
Within a single isotype, i.e., IgGl, there may be some variation in the amino acid sequence of the C region among individuals in the population. These differences are inherited genetically and determine Ig allotypes (i.e., differences among individuals of the same species). The areas with different amino acids are called allotypic markers. The markers in humans which have been defined are Gm on gamma heavy chains, Am on alpha heavy chains, and Km (or InV) on the K light chains. Three Km (on IgD and IgE), two Am (on IgA), and over twenty Gm (on IgG) allotypes have been defined. Inheritance of these markers is autosomally controlled. In some cases the molecular structure of the allotype marker is known. For example, the KM(1,2) allotype, has leucine at position 191 in the CL domain of the kappa light chain, while Km(3) allotype has valine at this position. These allotypic markers are isoantigens. They are among the epitopes that are recognized by individuals who mount an antibody response to an immunoglobulin from another individual. These allotypic markers were used in paternity testing and in studies of population genetics prior to the development of DNA-based methods.
Inherited Defects in Immune Defenses Leading to Pulmonary Disease
Published in Stephen D. Litwin, Genetic Determinants of Pulmonary Disease, 2020
The interpretation of data on familial involvement is problematical. Analysis of pedigrees show a wide spectrum of findings ranging from selected families in which the number of first degree relatives with hypogammaglobulinemia or associated problems is striking [82-87], to many kindreds with no relatives having the same or related problems. Part of the difficulty in interpretation of the data is the heterogeneity of this disease which cannot yet be distinguished by biochemical or other criteria. At this point no monogenic mechanisms of gene transmission can be substantiated and the familial clustering observed could be as easily due to infectious agents or common environmental exposure as to inheritance. Several approaches have been made to the genetic problem. Litwin and Fudenberg quantitated the amounts of Gm allotype IgGl in families of VID patients. The data showed abnormalities in Ig allotype expression in selected families but did not prove that the defective Ig allotype structural gene was inherited [87]. Douglas has presented data on mitogen testing in VID families which implied inheritance of a defect [88]. Yount et al. have documented IgG subclass abnormalities in VID kindreds; IgG3 was discordant and tended to be relatively high in many cases [89].
“Biologically Active” RNA and the Immune Response*
Published in Edward P. Cohen, A. Arthur Gottlieb, Immune RNA, 2020
The most unequivocal approach toward an answer to the question of whether biologically active RNA codes for immunoglobulins is that taken by Adler et al.56 These investigators, more than any others, initiated a series of investigations bearing most directly on the question of whether the RNA itself has informational properties. In their studies they extracted RNA from the peritoneal cells of rabbits homozygous at one allotype locus (Ab4/Ab4) and exposed them to lymph node cells of rabbits homozygous at a second allotype locus (Ab5/Ab5). The antibodies appearing had the characteristics of the RNA donor. (Table 3). The converse was true, e.g., RNA from Ab5/Ab5 rabbits led to the formation of immunoglobulins in lymph node cells of Ab4/Ab4 rabbits which were of the Ab5 type. The immunoglobulins newly formed by the recipient’s cells were characteristic of the RNA donor and were of the IgM class. IgG antibodies were formed as well, expressing the allotype markers of the recipient animal. This probably indicates that antigen fragments or RNA-antigen complexes were present in the peritoneal cell extracts and stimulated antibody formation de novo.
Non-targeted characterization of attributes affecting antibody-FcγRIIIa V158 (CD16a) binding via online affinity chromatography-mass spectrometry
Published in mAbs, 2022
Daniel W. Woodall, Thomas M. Dillon, Kevin Kalenian, Rupa Padaki, Scott Kuhns, David J. Semin, Pavel V. Bondarenko
Fcγ receptors (FcγR) are membrane-bound glycoproteins belonging to the immunoglobulin (Ig) superfamily that are found on the surfaces of many of the hematopoietic cells of the immune system. These receptors are responsible for the binding of IgG immune complexes and play an important role in modulating both adaptive and innate immune responses. Binding of FcγRs to IgG molecules plays an important role in activation and regulation of immune cells.1,1–3 FcγRIIIa (CD16a) is a low affinity Fc receptor associated with the antibody-dependent cell-mediated cytotoxicity (ADCC) pathway. The FcγRIIIa-V158 allotype used in this study has a higher affinity for both monomeric and immune-complexed IgG1, IgG3, and IgG4 than IIIa-158 F.4,5,6, ADCC results when antibodies recognize and bind to a cell-based target antigen and then recruit natural killer (NK) cells to actively lyse the antigen-expressing target cells. The ADCC response is often associated with NK cells, which express FcγRIIIa receptors on their cell surfaces. FcγRIIIa binds to the crystallizable fragment (Fc) region of an antibody and brings the effector (NK) cell into proximity of the antigen-expressing cell so that it may form a lytic synapse between the NK cell and the antigen-expressing cell.1,2,3,7
Pharmacological strategies for improving the prognosis of glioblastoma
Published in Expert Opinion on Pharmacotherapy, 2021
Divyaansh Raj, Pranjal Agrawal, Hallie Gaitsch, Elizabeth Wicks, Betty Tyler
Another antigen of interest is the tumor-specific human leukocyte antigen (HLA) peptidome. Proteome analysis for the HLA peptidome specific to GBM revealed 52 allotypes. The HLA peptidome was able to identify SOX11 as an antigen with two peptide sequences, AHSASEQQL and NFSDLVFTY, that were observed uniquely in the plasma (sHLA) and tumor membrane (mHLA) of the GBM when compared to healthy controls [45]. Developing active or adaptive immunotherapy against these specific HLA peptides could serve as a synergistic active and adaptive immunotherapeutic target. These allotypes are specific to each patient, however, and therefore unique antibodies would need to be developed for each tumor allotype- a process which has proven to be very expensive [45,46]. More research needs to be done in diverse cohorts to identify common HLA allotypes that could be developed into a more ubiquitous treatment for patients with GBM.
Autism spectrum disorders and natural killer cells: a review on pathogenesis and treatment
Published in Expert Review of Clinical Immunology, 2021
Sepideh Ebrahimi Meimand, Yasna Rostam-Abadi, Nima Rezaei
The HLA C1 allotype has interaction with KIR 2DS1 and activates NK cells. The KIR 2DS1 was remarkably higher in mothers of children with ASD. The HLA C2 allotype frequency was considerably higher in fathers of children with ASD but there was no difference seen in HLA C1 allotype. Interestingly, higher frequencies of the combination HLA-C2 + KIR2DS1 were not seen in their children with ASD. The activating KIR 3DS1/HLA BW4 complex frequency was higher in the maternal group [62]. HLA-C2 allele has been higher in children with ASD’s fathers. The allele interacts with KIR 2DS1 which was interestingly higher in children with ASD’s mothers. Overall, mothers have higher measures of activating signals comparing to fathers. The frequencies of most HLA and KIR alleles in children with ASD have been ranged between their parents’ frequencies. Surprisingly, each receptor gene and its corresponding ligand may be transferred together to the children. It is noteworthy that these gene families are located on different autosomal chromosomes, presumably having homozygous status [63].