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PubMed1981

Tolerance to allotypic determinants induced by lymphoid cells from congenic mice bearing the allotype.

Mice of one allotype (Igb) were immunized against immunoglobulin from a congenic strain of mice bearing another allotype (Iga). This Igb anti-Iga response was profoundly suppressed by injecting lymphoid cells from congenic Iga mice but not by serum Iga. Suppression was specific, could be induced by congenic B cells but not histoincompatible lymphoid cells and depended both on the time of administration of cells relative to immunogenic challenge and to the number of cells injected. Unresponsiveness was more easily induced in neonates than adults. It is considered that tolerance to the allotype depends on the properties of the cells to which they are bound.

Animals↗
PubMed1977

Human IgG3 allotypes, with special reference to a new allotype related to G3m(g) (G3m21).

The IgG3 allotype described as L1 (Blanc et al., 1976) occurs on the CH3 region of G3m(g) proteins, in contrast to G3m(g) that is known to be present on the CH2 region. G3m(g) and L1 are, as a rule, present on the same gamma3 heavy chain, just like the G3m(b) subspecificities of the CH2 region, (b1) and (b4), with those of the CH3 region (b0), (b3) and (b5). Several families were investigated that showed inheritance of rare combinations of IgG3 allotypes. The data obtained are suggestive for notation of L1 as (g5), since L1 probably occupies a position antithetical to (b5). The relation of amino acid substitutions to allotypes and isoallotypes is discussed.

Alleles↗
PubMed1989

An indirect asymmetrical sandwich ELISA using anti-allotype antibodies for the specific and quantitative measurement of mouse IgG2a of Igh-1b allotype.

We recently described an indirect double sandwich ELISA (Klein-Schneegans et al., J. Immunol. Methods (1989) 119, 117) which permits the specific and quantitative measurement of mouse IgM, IgA and IgG subclasses with one major exception: IgG2a of the b allotype (Igh-1b in mouse strains such as C57BL/6) could not be reliably quantitated even by a very specific and sensitive asymmetrical sandwich ELISA (using two different anti-IgG2a isotype antibodies for capture and for detection). We now describe a similar method based on the use of two different anti-IgG2a allotype antibodies for the capture and detection of IgG2a in the serum of Igh-1b mouse strains.

Animals↗
PubMed1980

Quantitative studies of Gm allotypes. V. Simultaneous presence of latent Gm allotypes and deficient Gm genes in a family with hypogammaglobulinaemic probands.

A study of Gm allotypes in a Caucasoid family with hypogammaglobulinaemic probands, showed qualitative (unexpected or lacking Gm allotypes) and quantitative (increased or decreased Gm contents) abnormalities in many relatives. Part of these observations can be most probably accounted for by inheritance of a GM1,17; 5,28 haplotype, not described in Caucasians yet, and by an in vivo expression of latent Gm genes.

Adolescent↗
PubMed1978

In vitro studies on allotype suppression. IV. Abrogation of waning suppression by normal immunoglobulin of the suppressed allotype.

The mechanism of allotype suppression in rabbits has been investigated by studying the in vitro immune responses of spleen cells from rabbits in advanced stages of spontaneous recovery from suppression. Whereas the spleen cells from highly suppressed rabbits can be released from their suppressed state only if treated with a combination of antibodies against the non-suppressed type and immunoglobulin (Ig) of the suppressed type, treatment with either of these two components alone suffices to overcome suppression when cells of more poorly suppressed spleen donors are used. The demonstration that suppression can be abrogated by normal Ig of the suppressed type alone, when cells are obtained from rabbits in the final phases of suppression, lends further support to the previously suggested concept that the probable role of this normal Ig in the release phenomenon may be that of neutralizing an effector of allotype-specific repression, possibly involving suppressor cells.

Animals↗
PubMed1985

[Production of allotype by bone marrow cells transferred to rabbits subjected to suppressor treatment by allotype].

Inbred rabbits of B/J strain were immunized against Salmonella typhi and their bone marrow cells plus LPS were injected into (Chbb: HM X B/J) F1 hybrids at the age of 3-7 weeks, which had received at birth a treatment of the allotype suppression. Antityphoid antibodies bearing the suppressed allotype were found in the serum of the recipients, which showed no signs of the graft versus host reaction.

Animals↗
PubMed1984

[Possible existence of autoantibodies against immunoglobulin allotypes in normal rabbits, and their relation to the expression of these allotypes].

The concentration of a3 allotype was increased in the serum of heterozygous a1 a3 rabbits which received antiidiotypic antibodies against anti-a3 antibodies in the perinatal period. This is explained by the normal presence of anti-a3 autoantibodies which control the expression of a3 allotype in heterozygous a1 a3 rabbits under physiological conditions.

Animals↗
PubMed1973

An idiotypic cross-reaction between allotype a3 and allotype a negative rabbit antibodies to streptococcal carbohydrate.

Two antibodies to Group C streptococcal carbohydrate isolated from an individual rabbit had similar relative binding affinities for a Group C immuno-adsorbent column. Their light chains were similar, if not identical, as were the constant regions of their heavy chains. Differences in the variable regions of the H chains of the two antibodies were detected by chemical analysis. The two antibodies had serologically identical idiotypic determinants although one antibody possessed the a3 allotype and the other had no detectable group a marker. The occurrence of such antibodies indicates the absence of obligatory associations between group a allotypes and idiotypic specificities, despite the fact that both determinants have antigenic components in the V(H) region of the H chain.

Animals↗
PubMed1976

Studies on the structural localization of rabbit H chain allotypic determinants controlled by the a locus. Purification and immunological properties of an immunopeptide bearing a3 allotypic determinants.

An immunopeptide bearing a3 allotypic determinant(s) was isolated from the gamma chain of an a3 homozygous rabbit (G222-2) immunized with type III pneumococcal vaccine. Immunocogical properties of peptides were studied using a radioimmunoassay that involved inhibition by these peptides of a reaction between 125I-labeled anti-a3 antibody and Sepharose-bound a3 immunoglobulin G (IgG). The gamma chain was isolated from IgG of restricted heterogeneity and then citraconylated and digested with trypsin. The tryptic digest (TD1) was passed through an anti-a3 immunoabsorbent column either directly or after an intermediate step of Sephadex G-75 chromatography. The bound peptides (T1) were eluted with 0.1 M acetic acid and further digested with trypsin. The digest (TD2) was again run on the anti-a3 immunoabsorbent column to purify the bound immunopeptide T2. In the radioimmunossay this immunopeptide was found to have major a3 determinant(s). Its molecular weight was found to be approximately 6,000, which decreased to about 3,000 after reduction and alkylation. These data, together with NH2- and COOH-terminal analyses and cysteine peptide mapping, demonstrated that T2 is composed of two polypeptide chains linked by a disulfide bond, one from the cysteine 22 region having lysine at the COOH terminus and the other from the cysteine 92 region arginine at the COOH terminus. The lysine peptide was separated from the arginine peptide and its NH2-terminal sequence was found to be Gly-Asx-Glx-Ser-Thr-Cys. Since the cysteine is at position 22, the lysine peptide starts at position 17. It has approximately 22 residues. The framework sequence from 17 to 20 is different from those reported so far. In addition, the heavy chain used in these studies has some other unusual features including a histidine, probably in the first hypervariable region. The presence of histidine in the first hypervariable region of rabbit heavy chain has not been reported previously. The other peptide which is about 30 amino acids in length and ends with arginine 94, probably includes positions 67, 70, 71, 84, and 85 that are believed to have substitutions correlating with a allotypes. In a hypothetical three-deminsional model of the Fv portion of rabbit anti-SIII antibody BS-5, residues 17 to 33 of the lysine peptide and 67 to 79 and 84 to 85 which may be present in the arginine peptide are fully exposed on the surface and are far removed from the antibody combining site.

Amino Acids↗
PubMed1982

Expression of kappa chain allotypes at the cell surface and in serum immunoglobulins of normal and allotype-suppressed heterozygous rabbits.

The kappa light chain allotypes b4 and b5 were measured in the serum and on the surfaces of peripheral blood lymphocytes of normal and allotype-suppressed heterozygous rabbits. Surface immunoglobulins (sIg) were detected by fluorescence microscopy and additional quantitative data were obtained by flow microfluorometry. Although a few b5-suppressed animals had no b5 in serum or on cell surfaces for years, most b5-suppressed and all b4-suppressed animals studied had some cells with sIg of the suppressed type by 1 year of age. In suppressed animals the level of serum Ig remained depressed throughout life but cells with sIg appeared in disproportionately large numbers. The effect was particularly striking in those animals suppressed for the b4 type.

Age Factors↗
PubMed1991

Assay restriction profiles of three monoclonal antibodies recognizing the G3m(u) allotype. Development of an allotype specific assay.

Three monoclonal antibodies raised against a purified human IgG3 paraprotein were found to exhibit a restriction profile for IgG3/G3m(u) and pan-IgG specificity which was dependent on the assay system. When adapted to an IgG3 subclass capture ELISA, all three McAbs discriminated between paraproteins expressing G3m(u) and antithetical markers G3m(st). One of the antibodies (PNF69C) was selected and conditions were optimised for Gm typing purposes. Using this system G3m(u) could be detected on captured IgG3 derived from human sera. This system may prove useful in the elucidation of Gm allotype profiles.

Animals↗
PubMed1987

The idiotypy of auto anti-allotype antibody induced in immunoglobulin allotype suppressed rabbits.

Rabbit anti-rabbit idiotype antibody was raised to both clonally heterogeneous and restricted auto anti-b6 antibodies induced in b6 allotype-suppressed (b6)/(b6) homozygous and b4/(b6) heterozygous rabbits. In every case the anti-idiotypic antibodies were specific only for the inducing antibody as shown by direct binding solid-phase RIA. Anti-idiotypes directed to the same antibody preparation had a similar but not identical specificity. It was demonstrated by IEF that the same idiotype specificity (spectrotype) was present throughout the anti-b6 response in individual rabbits.

Animals↗
PubMed1981

Immunoglobulin allotypes in European populations. IV. Gm, Am and Km allotypic markers in Valencia, Spain.

The distribution of Glm(f, z, a and x), G3m(b0, b1, b3, b5, c3, c5, g, s and t), A2m (1 and 2) and Km(1) allotypic determinants in a series of Spanish blood donors. The following results were obtained: Gmz,a;gAm1 = 0.199; Gmz,a;gAm2 = 0.019; Gmz,a,x;gAm1 = 0.081; Gmz,a,x;gAm2 = 0.005; Gmf;bAm1 = 0.677; Gmz,a;bAm1 = 0.019 and Km1 = 0.096. The results are similar to those reported for adjacent Basque and Portuguese populations. The origin of the Gmz,a;bAm1 haplotype is unknown.

Blood Donors↗
PubMed1975

Immunoglobulin Allotypes of European Populations. I. Gm and Km(Inv) allotypic markers in Hungarians.

The distribution of G1m(f, z, a, and x), G3m(b0, b1, b3, c3, c5, g, s, and t) and Km(1) (formerly Inv[1]) allotypic markers have been examined in 184 Hungarians. The results indicate that the frequency of the immunoglobulin haplotypes Gmza;g, Gmzax;g, Gmf;b and Km1 is similar to the frequencies observed in surrounding populations. In addition, Hungarians were found to be polymorphic for the Oriental haplotype Gmza;bst, and had low frequencies of other uncommon haplotypes. Our data indicate that about 5% of the Hungarian genome is of Oriental origin.

Gene Frequency↗
PubMed1975

Immunoglobulin allotypes of European populations. II.Gm, Am and Km(Inv) allotypic markers in Czechoslovakians.

The distribution of G1m(f,z,a, and x), G2m(n), G3m(b0, b1, b3, b5, c3, c5, g, s, t, and v), A2m(1 and 2) and Km(1) (formerly Inv[1]) allotypic determinants has been examined in a series of Czechoslovakian blood donors. The results indicate that Gmza;-;gvA2m1, Gmzax;-;gvA2m1, Gmf;n;bvA2m1 and Gmf;-;bvA2m1 are present in polymorphic frequencies. Further, 9 idiomorphic phenotypes were observed; however, without family data it was not possible to exactly define the majority of these. The observed frequencies of Gmza;g, Gmzax;g and Gmf;b and Km1 are similar to those observed previously in Czechoslovakians and similar to those observed in adjacent populations, though different from those observed in Western Europeans, primarily due to a higher frequency of Gmf;b in Czechoslovakians.

Czechoslovakia↗
PubMed1980

IgD allotypic determinants. I. Determinants expressed on murine IgD of the a allotype.

Allotypes of membrane IgD of 27 strains of mice were determined with a series of anti-delta reagents, each capable of binding to the IgD of BALB/c spleen cells. One of these reagents is a newly defined allospecific rabbit anti-mouse-delta a. Typing with these reagents reveals the strain distribution of the previously described IgD.36 (Ig5.1) and IgD.43 (Ig5.4) specificities and demonstrates the existence of a new specificity, IgD.45 (Ig5.5). The results confirm the previous subdivision of the Igh-Ce haplotype into Igh-Ce, to which A mice are assigned, and Igh-Cn, to which NZB and NZW mice are assigned. In addition, it is shown that the Igh-Cd haplotype must also be subdivided. AKR mice, which express the a allele at the Igh-5(delta) locus, are designated as possessing the Igh-Cd haplotype while AL/N and C.AL20 mice, which have the e allele at the Igh-5(delta) locus, are assigned a new Igh-C haplotype designation, o.

Absorption↗
PubMed1980

Concentration of IgG1 and IgG2a allotypes in serum of nude and normal allotype-congenic mice.

BALB/c (C) and C57BL/6 (B6) allotype--congenic strains of mice (C, C.B, B6, B6.C) were made congenitally anthymic by the introduction of the mutant nude gene (nu). The resulting nude mice (C.nu, C.B.nu, B6.nu and B6.C.nu) were found to produce highly variable quantities of IgG1 and IgG2a. Whether these mice showed high, normal, or low quantities of IgG1 or IgG2a relative to their normal counterparts depended on their age and genetic background. In all nude mice, IgG1 production appeared more sensitive to the loss of T cells than did IgG2a production. An extreme example of this was the deficiency of IgG1 but not IgG2a in adult B6.nu and B6.C.nu mice. Substantial quantities of both IgG1 and IgG2a were found in adult C.nu and C.B.nu mice.

Aging↗
PubMed1994

T cell-induced Ig allotypic suppression in mice. Basis for emergence or tolerization, during the perinatal period, of natural T cells specific to the IgG2ab allotype.

We have previously described an anti-IgG2ab T cell activity in normal Igha/a mice. Their congenic partner at the Igh locus (Ighb/b) and Igha/b hybrids bred from them, do not display this T cell activity but express IgG2ab. As these mice are supposed to possess the same genetic elements related to this potential T cell repertoire, only somatic selection mechanisms could be responsible for their different behavior. In this study, we investigated the basis for the emergence (in Igha/a mice) or tolerization (in Ighb/b-congenic mice and in Igha/b hybrids) of these natural anti-IgG2ab T cells. Stringent perinatal B cell deprivation in Ighb/b and Igha/b mice resulted in the emergence of anti-IgG2ab T cells, as these individuals could be subjected to autoimmune, T cell-mediated IgG2ab suppression. Furthermore, the acquisition of anti-IgG2ab T cell activity was drastically reduced in Igha/a mice, perinatally exposed to IgG2ab; thus, the presence of this allotype leads to tolerization of these specific T cells.

Animals↗