Antibody response to the streptococcal group A-variant polysaccharide in BASILEA rabbits lacking kappa-polypeptide chains.

Weiß, Siegfried; Kelus, A. S.; Braun, Dietmar

doi:10.1084/jem.146.5.1195

Cited by 14 publications

(2 citation statements)

References 23 publications

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“…A bas, 4548 (13,14). This K-like component differs in the beginning of the C region amino acid sequence from the known sequences ofb4, bS, b6, and b9 K chains (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…However, this situation is reversed in a variant rabbit strain designated BASILEA, which was developed and maintained by Kelus and Weiss (12). Homozygous BASILEA rabbits are characterized by the lack ofK chains bearing b4, b5, b6, or b9 allotypic markers, which are substituted by L chains of the A type bearing C7 and C21 allotypic specificities (12)(13)(14). The primary structure of the constant region ofA L chains derived from an antibody IgG raised in BASILEA rabbits was recently completed and showed extensive homology with A chains of other species (14,15 (16).…”

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confidence: 99%

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BASILEA rabbits express two types of immunoglobulin light chains: lambda and kappa-like.

García¹,

Brandt²,

Benammar³

et al. 1982

Proc. Natl. Acad. Sci. U.S.A.

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In the variant rabbit strain BASILEA, immunoglobulins G were shown to contain two distinct populations of IgG molecules whose light (L) chains belonged to the known A isotype and to a new K-like type. These two L chains differed from each other by electrophoretic, chemical, and antigenic properties. The K-like L chain fraction showed (i) an acid-labile Asp-Pro bond at the end of the joining region and (ii) a tryptic peptide, whose amino acid sequence ofthe NH2-terminal 15 residues was identical to the homologous constant (C) region sequence of b9 K chain with the exception of the residue in position 70, which is asparagine in the K-like chain instead of the characteristic half-cystine residue in all L chains of KB type expressing b4, b5, b6, or b9 allotypes. Serological and chemical studies have demonstrated to date the existence of five polymorphic forms of the domestic rabbit K light (L) chain allotypes designated b4, b5, b6, b9, and b4var (1-6). Extensive chemical differences in the constant (C) regions of b4, b5, b6, and b9 molecules have been reported (7-9) and are thought to reflect the expression of the antigenic determinants of the b allotypes (10). In standard domestic rabbits, A-type L chains are the minor component of the immunoglobulin L chain pool (11). However, this situation is reversed in a variant rabbit strain designated BASILEA, which was developed and maintained by Kelus and Weiss (12). Homozygous BASILEA rabbits are characterized by the lack ofK chains bearing b4, b5, b6, or b9 allotypic markers, which are substituted by L chains of the A type bearing C7 and C21 allotypic specificities (12-14). The primary structure of the constant region ofA L chains derived from an antibody IgG raised in BASILEA rabbits was recently completed and showed extensive homology with A chains of other species (14,15

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“…A bas, 4548 (13,14). This K-like component differs in the beginning of the C region amino acid sequence from the known sequences ofb4, bS, b6, and b9 K chains (Fig.…”

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

BASILEA rabbits express two types of immunoglobulin light chains: lambda and kappa-like.

García¹,

Brandt²,

Benammar³

et al. 1982

Proc. Natl. Acad. Sci. U.S.A.

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Clonal dominance of low‐affinity antibodies in rabbit hyperimmune anti‐streptococcal group A‐variant polysaccharide antisera

et al. 1979

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Intraveneous hyperimmunization of selectively bred rabbits with streptococcal group A-variant vaccines elicits antibody responses of restricted heterogeneity at high antibody levels. In these antisera, IgG with dissociation constants Kd = 10(-6) M constitutes 90% and IgG with Kp = 10(-9) M accounts for only 10% of the group A-variant polysaccharide-specific antibodies. The low affinity antibody fraction represents the dominant clonotypes. Preparative isoelectric focusing in granulated (Ultrodex G-75) gels was used to successfully purify single-band material belonging to dominant spectrotypes. Affinity studies with these antibody fractions with the highest reported degree of purity yielded Kd = 10(-6) M values, thus confirming that clonal dominance is exclusively associated with low-affinity antibodies. Since it is known from previous work (M. Cramer and D. G. Braun, Scand. J. Immunol. 1975. 4:63) and from the rabbit antisera used here that clonal dominance of this sort is long-lived, this work fails to support the argument of immune maturation. The data more logically relate to antibodies that emerge with different subspecificities -- recognized in the antigen as a function of time in immunization procedures -- rather than to an inherent property of the immune system.

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Rabbit allotype a locus subspecificities of homogeneous anti‐streptococcal antibodies

Rodkey¹,

Braun

1979

Eur J Immunol

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Rabbits were immunized with group A-variant (Av) streptococcal vaccine to elicit antisera containing antibodies of "restricted heterogeneity" specific for Av polysaccharide. Antibodies that migrated as single bands in polyacrylamide gel isoelectric focusing were isolated on agarose block electrophoresis and preparative isoelectric focusing. These homogeneous antibodies were analyzed for content of the a locus markers by inhibition of allotype-anti-allotype radioimmunoassays. Both single-band preparations and preparations containing 2--5 bands were deficient in content of the a locus markers. These analyses were strongly influenced by the different anti-allotype antisera used. Single-band preparations, deficient in a 2 or a 3 markers, were further used to produce anti-allotype antisera, and these sera were assayed for reaction with pooled a2 or a3 molecules. The results, in contrast to the a1 allotype, failed to demonstrate common determinants on either a 2 or a 3 molecules indicating that each a allotype consists of a set of different Ig molecules. The data suggest different evolutionary pathways of the a 1, as opposed to the a 2 and a 3 molecules.

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Antibody response to the streptococcal group A-variant polysaccharide in BASILEA rabbits lacking kappa-polypeptide chains.

Cited by 14 publications

References 23 publications

BASILEA rabbits express two types of immunoglobulin light chains: lambda and kappa-like.

BASILEA rabbits express two types of immunoglobulin light chains: lambda and kappa-like.

Clonal dominance of low‐affinity antibodies in rabbit hyperimmune anti‐streptococcal group A‐variant polysaccharide antisera

Rabbit allotype a locus subspecificities of homogeneous anti‐streptococcal antibodies

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