Genetic Characterization of a new allele of the rabbit group b Ck allotypes

Sogn, John A.; Kindt, Thomas J.

doi:10.1007/bf01843999

Cited by 18 publications

(8 citation statements)

References 27 publications

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“…Elution was obtained with a gradient 0% B to 60% B in 1 h. The flow rate is 1 mL/min. light chain, obtained after allotypic suppression of a b4/b5 rabbit (Chersi et al, 1980), suggests that variations may exist among the constant regions of b5 chains, as has been previously shown for b4 (Strosberg et al, 1974;Sogn & Kindt, 1978) and for b6 (Emorine et al, 1979). Among the six differences between the b5 constant region described by Chersi and that of light chain 2699, two (leucine for valine at position 195 and proline for alanine at position 196) could be technical, since they were deduced from amino acid compositions in Chersi et al report.…”

Section: Discussionmentioning

confidence: 67%

“…The b4 Var differs from b4 by two residues (serine for alanine at position 121 and leucine for glutamine at position 124). Genetic data show that b4 is an allele of b4 Var (Sogn & Kindt, 1978). Several different residues have also been observed in the b4 light chain sequence at position 172 (Am, Leu, and Val) (Appella et al, 1973;Chen et al, 1975;Van Hoegaerden & Strosberg, 1978).…”

Section: T-smentioning

confidence: 99%

“…A small number of substitutions appear to distinguish constant regions of the same allotype (Sogn & Kindt, 1976;Strosberg et al, 1974;Emorine et al, 1979) (N,N-dimethy1amino)azobenzene 4'4sothiocyanate. Each step of the degradation of radioactive peptides was counted in an Intertechnique liquid scintillation counter.…”

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confidence: 99%

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Partial amino acid sequence of a rabbit immunoglobulin light chain of allotype b5

Ayadi¹,

Dutka²,

Paroutaud³

et al. 1983

Biochemistry

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The amino acid sequence of a rabbit immunoglobulin light chain of allotype b5 has been nearly completed. A comparison of its structure with that of light chains of allotypes b4, b6, and b9 confirms that the constant regions of these various kappa chains differ by 20-35%. The substitutions are clustered in parts of the second half of the chain, and the b5 form bears more resemblance to the b6 chain than to any other, in good agreement with previous serological data. The analysis of the variable region reveals the existence of certain allotype-associated residues which have also been reported in other b5 chains, but not in proteins of the other allotypes. An examination of the rabbit light chain sequences between positions 96 and 107 suggests that this portion of the chain may be encoded separately by a joining "J" DNA segment, as has been described previously for murine and human immunoglobulins. In the rabbit, however, these J kappa regions appear to differ from one allotype to another. Together with the extensive variations of the constant regions, these data suggest that the rabbit kappa gene organization more closely resembles the murine gamma system (four different C gamma genes each flanked by its J segment) than the murine kappa system (a single C kappa gene).

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Section: Discussionmentioning

confidence: 67%

Section: T-smentioning

confidence: 99%

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Partial amino acid sequence of a rabbit immunoglobulin light chain of allotype b5

Ayadi¹,

Dutka²,

Paroutaud³

et al. 1983

Biochemistry

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“…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)(2)(3)(4)(5)(6). Extensive chemical differences in the constant (C) regions of b4, b5, b6, and b9 molecules have been reported (7)(8)(9) and are thought to reflect the expression of the antigenic determinants of the b allotypes (10).…”

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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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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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“…This led us to the view that the structural genes of the light chain might determine the probability of effective contact between Ig receptor and antigen (Szymanska et al, 1981) In rabbits heterozygous at the kappa light chain allotypic locus (Ab) the two allelic genes are not equally expressed. A preponderance of Ab4 over all other Ab alleles has been documented and is known as the 'pecking order' (Chou et al, 1967(Chou et al, , 1972(Chou et al, , 1974Sogn & Kindt, 1978). It is likely that this pecking order results from different probabilities of antigen capture by different allotypically marked receptors.…”

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confidence: 99%

Allotype and Charge‐related Differences in the Immune Response

Notenboom

Dubiski

and

et al. 1982

Int J Immunogenetics

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SUMMARY Rabbits homozygous at the Ab kappa chain allotypic locus (Ab4/Ab4 and Ab9/Ab9) were immunized with negatively and positively charged antigens. The negatively charged antigens were bovine serum albumin (BSA; pI = 4.9), ovalbumin (OV; pI = 4.9) and two synthetic polypeptides: copolymer L‐glutamic acid L‐tyrosine (abbreviated TG; pI = 4.8) and multichain poly (L‐tyrosine: L‐glutamic acid) poly D‐alanine: poly L‐lysine (poly L‐lysine backbone) (abbreviated (TG) ‐ AL; pI = 4.8). The positively charged antigen was hen egg lysozyme (LYS; pI = 10.2). Homozygous Ab9 rabbits responding to negatively charged antigens made less antibody than did Ab4 homozygotes. In contrast, both groups of animals responded equally well to positively charged lysozyme. The relative electric charges of the antibodies were assessed by Sephadex A‐50 chromatography. The charge distribution was found to depend on the charge of the eliciting antigen. The positively charged antibodies of Ab9/Ab9 rabbits were not nearly as positively charged as those raised in Ab4/Ab4 rabbits. The difference in average electric charges and in the range of these charges between Ig Ab4 and Ig Ab9 explain quantitative differences in antibody formation in response to negatively charged antigens and may be a contributing factor to the ‘pecking order’, i.e. unequal phenotypic expression of ligh chain genes in Ab4/Ab9 heterozygotes.

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Genetic Characterization of a new allele of the rabbit group b Ck allotypes

Cited by 18 publications

References 27 publications

Partial amino acid sequence of a rabbit immunoglobulin light chain of allotype b5

Partial amino acid sequence of a rabbit immunoglobulin light chain of allotype b5

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

Allotype and Charge‐related Differences in the Immune Response

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