Immunoglobulins allotypes, rabbit

Kindt, T.J., Mandy, W.J., Todd, C.W. (1970). Association of allotypic specificities of group a with allotypic specificities All and A12 in rabbit immunoglobulin. Biochemistry 9, 2028-2032. 

Knight, K.L. Becker, R.S. (1990). Molecular basis of the allelic inheritance of rabbit immunoglobulin VH allotypes implications for the generation of antibody diversity. Cell 60,963-970. 

Antigenic markers (allotypes) of immunoglobulin molecules were almost simultaneously reported for human and rabbit antibodies. Oudin (1956) observed that rabbit antibodies themselves elicited precipitating antibodies when they were injected into certain other rabbits. Oudin named the phenomenon allotypy and the antigenic determinants on the immunoglobulin molecules were called allotypes. At the same... 

J. Michael Kehoe and Rochelle Seide-Kehoe Table IV. Allotypic Specificities of Rabbit Immunoglobulins" ... 

As indicated in Table IV, allotype-specific antigenic determinants on rabbit secretory piece have been described by Knight et al. (1974). These markers have been shown to be unlinked to those associated with the other polypeptide chains found in rabbit immunoglobulins that were discussed previously. 

Allotype-related sequences in rabbit immunoglobulins are discussed in Chapter 9. 

A. Detection and Quantitation of Allotypic Determinants in Rabbit Immunoglobulins... 

We will not attempt to describe research on allotypes in its historical context but, rather, will summarize present information. Table 9.1 lists the allotypic markers of rabbit immunoglobulins and their associa-... 

Figure 2.2 Genetic loci involved in the synthesis of rabbit immunoglobulins as determined by allotype inheritance. It is not known if Vh genes of group a, x and y exist in single or multiple copies. Observations of Vl region subgroups suggest existence of multiple Vl genes.

Separation of rabbit allotypic b4 immunoglobulin 224 k) IgG from b4-negative immunoglobulin (A)... 

Early evidence pointing to a restriction in immunoglobulin expression was the demonstration that, in individuals who are heterozygous for allotype, myeloma proteins carry one or the other, but never both, of the allelic determinants found in the pooled immunoglobulin of that person (M rtensson, 1961 Harboe et al., 1962). This finding was interpreted to indicate that the alternate allotypic determinants are present on different immunoglobulin molecules, which are produced by different cells. Oudin (1960) had observed a presumably related phenomenon in rabbits. 

In 1963, shortly after the four-chain model for immunoglobulins was proposed, Dray and Nisonoff showed that immunoglobulin molecules from rabbits heterozygous for allotypic determinants at a light chain locus contain either light chains of one allotype, or of the other, but not both. These authors did not interpret the results... 

Dubiski, S. (1969). Immunochemistry and genetics of a new allotypic specificity A 4 of rabbit yG immunoglobulins recombination in somatic cells. J. Immunol. 103,120-128. 

Knight, K.L., Malek, T.R., Hanly, W.C. (1974). Recombinant rabbit secretory immunoglobulin molecules alpha chains with maternal (paternal) variable-region allotypes and paternal (maternal) constant-region allotypes. Proc. Natl. Acad. Sci. USA 71, 1169-1173. 

Pemis, B., Chiappino, G., Kelus, A.S., Gell, P.G.H. (1965). Cellular localization of immunoglobulins with different allotypic specificities in rabbit lymphoid tissues. J. Exp. Med. 122,853-876. 

The differences in the titer of antiallotype antibody produced reflect the particular antigenic determinants involved. The allotypic determinants of human immunoglobulins are small, often single amino acid interchanges in proteins of the same subclass. Amino acids involved in the determinant may be considerably removed from one another in the linear sequence in those instances when more than one amino acid is important, however. Examples are the group a and b allotypic determinants of rabbits which involve multiple amino acid differences scattered along the chain (Kindt, 1975). 

In this chapter we will discuss amino acid sequences of human and mouse L chains and of human and rabbit H chains. A few sequences of rabbit L chains are also tabulated. Other partial amino acid sequences are presented in connection with the phylogeny of immunoglobulins (Chapter 7), and allotype-related sequences are discussed in Chapter 9. The amino acid sequences to be discussed here represent only a small fraction of the existing literature but should serve to illustrate principles of immunoglobulin structure. 

In this chapter we shall describe properties of immunoglobulins of four mammalian species that have been studied quite extensively the rabbit, mouse, guinea pig, and horse. Human inununoglobulins are considered in Chapter 3 and the pattern of evolution of immunoglobulins in vertebrates in Chapter 7. Allotypy of immunoglobulins is reviewed in Chapter 9 and will not be considered here. Because of the extensive body of information available on amino acid sequences and allotypes a more complete understanding of the structure of the immunoglobulins of these species will require reference to Chapters 4 and 9. 

---