Genetic Control of the Immune Response to Myoglobin. V. Analysis of the Cross-Reactivity of 12 Myoglobins with Sperm-Whale Myoglobin Antisera of Inbred Mouse Strains in Terms of Substitutions in the Antigenic Sites and in the Environmental Residues of the Sites

Five inbred mouse strains which represent high and low responders to the random synthetic polypeptide poly(LTyr,LGlu)-polyDLAla--polyLLys, designated (T, G)-A--L, to which the immune response is controlled by an H-2-linked gene, were immunized with three ordered tetrapeptides composed of tyrosine and glutamic acid attached either to multichain poly-DL-alanine or to polyproline. Only one of the three antigenic determinants, namely tyrosyl-tyrosyl-glytamyl-glutamic acid (T-T-G-G), resembled the random peptide (T, G) in the pattern of immune responses elicited against it, and in the cross-reactivity of the specific antibodies with (T, G)-A--L. The immune response pattern to the other two ordered tetrapeptides, T-G-T-G and G-T-T-G, was different from that obtained with (T, G)-A--L, and no cross-reactivity was detected between the antibodies provoked with these peptides and (T, G)-A--L. Thus, it is suggested that T-T-G-G is a major determinant in the random (T, G)-A--L.

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Genetic control of the immune response to myoglobin. IV. Mouse antibodies in outbred and congenic strains against sperm-whale myoglobin recognize the same antigenic sites that are recognized by antibodies raised in other species

Molecular Immunology ◽

10.1016/0161-5890(81)90107-3 ◽

1981 ◽

Vol 18 (5) ◽

pp. 447-450 ◽

Cited By ~ 52

Author(s):

Sally S. Twining ◽

Chella S. David ◽

M.Zouhair Atassi

Keyword(s):

Immune Response ◽

Genetic Control ◽

Sperm Whale ◽

Congenic Strains ◽

Antigenic Sites ◽

Sperm Whale Myoglobin

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The antibody response to myoglobin is independent of the immunized species. Analysis in terms of replacements in the antigenic sites and in environmental residues of the cross-reactions of fifteen myoglobins with sperm-whale myoglobin antisera raised in different species

Biochemical Journal ◽

10.1042/bj1910681 ◽

1980 ◽

Vol 191 (3) ◽

pp. 681-697 ◽

Cited By ~ 53

Author(s):

S S Twining ◽

H Lehmann ◽

M Z Atassi

Keyword(s):

Amino Acid ◽

Antibody Response ◽

Three Dimensional ◽

Sperm Whale ◽

Cross Reactivity ◽

Antigenic Structure ◽

Amino Acid Substitutions ◽

Antigenic Sites ◽

The Cross ◽

Sperm Whale Myoglobin

The recent determination of the entire antigenic structure of sperm-whale myoglobin with rabbit and goat antisera has permitted the examination of whether the antigenic structure recognized by antibodies depends on the species in which the antisera are raised. Also, by knowledge of the antigenic structure, the molecular factors that determine and influence antigenicity can be better understood in terms of the effects of amino acid substitutions occurring in the antigenic sites and in the environmental residues of the sites. In the present work, the myoglobins from finback whale, killer whale, horse, chimpanzee, sheep, goat, bovine, echidna, viscacha, rabbit, dog, cape fox, mouse and chicken were examined for their ability to cross-react with antisera to sperm-whale myoglobin. By immunoadsorbent titration studies with radioiodinated antibodies, each of these myoglobins was able to bind antibodies to sperm-whale myoglobin raised in goat, rabbit, chicken, cat, pig and outbred mouse. It was found that the extent of cross-reaction of a given myoglobin was not dependent on the species in which the antisera were raised. This indicated that the antibody response to sperm-whale myoglobin (i.e. its antigenic structure) is independent of the species in which the antisera are raised and is not directed to regions of sequence differences between the injected myoglobin and the myoglobin of the immunized host. Indeed, in each antiserum from a given species examined, that antiserum reacted with the myoglobin of that species. The extent of this auto-reactivity for a given myoglobin was comparable with the general extent of cross-reactivity shown by that myoglobin with antisera raised in other species. The cross-reactivities and auto-reactivities (both of which are of similar extents for a given myoglobin) can be reasonably rationalized in terms of the effects of amino acid substitutions within the antigenic sites and within the residues close to these sites. These findings confirm that the antigenicity of the sites is inherent in their three-dimensional locations.

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CLONAL NATURE OF THE IMMUNE RESPONSE TO PHOSPHORYLCHOLINE

Journal of Experimental Medicine ◽

10.1084/jem.140.3.673 ◽

1974 ◽

Vol 140 (3) ◽

pp. 673-686 ◽

Cited By ~ 62

Author(s):

J. Latham Claflin ◽

Joseph M. Davie

Keyword(s):

Immune Response ◽

Binding Site ◽

Inbred Mouse ◽

Binding Specificity ◽

Rodent Species ◽

Mouse Strains ◽

Inbred Mouse Strains ◽

Myeloma Protein ◽

Clonal Nature ◽

Different Strains

A new idiotypic determinant(s) on mouse anti-PC antibodies is described. Antibodies to the determinant(s) were raised in rabbits by immunization with HOPC 8, a PC-binding myeloma protein, and were isolated from HOPC 8 immunoadsorbent by elution with PC. These antibodies react with binding site determinants on anti-PC antibodies raised in all 15 inbred mouse strains tested regardless of histocompatibility or allotype, but fail to react with antibodies of other specificities or with anti-PC antibodies raised in other rodent species. These results correlate closely with other studies which show similar binding specificity of anti-PC antibodies raised in 17 different strains of mice. The site-associated idiotypic determinant(s) is clearly distinct from that detected by mouse anti-HOPC 8 antisera. This latter determinant(s) is present on anti-PC antibodies of only a few strains of mice and may not be in the binding site.

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