Localization and verification by synthesis of five antigenic sites of bovine serum albumin

Atassi, M. Zouhair; Sakata, Shigeki; Kazim, A. Latif

doi:10.1042/bj1790327

Cited by 52 publications

(15 citation statements)

References 18 publications

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“…This is consistent with the observation that peptides, even though active, will have predominantly random conformations and C> thus diminished affinities for their antibodies (Atassi & Saplin, 1968). Further, a considerable proportion of a peptide on the immunoadsorbent is expected to a~have been rendered inactive owing to attach-0 ment of the peptide via side chains essential for binding with antibody, and to steric inaccessibility (Twining & Atassi, 1979;Atassi et al, 1979). The binding of antibodies by these peptide-adsorbents, however, was completely inhibited by the addition of free uncoupled Hb to the reaction (results not shown).…”

Section: Synthesis Purification and Characterization Of The Peptidessupporting

confidence: 81%

Structurally inherent antigenic sites. Localization of the antigenic sites of the α-chain of human haemoglobin in three host species by a comprehensive synthetic approach

Kazim¹,

Atassi²

1982

Biochemical Journal

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The antigenic structure of the alpha-chain of human haemoglobin was studied by a synthetic approach consisting of the synthesis of a series of consecutive overlapping peptides that together systematically represent the entire primary structure of the protein. This approach enabled the identification of a full profile of immunochemically active alpha-chain peptides and the localization of its major 'continuous' antigenic sites. Antibodies to haemoglobin raised in each of three different species (goat, rabbit and mouse) recognize similar sites on the alpha-chain. Further, the molecular locations of these sites coincide with alpha-chain regions extrapolated from antigenic sites of the conformationally similar myoglobin molecule. These findings support our earlier proposed concept of 'structurally inherent antigenic sites', namely that antigenicity is conferred on certain surface regions of proteins by virtue of their three-dimensional locations. Thus the antigenic sites of conformationally related proteins are likely to have similar molecular locations.

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Section: Synthesis Purification and Characterization Of The Peptidessupporting

confidence: 81%

Structurally inherent antigenic sites. Localization of the antigenic sites of the α-chain of human haemoglobin in three host species by a comprehensive synthetic approach

Kazim¹,

Atassi²

1982

Biochemical Journal

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“…'Structurally inherent' antigenic sites have also been identified in human Hb (Kazim & Atassi, 1977b) and soyabean leghaemoglobin (Hurrell et al, 1978) by extrapolation of the three-dimensional locations of the antigenic sites of sperm-whale Mb. And our studies on bovine and human serum albumins (Atassi et al, 1979;Sakata & Atassi, 1980a) show that their antigenic sites are located at equivalent structural locations.…”

Section: Analysis Of Methods For Studying Cross-reactions Of Proteinsmentioning

confidence: 78%

“…under depleting conditions), all the cross-reacting antibodies in anti-(sperm-whale Mb) sera that can bind with other myoglobins from various species. The immunoadsorbent titration technique employed in the present work makes it possible to achieve this even when the cross-reacting antigenic sites cannot, owing to decreased affinity, effectively compete with the native protein (Kazim & Atassi, 1977b;Sakata & Atassi, 1979a,b;Atassi et al, 1979).…”

Section: Analysis Of Methods For Studying Cross-reactions Of Proteinsmentioning

confidence: 99%

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

Twining¹,

Lehmann²,

Atassi³

1980

Biochemical Journal

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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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“…In recent years, the full profile of antigenic sites involved in B cell recognition (antibody binding) of several proteins-myoglobin (Atassi, 1975), lysozyme (Atassi, 1978), serum albumin (Atassi et al, 1979;Sakata & Atassi, 1980; and haemoglobin (Kazim & Atassi, 1980;Yoshioka & Atassi, 1983)-have been elucidated. In addition, Correspondence: Dr M. Z. Atassi, Department of Biochemistry, Baylor College of Medicine, Houston, TX partial profiles of B cell recognition have been defined in tobacco mosaic virus protein (Benjamini, 1977;Benjamini et al, 1978) cytochrome c (Atassi, 1981) and influenza virus haemagglutinin (Atassi & Webster, 1983;Atassi & Kurisaki, 1984).…”

Section: Introductionmentioning

confidence: 99%

T Cell Recognition of Lysozyme Iv. Localization and Genetic Control of the Continuous T Cell Recognition Sites by Synthetic Overlapping Peptides Representing the Entire Protein Chain

Bixler

Yoshida

Atassi

1984

Int J Immunogenetics

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SUMMARY Recently, this laboratory has developed a comprehensive strategy for the systematic localization of all the ‘continous’ antigenic (as well as other binding) sites of complex multivalent protein antigens involved in B and T cell recognition. The strategy depends on the syntheis of consecutive overlapping peptides that together account for the entire protein chain. This strategy was applied here for the localization of the ‘continuous’ T cell recognition sites of hen egg lysozyme. Eight overlapping peptides encompassing the entire protein chain of lysozyme were synthesized and examined for their ability to stimulate in vitro proliferation of T cells from several mouse strains (A/J, H‐2a; BALB/c and DBA/2, H‐2d; B10.BR, H‐2k; DBA/1, H‐2a; SJL, H‐2s) that had been primed with native lysozyme. This approach enabled the identification of a full profile of in vitro active lysozyme peptides and the localization of four major T cell recognition sites, three of which were subject to individual control.

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Localization and verification by synthesis of five antigenic sites of bovine serum albumin

Cited by 52 publications

References 18 publications

Structurally inherent antigenic sites. Localization of the antigenic sites of the α-chain of human haemoglobin in three host species by a comprehensive synthetic approach

Structurally inherent antigenic sites. Localization of the antigenic sites of the α-chain of human haemoglobin in three host species by a comprehensive synthetic approach

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

T Cell Recognition of Lysozyme Iv. Localization and Genetic Control of the Continuous T Cell Recognition Sites by Synthetic Overlapping Peptides Representing the Entire Protein Chain

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