Antigenic structure of myoglobin: The complete immunochemical anatomy of a protein and conclusions relating to antigenic structures of proteins

Atassi, M. Zouhair

doi:10.1016/0019-2791(75)90010-5

Cited by 466 publications

(154 citation statements)

References 80 publications

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“…The predicted locations synthesized here are larger than the precisely delineated antigenic sites of sperm-whale myoglobin (Atassi, 1975) or of hen egg-white lysozyme (Atassi, 1978a,b) and may thus be larger than the actual antigenic sites. They were intentionally enlarged to give the prediction a greater likelihood of success by avoiding errors in prediction of boundaries.…”

Section: Discussionmentioning

confidence: 67%

“…The antibody response to native protein antigens is directed against their native conformation (Atassi, 1967;Atassi & Thomas, 1969). We have reported (Kazim & Atassi, 1977 (Okuda et al, 1978) and varies with the immunized animal (Atassi, 1975(Atassi, , 1978aKoketsu & Atassi, 1973; Lee & Atassi, 1977) and with the period antisera are obtained after immunization (Sakata & Atassi, 1978). The other antigenic sites on bovine serum albumin may either be non-equivalent or be of the type termed (Atassi, 1978a,b;Atassi & Smith, 1978) discontinuous antigenic sites (i.e.…”

Section: Discussionmentioning

confidence: 99%

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

Atassi¹,

Sakata²,

Kazim³

1979

Biochemical Journal

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Recently we have shown that the major antigenic sites of bovine serum albumin exhibit functional equivalence progressively increasing with the time at which antibodies are obtained after the first immunization. Analysis of our recent immunochemical findings and the known covalent structure of bovine serum albumin have enabled us to predict the locations of five antigenic sites of bovine serum albumin. The predicted locations were synthesized, and immunochemical studies with late-course antisera showed them to constitute antigenic sites of native bovine serum albumin.

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Section: Discussionmentioning

confidence: 67%

Section: Discussionmentioning

confidence: 99%

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

Atassi¹,

Sakata²,

Kazim³

1979

Biochemical Journal

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“…Immunogenic epitopes are defined as those parts of a protein that elicit the antibody response when the whole protein is the immunogen. These immunogenic epitopes are believed to be confined to a few loci on the molecule (1)(2)(3). On the other hand, a region of a protein molecule to which an antibody can bind is defined as an antigenic epitope.…”

mentioning

confidence: 99%

Use of peptide synthesis to probe viral antigens for epitopes to a resolution of a single amino acid.

Geysen¹,

Meloen²,

Barteling³

1984

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

1,318

691

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A procedure is described for rapid concurrent synthesis on solid supports of hundreds of peptides, of sufficient purity to react in an enzyme-linked immunosorbent assay. Interaction of synthesized peptides with antibodies is then easily detected without removing them from the support. In this manner an immunogenic epitope of the immunologically important coat protein of foot-and-mouth disease virus (type O1) is located with a resolution of seven amino acids, corresponding to amino acids 146-152 of that protein. Then, a complete replacement set of peptides in which all 20 amino acids were substituted in turn at every position within the epitope was synthesized, and the particular amino acids conferring specificity for the reaction with antibody were determined. It was found that the leucine residues at positions 148 and 151 were essential for reaction with antisera raised against intact virus. A lesser contribution was derived from the glutamine and alanine residues at positions 149 and 152, respectively. Aside from the practical significance for locating and examining epitopes at high resolution, these findings may lead to better understanding of the basis of antigen-antibody interaction and antibody specificity. Recombinant DNA technology now makes possible by deduction from the determined nucleotide sequences reliable amino acid sequences of biologically important proteins. However, methods for identifying the loci in a protein that constitute the antigenic and immunogenic epitopes are few and time consuming and form the bottleneck to further rapid progress. Immunogenic epitopes are defined as those parts of a protein that elicit the antibody response when the whole protein is the immunogen. These immunogenic epitopes are believed to be confined to a few loci on the molecule (1-3). On the other hand, a region of a protein molecule to which an antibody can bind is defined as an antigenic epitope. Antisera prepared against chemically synthesized peptides corresponding to short linear tracts of the total polypeptide sequence have been shown to react well with the native protein (4-9). However, interactions were also found to occur even when the site of interaction did not correspond to an immunogenic epitope of the native protein. This has been interpreted to mean that the number of immunogenic epitopes of a protein is less than the number of antigenic epitopes (4). Conversely, since antibodies produced against the native protein are, by definition, directed to the immunogenic epitopes, it follows that peptides reacting with these antibodies must contain elements of the epitopes. From a study of the few proteins for which the determinants have been accurately mapped, it is postulated that a determinant may consist of a single element (continuous) or of more than one element brought together from linearly distant regions of the polypeptide chain by the folding of that chain as it exists in the native state (discontinuous) (10). Systematic mapping of all the detectable reactive elements of a protein by the ...

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“…What we may be detecting, therefore, with synthetic peptide N-acetyl-(1-4) are antibodies to a topographic determinant on the intact protein that includes both the NH2-terminal region and residue 89. Such a situation is thought to occur with myoglobin where surface residues, which are remote in sequence from the short contiguous sequences originally proposed by Atassi as representing the total antigenicity of the molecule (27), have been clearly identified as being involved in the antigenic sites of this protein (28). If this is the case, the primary response to this determinant on polymerized cyt c may, in fact, be stimulated by the evolutionarily variant residue 89.…”

Section: Methodsmentioning

confidence: 96%

Analysis of an evolutionarily conserved antigenic site on mammalian cytochrome c using synthetic peptides.

Jemmerson¹,

Morrow²,

Paterson³

1985

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

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Two synthetic peptides inclusive of the NH2-terminal N-acetyl-Gly-Asp-Val-Glu tetrapeptide of mammalian cytochrome c (cyt c) were used in this study to address the question of whether mammals can respond immunologically to an evolutionarily conserved region of a protein. These peptides were assessed for their capacity (i) to act as immunogens for the production of anti-self cyt c antisera and (ii) to bind rabbit anti-rodent cyt c antibody. The findings from these studies indicate the existence of an immunogenic determinant in an evolutionarily conserved region of cyt c that contains residues 1-4. This determinant can induce anti-self cyt c antibodies whether presented as a peptide on a carrier protein or in the context of the intact molecule as polymerized mammalian cyt C.

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Antigenic structure of myoglobin: The complete immunochemical anatomy of a protein and conclusions relating to antigenic structures of proteins

Cited by 466 publications

References 80 publications

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

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

Use of peptide synthesis to probe viral antigens for epitopes to a resolution of a single amino acid.

Analysis of an evolutionarily conserved antigenic site on mammalian cytochrome c using synthetic peptides.

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