Immunochemistry of sperm-whale myoglobin—XXII

Atassi, M. Zouhair; Pai, Rong-Chang

doi:10.1016/0019-2791(75)90223-2

Cited by 47 publications

(11 citation statements)

References 20 publications

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“…They were tested for their response pattern after 5 and 4 cycles of restimulation and resting, respectively ( Table 4). The B2 line responded to p (10)(11)(12)(13)(14)(15)(16)(17)(18)(19)(20)(21)(22), d-Mb and h-Mb, while the B3 line responded to the same peptide and to h-Mb, but not d-Mb. Table 5).…”

Section: Proliferative Response Of B6 T Cell Lines and Clonesmentioning

confidence: 97%

T cell response to myoglobin: a comparison of T cell clones in high‐responder and low‐responder mice

et al. 1988

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Mice carrying the H-2b haplotype (e.g., inbred strains C57BL/6 and C57BL/10) are low responders to sperm whale myoglobin when tested in the T cell proliferation assay. Their response is improved by the removal of the Ly-2+ cells from the lymph node population, but it still remains significantly lower than that of cells cells from high-responder strains (e.g., DBA/2, H-2d). To determine whether T cells from the low and high-responder mice recognize the same or different epitopes on the immunizing antigen, we obtained sets of T cell clones from both strains and tested them against peptides representing different regions of the myoglobin molecule, as well as against myoglobins from species other than the sperm whale. Four types of T cell clones were obtained from the DBA/2 mice: 3 types responded to the peptide 107-120 (9 clones altogether), and 1 type responded to the peptide 133-149 (4 clones altogether). The 3 types responding to the peptide 107-120 could be distinguished by their response to horse myoglobin or by the restriction of the response (Ad vs. Ed). Similarly, 5 types of T cell clones were obtained from the C57BL/6 mice: 2 types responded to the peptide 10-22 (1 type, but not the other, responded to horse myoglobin); 1 type responded to the peptide 133-149; and 2 types did not respond to any of the peptides used (1 type, but not the other, responded to dog myoglobin). All 5 types (13 clones altogether) were presumably Ab restricted. These results demonstrate the diversity of epitopes in single antigenic regions and show equivalent heterogeneity of T cell repertoires in high and low responder mice. Attempts to demonstrate specific T cell suppression in the low responder mice failed; only partial, nonspecific suppression was observed.

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Section: Proliferative Response Of B6 T Cell Lines and Clonesmentioning

confidence: 97%

T cell response to myoglobin: a comparison of T cell clones in high‐responder and low‐responder mice

et al. 1988

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“…b) During the boundary delineation of the antigenic sites of Mb and lysozyme, we have found quite frequently (but not always) that a portion of an antigenic site can bind some (but not all) of the antibodies to the whole site [17,[56][57][58]62,63]. The binding ability of a portion of an antigenic site can be due to the fact [17] that 'antibodies are made against various parts of the site.…”

Section: Heterogeneity Of the Responsementioning

confidence: 99%

Antigenic structures of proteins. Their determination has revealed important aspects of immune recognition and generated strategies for synthetic mimicking of protein binding sites

Atassi

1984

Eur J Biochem

237

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Studies in this laboratory have resulted in the delineation and synthetic verification of several complete protein antigenic structures that are recognized by antibodies. More recently, for the first time, the full profiles of the sites that are recognized by T cells have been localized and confirmed by synthesis for two proteins, myoglobin and lysozyme. These have thus far constituted the only complete antigenic structures to be determined. The availability of these antigenic structures has enabled us to investigate in detail the molecular and cellular parameters responsible for immune recognition, responses to, and control and regulation of these responses to protein antigens at the molecular and submolecular levels. Moreover, these investigations have afforded general strategies for the synthetic mimicking of not only antigenic sites, but also protein binding sites involved in other biological activities.

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“…Therefore, we sought a method that was not predicated upon predictions of particular structural features but rather sought a simple correlation with surface location of stretches of peptide chain and the likelihood of antibody binding. A guiding principle was the notion that many surface oriented regions are nonantigenic (1). This led us to take an empirical approach in our analysis and to arbitrarily manipulate the emphasis placed on certain amino acids in order to find a particular kind of sequence that is favored for antibody binding (which may not strictly depend on the hydrophilicity of the sequence).…”

mentioning

confidence: 99%

“…To precisely delineate antigenic determinants, it is necessary to prepare a large number ofwell-characterized chemical derivatives and peptide fragments from the original protein antigen and then to test these derivatives for immunological activity (1,2). Alternatively, a homologous series of proteins may be used to assess the influence ofparticular amino acid substitutions, thereby implicating certain regions as antigenic determinants (3,4); this approach requires knowledge of complete primary structures for a number of proteins before the immunological results can be interpreted.…”

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confidence: 99%

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Prediction of protein antigenic determinants from amino acid sequences.

Hopp¹,

Woods²

1981

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

3,264

1,549

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A method is presented for locating protein antigenic determinants by analyzing amino acid sequences in order to find the point of greatest local hydrophilicity. This is accomplished by assigning each amino acid a numerical value (hydrophilicity value) and then repetitively averaging these values along the peptide chain. The point ofhighest local average hydrophilicity is invariably located in, or immediately adjacent to, an antigenic determinant. It was found that the prediction success rate depended on averaging group length, with hexapeptide averages yielding optimal results. The method was developed using 12 proteins for which extensive immunochemical analysis has been carried out and subsequently was used to predict antigenic determinants for the following proteins: hepatitis B surface antigen, influenza hemagglutinins, fowl plague virus hemagglutinin, human histocompatibility antigen HLA-B7, human interferons, Escherichia coli and cholera enterotoxins, ragweed allergens Ra3 and Ra5, and streptococcal M protein. The and indicate that they are frequently found on regions of a molecule that have an unusually high degree of exposure to solvent-i. e., regions which project into the medium (for reviews, see refs. 1 and 3). This, together with the fact that charged, hydrophilic amino acid side chains are common features of antigenic determinants, led us to investigate the possibility that at least some antigenic determinants might be associated with stretches of amino acid sequence that contain a large number of charged and polar residues and are lacking in large hydrophobic residues. A suitable means of methodically searching for such regions was found by combining a method like that of Chou and Fasman (5), in which numerical values for amino acids are repetitively averaged over the length ofa polypeptide chain, with a set ofvalues expressing the relative hydrophilicity of each amino acid. Suitable values were available in the solvent parameters assigned by Levitt (6), which are derivatives ofthe hydrophobicity values ofNozaki and Tanford (9).In Table 1 are listed the numerical values (hydrophilicity values) assigned to the 20 amino acids commonly found in proteins. In the first column, the values of Levitt (6) are listed, whereas the second column lists the values that were finally chosen for our hydrophilicity calculations. The values were generally retained as expressed by Levitt; however, changes in the values for proline, asparatic acid, and glutamic acid improve the prediction results, as explained later. Hydrophilicity analysis of a protein is carried out by the following method.Each amino acid in the sequence of the protein is assigned its hydrophilicity value, then these values are repetitively averaged down the length of the polypeptide chain, generating a series of local hydrophilicity values. The number of hydrophilicity values that are averaged at each repetition is arbitrary, and we chose groups of six for our initial studies because this is the approximate size ofan antigenic determinant...

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Immunochemistry of sperm-whale myoglobin—XXII

Cited by 47 publications

References 20 publications

T cell response to myoglobin: a comparison of T cell clones in high‐responder and low‐responder mice

T cell response to myoglobin: a comparison of T cell clones in high‐responder and low‐responder mice

Antigenic structures of proteins. Their determination has revealed important aspects of immune recognition and generated strategies for synthetic mimicking of protein binding sites

Prediction of protein antigenic determinants from amino acid sequences.

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