Academic literature on the topic 'Peptide/antigen'

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Journal articles on the topic "Peptide/antigen"

1

Tam, James P., and Fidel Zavala. "Multiple antigen peptide." Journal of Immunological Methods 124, no. 1 (1989): 53–61. http://dx.doi.org/10.1016/0022-1759(89)90185-3.

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2

TAKIGUCHI, MASAFUMI. "HLA AND ANTIGEN PEPTIDE." Vox Sanguinis 70, S3 (1996): 102–10. http://dx.doi.org/10.1111/j.1423-0410.1996.tb01380.x.

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3

Marusina, Kate, and John J. Monaco. "Peptide transport in antigen presentation." Current Opinion in Hematology 3, no. 1 (1996): 19–26. http://dx.doi.org/10.1097/00062752-199603010-00004.

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4

Adorini, Luciano, and Zoltan A. Nagy. "Peptide competition for antigen presentation." Immunology Today 11 (January 1990): 21–24. http://dx.doi.org/10.1016/0167-5699(90)90006-u.

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5

de Kroon, A. I., and H. M. McConnell. "Enhancement of peptide antigen presentation by a second peptide." Proceedings of the National Academy of Sciences 90, no. 19 (1993): 8797–801. http://dx.doi.org/10.1073/pnas.90.19.8797.

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6

Watts, T. H., J. Gariepy, G. K. Schoolnik, and H. M. McConnell. "T-cell activation by peptide antigen: effect of peptide sequence and method of antigen presentation." Proceedings of the National Academy of Sciences 82, no. 16 (1985): 5480–84. http://dx.doi.org/10.1073/pnas.82.16.5480.

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7

Tran, Phat, Jonathan Kopel, Joe A. Fralick, and Ted W. Reid. "The Use of an Organo-Selenium Peptide to Develop New Antimicrobials That Target a Specific Bacteria." Antibiotics 10, no. 6 (2021): 611. http://dx.doi.org/10.3390/antibiotics10060611.

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This study examines the use of a covalently selenium-bonded peptide and phage that binds to the Yersinia pestis F1 antigen for the targeting and killing of E. coli expressing this surface antigen. Using a Ph.D.-12 phage-display library for affinity selection of the phage which would bind the F1 antigen of Y. pestis, a phage displaying a peptide that binds the F1 antigen with high affinity and specificity was identified. Selenium was then covalently attached to the display phage and the corresponding F1-antigen-binding peptide. Both the phage and peptides with selenium covalently attached retained their binding specificity for the Y. pestis F1 antigen. The phage or peptide not labeled with selenium did not kill the targeted bacteria, while the phage or peptide labeled with selenium did. In addition, the seleno-peptide, expressing the F1 targeting sequence only, killed cells expressing the F1 antigen but not the parent strain that did not express the F1 antigen. Specifically, the seleno-peptide could kill eight logs of bacteria in less than two hours at a 10-µM concentration. These results demonstrate a novel approach for the development of an antibacterial agent that can target a specific bacterial pathogen for destruction through the use of covalently attached selenium and will not affect other bacteria.
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8

Huang, Wolin, Bernardetta Nardelli, and James P. Tam. "Lipophilic multiple antigen peptide system for peptide immunogen and synthetic vaccine." Molecular Immunology 31, no. 15 (1994): 1191–99. http://dx.doi.org/10.1016/0161-5890(94)90033-7.

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9

Coles, Charlotte H., Catriona McMurran, Angharad Lloyd, et al. "T cell receptor interactions with human leukocyte antigen govern indirect peptide selectivity for the cancer testis antigen MAGE-A4." Journal of Biological Chemistry 295, no. 33 (2020): 11486–94. http://dx.doi.org/10.1074/jbc.ra120.014016.

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T cell-mediated immunity is governed primarily by T cell receptor (TCR) recognition of peptide-human leukocyte antigen (pHLA) complexes and is essential for immunosurveillance and disease control. This interaction is generally stabilized by interactions between the HLA surface and TCR germline-encoded complementarity-determining region (CDR) loops 1 and 2, whereas peptide selectivity is guided by direct interactions with the TCR CDR3 loops. Here, we solved the structure of a newly identified TCR in complex with a clinically relevant peptide derived from the cancer testis antigen melanoma antigen-A4 (MAGE-A4). The TCR bound pHLA in a position shifted toward the peptide's N terminus. This enabled the TCR to achieve peptide selectivity via an indirect mechanism, whereby the TCR sensed the first residue of the peptide through HLA residue Trp-167, which acted as a tunable gateway. Amino acid substitutions at peptide position 1 predicted to alter the HLA Trp-167 side-chain conformation abrogated TCR binding, indicating that this indirect binding mechanism is essential for peptide recognition. These findings extend our understanding of the molecular rules that underpin antigen recognition by TCRs and have important implications for the development of TCR-based therapies.
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10

Van Kaer, Luc. "Antigen Presentation: Discovery of the Peptide TAP." Journal of Immunology 180, no. 5 (2008): 2723–24. http://dx.doi.org/10.4049/jimmunol.180.5.2723.

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