Subtle sequence differences in a turnour-associated peptide epitope translate into major changes in antigenicity
Persson, Jonas LU ; Lantto, Johan LU ; Drakenberg, Torbjörn LU and Ohlin, Mats LU
(2005)
In Molecular Immunology
42(11).
p.1321-1330
- Abstract
- Antigenicity, the ability to bind to members of repertoire of diverse immune receptors, is a concept that is poorly characterised with respect to its defining parameters. To learn more about its makeup, we have investigated the ability of two peptides with highly related sequences, derived from the tumour-associated antigen mucin-1, to recruit in vitro members from a large naive repertoire of synthetic human antibody fragments. One of the peptides represents the epitope that is immunodominant in mice. We now demonstrate that the other peptide, which differs from the first only by a very conservative aspartate-threonine to glutamate-serine change, is much less antigenic than the first peptide. This is so despite the fact that there is no... (More)
- Antigenicity, the ability to bind to members of repertoire of diverse immune receptors, is a concept that is poorly characterised with respect to its defining parameters. To learn more about its makeup, we have investigated the ability of two peptides with highly related sequences, derived from the tumour-associated antigen mucin-1, to recruit in vitro members from a large naive repertoire of synthetic human antibody fragments. One of the peptides represents the epitope that is immunodominant in mice. We now demonstrate that the other peptide, which differs from the first only by a very conservative aspartate-threonine to glutamate-serine change, is much less antigenic than the first peptide. This is so despite the fact that there is no observable difference in the tendency of the two peptides to adopt a structure in solution. Furthermore, the peptides differ in their immunodominant parts and the less antigenic peptide selects for antibody fragments targeting residues outside of the epitope considered to be immunodominant in mice. We conclude that subtle sequence changes greatly, affect antigenicity and immunodominance of epitopes in this important tumour-associated antigen. (c) 2005 Elsevier Ltd. All rights reserved. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/152130
- author
- Persson, Jonas
LU
; Lantto, Johan
LU
; Drakenberg, Torbjörn
LU
and Ohlin, Mats
LU
- organization
- publishing date
- 2005
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Molecular Immunology
- volume
- 42
- issue
- 11
- pages
- 1321 - 1330
- publisher
- Pergamon Press Ltd.
- external identifiers
-
- pmid:15950728
- wos:000230336400007
- scopus:20444408755
- ISSN
- 1872-9142
- DOI
- 10.1016/j.molimm.2004.12.010
- language
- English
- LU publication?
- yes
- id
- ef5fc94a-09af-4484-be79-cc648a05f568 (old id 152130)
- date added to LUP
- 2016-04-01 16:33:40
- date last changed
- 2022-01-28 20:34:01
@article{ef5fc94a-09af-4484-be79-cc648a05f568,
abstract = {{Antigenicity, the ability to bind to members of repertoire of diverse immune receptors, is a concept that is poorly characterised with respect to its defining parameters. To learn more about its makeup, we have investigated the ability of two peptides with highly related sequences, derived from the tumour-associated antigen mucin-1, to recruit in vitro members from a large naive repertoire of synthetic human antibody fragments. One of the peptides represents the epitope that is immunodominant in mice. We now demonstrate that the other peptide, which differs from the first only by a very conservative aspartate-threonine to glutamate-serine change, is much less antigenic than the first peptide. This is so despite the fact that there is no observable difference in the tendency of the two peptides to adopt a structure in solution. Furthermore, the peptides differ in their immunodominant parts and the less antigenic peptide selects for antibody fragments targeting residues outside of the epitope considered to be immunodominant in mice. We conclude that subtle sequence changes greatly, affect antigenicity and immunodominance of epitopes in this important tumour-associated antigen. (c) 2005 Elsevier Ltd. All rights reserved.}},
author = {{Persson, Jonas and Lantto, Johan and Drakenberg, Torbjörn and Ohlin, Mats}},
issn = {{1872-9142}},
language = {{eng}},
number = {{11}},
pages = {{1321--1330}},
publisher = {{Pergamon Press Ltd.}},
series = {{Molecular Immunology}},
title = {{Subtle sequence differences in a turnour-associated peptide epitope translate into major changes in antigenicity}},
url = {{http://dx.doi.org/10.1016/j.molimm.2004.12.010}},
doi = {{10.1016/j.molimm.2004.12.010}},
volume = {{42}},
year = {{2005}},
}