Identification and fine mapping of a linear B cell epitope of human vimentin

Research output: Contribution to journalJournal articlepeer-review

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Identification and fine mapping of a linear B cell epitope of human vimentin. / Dam, Catharina E.; Houen, Gunnar ; Hansen, Paul Robert; Trier, Nicole.

In: Scandinavian Journal of Clinical & Laboratory Investigation, Vol. 74, No. 6, 2014, p. 506-514.

Research output: Contribution to journalJournal articlepeer-review

Harvard

Dam, CE, Houen, G, Hansen, PR & Trier, N 2014, 'Identification and fine mapping of a linear B cell epitope of human vimentin', Scandinavian Journal of Clinical & Laboratory Investigation, vol. 74, no. 6, pp. 506-514. https://doi.org/10.3109/00365513.2014.908474

APA

Dam, C. E., Houen, G., Hansen, P. R., & Trier, N. (2014). Identification and fine mapping of a linear B cell epitope of human vimentin. Scandinavian Journal of Clinical & Laboratory Investigation, 74(6), 506-514. https://doi.org/10.3109/00365513.2014.908474

Vancouver

Dam CE, Houen G, Hansen PR, Trier N. Identification and fine mapping of a linear B cell epitope of human vimentin. Scandinavian Journal of Clinical & Laboratory Investigation. 2014;74(6):506-514. https://doi.org/10.3109/00365513.2014.908474

Author

Dam, Catharina E. ; Houen, Gunnar ; Hansen, Paul Robert ; Trier, Nicole. / Identification and fine mapping of a linear B cell epitope of human vimentin. In: Scandinavian Journal of Clinical & Laboratory Investigation. 2014 ; Vol. 74, No. 6. pp. 506-514.

Bibtex

@article{c284496c7c744c6c826ba2997961292d,
title = "Identification and fine mapping of a linear B cell epitope of human vimentin",
abstract = "Knowledge about antibody-antigen interactions is important for the understanding of the immune system mechanisms and for supporting development of drugs and biomarkers. A tool for identification of these antigenic epitopes of specific antibodies is epitope mapping. In this study, a modified enzyme-linked immunosorbent assay was applied for epitope mapping of a mouse monoclonal vimentin antibody using overlapping resin-bound peptides covering the entire vimentin protein. The minimal epitope required for binding was identified as the LDSLPLVD sequence using N- and C-terminally truncated peptides. The peptide sequence LDSLPLVDTH was identified as the complete epitope, corresponding to amino acids 428–437 in the C-terminal end of the human vimentin protein. Alanine scanning and functionality scanning applying substituted peptides were used to identify amino acids essential for antibody reactivity. In particular, the two aspartate residues were found to be essential for antibody reactivity since these amino acids could not be substituted without a reduction in antibody reactivity. The majority of the remaining amino acids could be substituted without reducing antibody reactivity notably. These results confirm that charged amino acids are essential for antibody reactivity and that the vimentin antibody is dependent on side-chain interactions in combination with backbone interactions.",
author = "Dam, {Catharina E.} and Gunnar Houen and Hansen, {Paul Robert} and Nicole Trier",
year = "2014",
doi = "10.3109/00365513.2014.908474",
language = "English",
volume = "74",
pages = "506--514",
journal = "Scandinavian Journal of Clinical & Laboratory Investigation",
issn = "0036-5513",
publisher = "Taylor & Francis",
number = "6",

}

RIS

TY - JOUR

T1 - Identification and fine mapping of a linear B cell epitope of human vimentin

AU - Dam, Catharina E.

AU - Houen, Gunnar

AU - Hansen, Paul Robert

AU - Trier, Nicole

PY - 2014

Y1 - 2014

N2 - Knowledge about antibody-antigen interactions is important for the understanding of the immune system mechanisms and for supporting development of drugs and biomarkers. A tool for identification of these antigenic epitopes of specific antibodies is epitope mapping. In this study, a modified enzyme-linked immunosorbent assay was applied for epitope mapping of a mouse monoclonal vimentin antibody using overlapping resin-bound peptides covering the entire vimentin protein. The minimal epitope required for binding was identified as the LDSLPLVD sequence using N- and C-terminally truncated peptides. The peptide sequence LDSLPLVDTH was identified as the complete epitope, corresponding to amino acids 428–437 in the C-terminal end of the human vimentin protein. Alanine scanning and functionality scanning applying substituted peptides were used to identify amino acids essential for antibody reactivity. In particular, the two aspartate residues were found to be essential for antibody reactivity since these amino acids could not be substituted without a reduction in antibody reactivity. The majority of the remaining amino acids could be substituted without reducing antibody reactivity notably. These results confirm that charged amino acids are essential for antibody reactivity and that the vimentin antibody is dependent on side-chain interactions in combination with backbone interactions.

AB - Knowledge about antibody-antigen interactions is important for the understanding of the immune system mechanisms and for supporting development of drugs and biomarkers. A tool for identification of these antigenic epitopes of specific antibodies is epitope mapping. In this study, a modified enzyme-linked immunosorbent assay was applied for epitope mapping of a mouse monoclonal vimentin antibody using overlapping resin-bound peptides covering the entire vimentin protein. The minimal epitope required for binding was identified as the LDSLPLVD sequence using N- and C-terminally truncated peptides. The peptide sequence LDSLPLVDTH was identified as the complete epitope, corresponding to amino acids 428–437 in the C-terminal end of the human vimentin protein. Alanine scanning and functionality scanning applying substituted peptides were used to identify amino acids essential for antibody reactivity. In particular, the two aspartate residues were found to be essential for antibody reactivity since these amino acids could not be substituted without a reduction in antibody reactivity. The majority of the remaining amino acids could be substituted without reducing antibody reactivity notably. These results confirm that charged amino acids are essential for antibody reactivity and that the vimentin antibody is dependent on side-chain interactions in combination with backbone interactions.

U2 - 10.3109/00365513.2014.908474

DO - 10.3109/00365513.2014.908474

M3 - Journal article

C2 - 24792370

VL - 74

SP - 506

EP - 514

JO - Scandinavian Journal of Clinical & Laboratory Investigation

JF - Scandinavian Journal of Clinical & Laboratory Investigation

SN - 0036-5513

IS - 6

ER -

ID: 119771612