Identification of a linear epitope recognized by a monoclonal antibody directed to the heterogeneous nucleoriboprotein A2

Research output: Contribution to journalJournal articleResearchpeer-review

Standard

Identification of a linear epitope recognized by a monoclonal antibody directed to the heterogeneous nucleoriboprotein A2. / Tronstrøm, Julie; Dragborg, Anette H.; Hansen, Paul Robert; Houen, Gunnar; Trier, Nicole Hartwig.

In: Protein and Peptide Letters, Vol. 21, No. 1, 2014, p. 25-31.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Tronstrøm, J, Dragborg, AH, Hansen, PR, Houen, G & Trier, NH 2014, 'Identification of a linear epitope recognized by a monoclonal antibody directed to the heterogeneous nucleoriboprotein A2', Protein and Peptide Letters, vol. 21, no. 1, pp. 25-31. https://doi.org/10.2174/09298665113209990085

APA

Tronstrøm, J., Dragborg, A. H., Hansen, P. R., Houen, G., & Trier, N. H. (2014). Identification of a linear epitope recognized by a monoclonal antibody directed to the heterogeneous nucleoriboprotein A2. Protein and Peptide Letters, 21(1), 25-31. https://doi.org/10.2174/09298665113209990085

Vancouver

Tronstrøm J, Dragborg AH, Hansen PR, Houen G, Trier NH. Identification of a linear epitope recognized by a monoclonal antibody directed to the heterogeneous nucleoriboprotein A2. Protein and Peptide Letters. 2014;21(1):25-31. https://doi.org/10.2174/09298665113209990085

Author

Tronstrøm, Julie ; Dragborg, Anette H. ; Hansen, Paul Robert ; Houen, Gunnar ; Trier, Nicole Hartwig. / Identification of a linear epitope recognized by a monoclonal antibody directed to the heterogeneous nucleoriboprotein A2. In: Protein and Peptide Letters. 2014 ; Vol. 21, No. 1. pp. 25-31.

Bibtex

@article{b74be321b39d44b4942a1e15525701dd,
title = "Identification of a linear epitope recognized by a monoclonal antibody directed to the heterogeneous nucleoriboprotein A2",
abstract = "Rheumatoid arthritis (RA) is a chronic autoimmune disorder, characterized by progressive joint destruction and disability. Classical autoantibodies of RA are rheumatoid factors and citrulline antibodies. Patients positive for these autoantibodies are usually associated with a progressive disease course. A subgroup of RA patients does not express citrulline antibodies, instead are approximately 35{\%} of these anti-citrulline-negative patients reported to express autoantibodies to the heterogeneous nucleoriboprotein A2, a ribonucleoprotein involved in RNA transport and processing also referred to as RA33. In the absence of citrulline antibodies, RA33 antibodies have been suggested to be associated with a milder disease course. In this study we screened the reactivity of a monoclonal antibody to RA33-derived peptides by modified enzyme-linked immunosorbent assays (ELISA). Terminally truncated resin-bound peptides were applied for determination of the functional epitope necessary for antibody recognition. In addition, screening of substituted peptides by modified ELISA identified amino acids necessary for antibody reactivity. A potential epitope was identified in the region 71-79 (PHSIDGRVV), where the amino acids Ser, Ile and Asp were found to be essential for antibody reactivity. These amino acids were found to contribute to the antibody-antigen interface through side-chain interactions, possibly in combination with a positively charged amino acid in position 77. Moreover, the amino acids in the N-terminal end (Pro and His) were found to contribute to the interface through backbone contributions. No notable reactivity was found with RA-positive patient sera, thus screening of RA33 antibodies does not seem to be a supplementary for the diagnosis of RA.",
author = "Julie Tronstr{\o}m and Dragborg, {Anette H.} and Hansen, {Paul Robert} and Gunnar Houen and Trier, {Nicole Hartwig}",
year = "2014",
doi = "10.2174/09298665113209990085",
language = "English",
volume = "21",
pages = "25--31",
journal = "Protein and Peptide Letters",
issn = "0929-8665",
publisher = "Bentham Science Publishers",
number = "1",

}

RIS

TY - JOUR

T1 - Identification of a linear epitope recognized by a monoclonal antibody directed to the heterogeneous nucleoriboprotein A2

AU - Tronstrøm, Julie

AU - Dragborg, Anette H.

AU - Hansen, Paul Robert

AU - Houen, Gunnar

AU - Trier, Nicole Hartwig

PY - 2014

Y1 - 2014

N2 - Rheumatoid arthritis (RA) is a chronic autoimmune disorder, characterized by progressive joint destruction and disability. Classical autoantibodies of RA are rheumatoid factors and citrulline antibodies. Patients positive for these autoantibodies are usually associated with a progressive disease course. A subgroup of RA patients does not express citrulline antibodies, instead are approximately 35% of these anti-citrulline-negative patients reported to express autoantibodies to the heterogeneous nucleoriboprotein A2, a ribonucleoprotein involved in RNA transport and processing also referred to as RA33. In the absence of citrulline antibodies, RA33 antibodies have been suggested to be associated with a milder disease course. In this study we screened the reactivity of a monoclonal antibody to RA33-derived peptides by modified enzyme-linked immunosorbent assays (ELISA). Terminally truncated resin-bound peptides were applied for determination of the functional epitope necessary for antibody recognition. In addition, screening of substituted peptides by modified ELISA identified amino acids necessary for antibody reactivity. A potential epitope was identified in the region 71-79 (PHSIDGRVV), where the amino acids Ser, Ile and Asp were found to be essential for antibody reactivity. These amino acids were found to contribute to the antibody-antigen interface through side-chain interactions, possibly in combination with a positively charged amino acid in position 77. Moreover, the amino acids in the N-terminal end (Pro and His) were found to contribute to the interface through backbone contributions. No notable reactivity was found with RA-positive patient sera, thus screening of RA33 antibodies does not seem to be a supplementary for the diagnosis of RA.

AB - Rheumatoid arthritis (RA) is a chronic autoimmune disorder, characterized by progressive joint destruction and disability. Classical autoantibodies of RA are rheumatoid factors and citrulline antibodies. Patients positive for these autoantibodies are usually associated with a progressive disease course. A subgroup of RA patients does not express citrulline antibodies, instead are approximately 35% of these anti-citrulline-negative patients reported to express autoantibodies to the heterogeneous nucleoriboprotein A2, a ribonucleoprotein involved in RNA transport and processing also referred to as RA33. In the absence of citrulline antibodies, RA33 antibodies have been suggested to be associated with a milder disease course. In this study we screened the reactivity of a monoclonal antibody to RA33-derived peptides by modified enzyme-linked immunosorbent assays (ELISA). Terminally truncated resin-bound peptides were applied for determination of the functional epitope necessary for antibody recognition. In addition, screening of substituted peptides by modified ELISA identified amino acids necessary for antibody reactivity. A potential epitope was identified in the region 71-79 (PHSIDGRVV), where the amino acids Ser, Ile and Asp were found to be essential for antibody reactivity. These amino acids were found to contribute to the antibody-antigen interface through side-chain interactions, possibly in combination with a positively charged amino acid in position 77. Moreover, the amino acids in the N-terminal end (Pro and His) were found to contribute to the interface through backbone contributions. No notable reactivity was found with RA-positive patient sera, thus screening of RA33 antibodies does not seem to be a supplementary for the diagnosis of RA.

U2 - 10.2174/09298665113209990085

DO - 10.2174/09298665113209990085

M3 - Journal article

VL - 21

SP - 25

EP - 31

JO - Protein and Peptide Letters

JF - Protein and Peptide Letters

SN - 0929-8665

IS - 1

ER -

ID: 49464444