Purification and characterization of human autoantibodies directed to specific regions on U1RNA; recognition of native U1RNP complexes (original) (raw)

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Institute for Molecular Biology and Tumor Research

Emil-Mannkopffstrasse 2, D-3550 Marburg, Germany

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Institute for Molecular Biology and Tumor Research

Emil-Mannkopffstrasse 2, D-3550 Marburg, Germany

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Walther J. van Venrooij*

* To whom correspondence should be addressed.

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Revision received:

01 October 1993

Accepted:

01 October 1993

Published:

11 November 1993

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Reneé M. Hoet, Berthold Kastner, Reinhard Lührmann, Walther J. van Venrooij, Purification and characterization of human autoantibodies directed to specific regions on U1RNA; recognition of native U1RNP complexes, Nucleic Acids Research, Volume 21, Issue 22, 11 November 1993, Pages 5130–5136, https://doi.org/10.1093/nar/21.22.5130
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Abstract

Antibodies against naked U1RNA can be found in sera from patients with overlap syndromes of systemic lupus erythematosus (SLE) in addition to antibodies directed to the proteins of U1 ribonucleoproteins (U1RNP). We investigated the reactivity of these U1 RNA specific autoantibodies with the native U1RNP particle both in vitro and inside the cell. For this purpose a method was developed to purify human autoantibodies directed to specific regions of U1 RNA. The antibodies are specifically directed to either stemloop II or stemloop IV of U1RNA and do not crossreact with protein components of U1 RNP. Both types of antibody are able to precipitate from cell extracts native UlsnRNPs containing most, if not all, protein components. Immunofluorescence patterns indicate that the antigenic sites on the RNA, i.e. the stem of stemloop II and the loop of stemloop IV, are also available after fixation of the cells. Immunoelectron microscopy employing anti-stemloop IV antibodies and purified, complete UlsnRNP particles showed that stemloop IV is located within the body of the U1RNP complex, which also comprises the Sm site and the common Sm proteins. The anti-U1 RNA autoantibodies described in this paper recognize native U1RNP particles within the cell and can therefore be used as tools to study mechanisms involved in splicing of pre-mRNA.

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© 1993 Oxford University Press

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