{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,13]],"date-time":"2026-02-13T08:35:18Z","timestamp":1770971718462,"version":"3.50.1"},"reference-count":54,"publisher":"Portland Press Ltd.","issue":"1","license":[{"start":{"date-parts":[[2019,7,25]],"date-time":"2019-07-25T00:00:00Z","timestamp":1564012800000},"content-version":"vor","delay-in-days":2408,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc\/2.5\/"}],"content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2013,2,1]]},"abstract":"<jats:p>The human RPSA [ribosomal protein SA; also known as LamR1(laminin receptor 1)] belongs to the ribosome but is also a membrane receptor for laminin, growth factors, prion, pathogens and the anticarcinogen EGCG (epigallocatechin-gallate). It contributes to the crossing of the blood\u2013brain barrier by neurotropic viruses and bacteria, and is a biomarker of metastasis. RPSA includes an N-terminal domain, which is folded and homologous to the prokaryotic RPS2, and a C-terminal extension, which is intrinsically disordered and conserved in vertebrates. We used recombinant derivatives of RPSA and its N- and C-domains to quantify its interactions with ligands by in-vitro immunochemical and spectrofluorimetric methods. Both N- and C-domains bound laminin with KD (dissociation constants) of 300\u00a0nM. Heparin bound only to the N-domain and competed for binding to laminin with the negatively charged C-domain, which therefore mimicked heparin. EGCG bound only to the N-domain with a KD of 100\u00a0nM. Domain 3 of the envelope protein from yellow fever virus and serotypes-1 and -2 of dengue virus bound preferentially to the C-domain whereas that from West Nile virus bound only to the N-domain. Our quantitative in-vitro approach should help clarify the mechanisms of action of RPSA, and ultimately fight against cancer and infectious agents.<\/jats:p>","DOI":"10.1042\/bsr20120103","type":"journal-article","created":{"date-parts":[[2012,11,12]],"date-time":"2012-11-12T09:18:12Z","timestamp":1352711892000},"update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":19,"title":["The folded and disordered domains of human ribosomal protein SA have both idiosyncratic and shared functions as membrane receptors"],"prefix":"10.1042","volume":"33","author":[{"given":"Nora","family":"Zidane","sequence":"first","affiliation":[{"name":"Institut Pasteur, Unit of Molecular Prevention and Therapy of Human Diseases, Department of Infection and Epidemiology, rue du Dr. Roux, F-75015 Paris, France"},{"name":"CNRS, URA3012, rue du Dr. Roux, F-75015 Paris, France"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mohamed\u00a0B.","family":"Ould-Abeih","sequence":"additional","affiliation":[{"name":"Institut Pasteur, Unit of Molecular Prevention and Therapy of Human Diseases, Department of Infection and Epidemiology, rue du Dr. Roux, F-75015 Paris, France"},{"name":"CNRS, URA3012, rue du Dr. Roux, F-75015 Paris, France"},{"name":"Universit\u00e9 Paris Diderot, Sorbonne Paris Cit\u00e9, Cellule Pasteur, rue du Dr. Roux, F-75015 Paris, France"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Isabelle","family":"Petit-Topin","sequence":"additional","affiliation":[{"name":"Institut Pasteur, Unit of Molecular Prevention and Therapy of Human Diseases, Department of Infection and Epidemiology, rue du Dr. Roux, F-75015 Paris, France"},{"name":"CNRS, URA3012, rue du Dr. Roux, F-75015 Paris, France"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hugues","family":"Bedouelle","sequence":"additional","affiliation":[{"name":"Institut Pasteur, Unit of Molecular Prevention and Therapy of Human Diseases, Department of Infection and Epidemiology, rue du Dr. Roux, F-75015 Paris, France"},{"name":"CNRS, URA3012, rue du Dr. Roux, F-75015 Paris, France"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","published-online":{"date-parts":[[2012,12,20]]},"reference":[{"key":"2021111619074837400_B1","first-page":"495","article-title":"Isolation from a multigene family of the active human gene of the metastasis-associated multifunctional protein 37LRP\/p40 at chromosome 3p21.3","volume":"13","author":"Jackers","year":"1996","journal-title":"Oncogene"},{"key":"2021111619074837400_B2","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1016\/0014-4827(85)90266-6","article-title":"Monoclonal antibodies to the human laminin receptor recognize structurally distinct sites","volume":"156","author":"Liotta","year":"1985","journal-title":"Exp. 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