The folded and disordered domains of human ribosomal protein SA have both idiosyncratic and shared functions as membrane receptors
| Autor: | Mohamed B. Ould-Abeih, Nora Zidane, Hugues Bedouelle, Isabelle Petit-Topin |
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| Přispěvatelé: | Prévention et Thérapie Moléculaires des Maladies Infectieuses Humaines, Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Université Paris Diderot - Paris 7 (UPD7), This work was supported by the Pasteur-Weizmann Council and Fondation ARC (grants to M.B.O.-A.) and by ANR [grant number 2010-INTB-1601-03 (to H.B.)]., ANR-10-INTB-1601,ARBOAS,Déchiffrer le rôle de la famille des gènes OAS chez l'homme dans la pathogénèse d'une infection arbovirale(2010), Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS) |
| Rok vydání: | 2012 |
| Předmět: |
Protein Folding
MESH: Heparin DENV dengue virus lcsh:Life lcsh:QR1-502 Plasma protein binding heparin Ligands 67LR 67 kDa laminin receptor an alternative name for LamR1 Biochemistry Ribosome lcsh:Microbiology MESH: Recombinant Proteins MESH: Protein Structure Tertiary 0302 clinical medicine Protein structure Viral Envelope Proteins flavivirus MESH: Receptors Laminin Laminin Protein Interaction Mapping LamR1 laminin receptor 1 (an alternative name for RPSA) MESH: Ligands 37LRP 37 kDa laminin receptor precursor 0303 health sciences WNV West-Nile virus [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM] biology MESH: Escherichia coli Immunochemistry Tryptophan MESH: Enzyme-Linked Immunosorbent Assay MESH: Laminin Recombinant Proteins 3. Good health pNPP pNP phosphate pNP p-nitrophenol [SDV.IMM.IA]Life Sciences [q-bio]/Immunology/Adaptive immunology 030220 oncology & carcinogenesis ED1 ED2 and ED3 domains 1 2 and 3 of the flaviviral envelope protein E Protein folding Yellow fever virus West Nile virus MESH: Spectrometry Fluorescence Protein Binding RPS2 ribosomal protein S2 Ribosomal Proteins Biophysics Enzyme-Linked Immunosorbent Assay S2 Receptors Laminin 03 medical and health sciences Ribosomal protein Cell surface receptor Escherichia coli Humans cancer MESH: Protein Binding mAb monoclonal antibody [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM] VEEV Venezualian equine encephalitis virus Molecular Biology MESH: Tryptophan MESH: West Nile virus 030304 developmental biology Original Paper MESH: Humans MESH: Immunochemistry Cell Membrane MESH: Protein Interaction Mapping Ribosomal protein SA laminin receptor 1 (LamR1) Cell Biology intrinsically disordered protein MESH: Yellow fever virus Protein Structure Tertiary lcsh:QH501-531 Spectrometry Fluorescence YFV yellow fever virus RPSA ribosomal protein SA MESH: Viral Envelope Proteins biology.protein SINV Sindbis virus epigallocatechin-gallate (EGCG) EGCG epigallocatechin gallate MESH: Cell Membrane |
| Zdroj: | Bioscience Reports Bioscience Reports, 2012, 33 (1), pp.113-124. ⟨10.1042/BSR20120103⟩ Bioscience Reports, Portland Press, 2012, 33 (1), pp.113-124. ⟨10.1042/BSR20120103⟩ Bioscience Reports, Vol 33, Iss 1, p e00011 (2012) |
| ISSN: | 1573-4935 0144-8463 |
| DOI: | 10.1042/bsr20120103 |
| Popis: | International audience; 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 (epigallocatechingallate). It contributes to the crossing of the blood-brain 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 K D (dissociation constants) of 300 nM. 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 K D of 100 nM. 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. |
| Databáze: | OpenAIRE |
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