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Mode of interaction between beta2GPI and lipoprotein receptors suggests mutually exclusive binding of beta2GPI to the receptors and anionic phospholipids.

Lee CJ, De Biasio A, Beglova N
Structure 18 366-76 (2010)
Cited: 22 times
EuropePMC logo PMID: 20223219

Abstract

Lipoprotein receptors of the LDLR family serve as clearance receptors for beta2GPI and as signaling receptors for the beta2GPI/antibody complexes in antiphospholipid syndrome. We compared four ligand-binding LA modules from LDLR and ApoER2 for their ability to bind domain V of beta2GPI (beta2GPI-DV). We found that the LA modules capable of binding beta2GPI-DV interact with the same region on beta2GPI-DV using residues at their calcium-coordination site. The structure of a complex between beta2GPI-DV and LA4 of LDLR, solved by molecular docking guided by NMR-derived restraints and extensively validated, represents the general mode of interaction between beta2GPI and lipoprotein receptors. We have shown that beta2GPI-DV cannot simultaneously bind to lipoprotein receptors and anionic phospholipids, suggesting that the association of beta2GPI/anti-beta2GPI antibody complexes with anionic phospholipids will interfere with lipoprotein receptors' signaling in APS.

Articles - 2kri mentioned but not cited (6)

  1. Elucidation of the conformational free energy landscape in H.pylori LuxS and its implications to catalysis. Bhattacharyya M, Vishveshwara S. BMC Struct. Biol. 10 27 (2010)
  2. New horizons for lipoprotein receptors: communication by β-propellers. Andersen OM, Dagil R, Kragelund BB. J. Lipid Res. 54 2763-2774 (2013)
  3. An A1-A1 mutant with improved binding and inhibition of β2GPI/antibody complexes in antiphospholipid syndrome. Kolyada A, Karageorgos I, Mahlawat P, Beglova N. FEBS J. 282 864-873 (2015)
  4. Identification of the binding site for fondaparinux on Beta2-glycoprotein I. Kolyada A, De Biasio A, Beglova N. Biochim. Biophys. Acta 1834 2080-2088 (2013)
  5. Targeting Neuroblastoma Cell Surface Proteins: Recommendations for Homology Modeling of hNET, ALK, and TrkB. Haddad Y, Heger Z, Adam V. Front Mol Neurosci 10 7 (2017)
  6. Dimerized Domain V of Beta2-Glycoprotein I Is Sufficient to Upregulate Procoagulant Activity in PMA-Treated U937 Monocytes and Require Intact Residues in Two Phospholipid-Binding Loops. Kolyada A, Barrios DA, Beglova N. Antibodies (Basel) 6 (2017)


Reviews citing this publication (5)

  1. The pathogenesis of the antiphospholipid syndrome. Giannakopoulos B, Krilis SA. N. Engl. J. Med. 368 1033-1044 (2013)
  2. The significance of autoantibodies against β2-glycoprotein I. de Groot PG, Urbanus RT. Blood 120 266-274 (2012)
  3. Low-density lipoprotein receptor-related protein-1: role in the regulation of vascular integrity. Strickland DK, Au DT, Cunfer P, Muratoglu SC. Arterioscler. Thromb. Vasc. Biol. 34 487-498 (2014)
  4. Anti-β2-glycoprotein I antibodies. Willis R, Pierangeli SS. Ann. N. Y. Acad. Sci. 1285 44-58 (2013)
  5. Entangling COVID-19 associated thrombosis into a secondary antiphospholipid antibody syndrome: Diagnostic and therapeutic perspectives (Review). Cavalli E, Bramanti A, Ciurleo R, Tchorbanov AI, Giordano A, Fagone P, Belizna C, Bramanti P, Shoenfeld Y, Nicoletti F. Int J Mol Med 46 903-912 (2020)

Articles citing this publication (11)

  1. SorLA complement-type repeat domains protect the amyloid precursor protein against processing. Mehmedbasic A, Christensen SK, Nilsson J, Rüetschi U, Gustafsen C, Poulsen AS, Rasmussen RW, Fjorback AN, Larson G, Andersen OM. J. Biol. Chem. 290 3359-3376 (2015)
  2. A novel dimeric inhibitor targeting Beta2GPI in Beta2GPI/antibody complexes implicated in antiphospholipid syndrome. Kolyada A, Lee CJ, De Biasio A, Beglova N. PLoS ONE 5 e15345 (2010)
  3. Inhibition of thrombotic properties of persistent autoimmune anti-β2GPI antibodies in the mouse model of antiphospholipid syndrome. Kolyada A, Porter A, Beglova N. Blood 123 1090-1097 (2014)
  4. Modulation of Mitochondrial Antiviral Signaling by Human Herpesvirus 8 Interferon Regulatory Factor 1. Hwang KY, Choi YB. J. Virol. 90 506-520 (2016)
  5. Factor VIII Interacts with the Endocytic Receptor Low-density Lipoprotein Receptor-related Protein 1 via an Extended Surface Comprising "Hot-Spot" Lysine Residues. van den Biggelaar M, Madsen JJ, Faber JH, Zuurveld MG, van der Zwaan C, Olsen OH, Stennicke HR, Mertens K, Meijer AB. J. Biol. Chem. 290 16463-16476 (2015)
  6. Anti-β2-glycoprotein I and anti-prothrombin antibodies cause lupus anticoagulant through different mechanisms of action. Noordermeer T, Molhoek JE, Schutgens REG, Sebastian SAE, Drost-Verhoef S, van Wesel ACW, de Groot PG, Meijers JCM, Urbanus RT. J Thromb Haemost 19 1018-1028 (2021)
  7. High Affinity Binding of the Receptor-associated Protein D1D2 Domains with the Low Density Lipoprotein Receptor-related Protein (LRP1) Involves Bivalent Complex Formation: CRITICAL ROLES OF LYSINES 60 AND 191. Prasad JM, Young PA, Strickland DK. J. Biol. Chem. 291 18430-18439 (2016)
  8. High-affinity binding of plasminogen-activator inhibitor 1 complexes to LDL receptor-related protein 1 requires lysines 80, 88, and 207. Migliorini M, Li SH, Zhou A, Emal CD, Lawrence DA, Strickland DK. J Biol Chem 295 212-222 (2020)
  9. Soluble analog of ApoER2 targeting beta2-glycoprotein I in immune complexes counteracts hypertension in lupus-prone mice with spontaneous antiphospholipid syndrome. Kolyada A, Ke Q, Karageorgos I, Mahlawat P, Barrios DA, Kang PM, Beglova N. J. Thromb. Haemost. 14 1298-1307 (2016)
  10. Structures of LRP2 reveal a molecular machine for endocytosis. Beenken A, Cerutti G, Brasch J, Guo Y, Sheng Z, Erdjument-Bromage H, Aziz Z, Robbins-Juarez SY, Chavez EY, Ahlsen G, Katsamba PS, Neubert TA, Fitzpatrick AWP, Barasch J, Shapiro L. Cell 186 821-836.e13 (2023)
  11. The J-elongated conformation of β2-glycoprotein I predominates in solution: implications for our understanding of antiphospholipid syndrome. Ruben E, Planer W, Chinnaraj M, Chen Z, Zuo X, Pengo V, De Filippis V, Alluri RK, McCrae KR, Macor P, Tedesco F, Pozzi N. J Biol Chem 295 10794-10806 (2020)


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