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Human C4b-binding protein, structural basis for interaction with streptococcal M protein, a major bacterial virulence factor.

Jenkins HT, Mark L, Ball G, Persson J, Lindahl G, Uhrin D, Blom AM, Barlow PN
J Biol Chem 281 3690-7 (2006)
Cited: 43 times
EuropePMC logo PMID: 16330538

Abstract

Human C4b-binding protein (C4BP) protects host tissue, and those pathogens able to hijack this plasma glycoprotein, from complement-mediated destruction. We now show that the first two complement control protein (CCP) modules of the C4BP alpha-chain, plus the four residues connecting them, are necessary and sufficient for binding a bacterial virulence factor, the Streptococcus pyogenes M4 (Arp4) protein. Structure determination by NMR reveals two tightly coupled CCP modules in an elongated arrangement within this region of C4BP. Chemical shift perturbation studies demonstrate that the N-terminal, hypervariable region of M4 binds to a site including strand 1 of CCP module 2. This interaction is accompanied by an intermodular reorientation within C4BP. We thus provide a detailed picture of an interaction whereby a pathogen evades complement.

Articles - 2a55 mentioned but not cited (3)

  1. Structure of the N-terminal region of complement factor H and conformational implications of disease-linked sequence variations. Hocking HG, Herbert AP, Kavanagh D, Soares DC, Ferreira VP, Pangburn MK, Uhrín D, Barlow PN. J Biol Chem 283 9475-9487 (2008)
  2. Binding of complement inhibitor C4b-binding protein to a highly virulent Streptococcus pyogenes M1 strain is mediated by protein H and enhances adhesion to and invasion of endothelial cells. Ermert D, Weckel A, Agarwal V, Frick IM, Björck L, Blom AM. J Biol Chem 288 32172-32183 (2013)
  3. The dipeptidyl peptidase IV inhibitors vildagliptin and K-579 inhibit a phospholipase C: a case of promiscuous scaffolds in proteins. Chakraborty S, Rendón-Ramírez A, Ásgeirsson B, Dutta M, Ghosh AS, Oda M, Venkatramani R, Rao BJ, Dandekar AM, Goñi FM. F1000Res 2 286 (2013)


Reviews citing this publication (13)

  1. Complement driven by conformational changes. Gros P, Milder FJ, Janssen BJ. Nat Rev Immunol 8 48-58 (2008)
  2. Complement evasion strategies of pathogens-acquisition of inhibitors and beyond. Blom AM, Hallström T, Riesbeck K. Mol Immunol 46 2808-2817 (2009)
  3. The streptococcal M protein: a highly versatile molecule. Smeesters PR, McMillan DJ, Sriprakash KS. Trends Microbiol 18 275-282 (2010)
  4. Bacterial complement evasion. Rooijakkers SH, van Strijp JA. Mol Immunol 44 23-32 (2007)
  5. Innate immunity activation on biomaterial surfaces: a mechanistic model and coping strategies. Ekdahl KN, Lambris JD, Elwing H, Ricklin D, Nilsson PH, Teramura Y, Nicholls IA, Nilsson B. Adv Drug Deliv Rev 63 1042-1050 (2011)
  6. Targeted complement inhibition as a promising strategy for preventing inflammatory complications in hemodialysis. DeAngelis RA, Reis ES, Ricklin D, Lambris JD. Immunobiology 217 1097-1105 (2012)
  7. Deciphering complement mechanisms: the contributions of structural biology. Arlaud GJ, Barlow PN, Gaboriaud C, Gros P, Narayana SV. Mol Immunol 44 3809-3822 (2007)
  8. The nonideal coiled coil of M protein and its multifarious functions in pathogenesis. Ghosh P. Adv Exp Med Biol 715 197-211 (2011)
  9. A survey of the year 2006 literature on applications of isothermal titration calorimetry. Okhrimenko O, Jelesarov I. J Mol Recognit 21 1-19 (2008)
  10. Contribution of interactions between complement inhibitor C4b-binding protein and pathogens to their ability to establish infection with particular emphasis on Neisseria gonorrhoeae. Blom AM, Ram S. Vaccine 26 Suppl 8 I49-55 (2008)
  11. Putting the structure into complement. Lea SM, Johnson S. Immunobiology 217 1117-1121 (2012)
  12. Diverse Functions of C4b-Binding Protein in Health and Disease. Werner LM, Criss AK. J Immunol 211 1443-1449 (2023)
  13. IgA-specific proteins of pathogenic bacteria. Kazeeva TN, Shevelev AB. Biochemistry (Mosc) 74 12-21 (2009)

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