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A structural model of the Staphylococcus aureus ClfA-fibrinogen interaction opens new avenues for the design of anti-staphylococcal therapeutics.

<div class='caption-title'>ClfA229–545 binds to Fg γ chain peptides.</div>
<div class='caption-title'>Fg and Fg γ1–17D16A peptide truncations binding to different forms of ClfA.</div>
<div class='caption-title'>Representation of ClfAD327C/K541C (N2–N3)-peptide complex.</div>
Ganesh VK, Rivera JJ, Smeds E, Ko YP, Bowden MG, Wann ER, Gurusiddappa S, Fitzgerald JR, Höök M
OpenAccess logo PLoS Pathog 4 e1000226 (2008)
Cited: 98 times
EuropePMC logo PMID: 19043557

Abstract

The fibrinogen (Fg) binding MSCRAMM Clumping factor A (ClfA) from Staphylococcus aureus interacts with the C-terminal region of the fibrinogen (Fg) gamma-chain. ClfA is the major virulence factor responsible for the observed clumping of S. aureus in blood plasma and has been implicated as a virulence factor in a mouse model of septic arthritis and in rabbit and rat models of infective endocarditis. We report here a high-resolution crystal structure of the ClfA ligand binding segment in complex with a synthetic peptide mimicking the binding site in Fg. The residues in Fg required for binding to ClfA are identified from this structure and from complementing biochemical studies. Furthermore, the platelet integrin alpha(IIb)beta(3) and ClfA bind to the same segment in the Fg gamma-chain but the two cellular binding proteins recognize different residues in the common targeted Fg segment. Based on these differences, we have identified peptides that selectively antagonize the ClfA-Fg interaction. The ClfA-Fg binding mechanism is a variant of the "Dock, Lock and Latch" mechanism previously described for the Staphylococcus epidermidis SdrG-Fg interaction. The structural insights gained from analyzing the ClfANFg peptide complex and identifications of peptides that selectively recognize ClfA but not alpha(IIb)beta(3) may allow the design of novel anti-staphylococcal agents. Our results also suggest that different MSCRAMMs with similar structural organization may have originated from a common ancestor but have evolved to accommodate specific ligand structures.

Reviews - 2vr3 mentioned but not cited (2)

  1. Structural biology of Gram-positive bacterial adhesins. Vengadesan K, Narayana SV. Protein Sci 20 759-772 (2011)
  2. Interactions in bacterial biofilm development: a structural perspective. Garnett JA, Matthews S. Curr Protein Pept Sci 13 739-755 (2012)

Articles - 2vr3 mentioned but not cited (8)

  1. A structural model of the Staphylococcus aureus ClfA-fibrinogen interaction opens new avenues for the design of anti-staphylococcal therapeutics. Ganesh VK, Rivera JJ, Smeds E, Ko YP, Bowden MG, Wann ER, Gurusiddappa S, Fitzgerald JR, Höök M. PLoS Pathog 4 e1000226 (2008)
  2. Benchmarking of different molecular docking methods for protein-peptide docking. Agrawal P, Singh H, Srivastava HK, Singh S, Kishore G, Raghava GPS. BMC Bioinformatics 19 426 (2019)
  3. Evidence for steric regulation of fibrinogen binding to Staphylococcus aureus fibronectin-binding protein A (FnBPA). Stemberk V, Jones RP, Moroz O, Atkin KE, Edwards AM, Turkenburg JP, Leech AP, Massey RC, Potts JR. J Biol Chem 289 12842-12851 (2014)
  4. Lessons from the Crystal Structure of the S. aureus Surface Protein Clumping Factor A in Complex With Tefibazumab, an Inhibiting Monoclonal Antibody. Ganesh VK, Liang X, Geoghegan JA, Cohen ALV, Venugopalan N, Foster TJ, Hook M. EBioMedicine 13 328-338 (2016)
  5. Using parallelized incremental meta-docking can solve the conformational sampling issue when docking large ligands to proteins. Devaurs D, Antunes DA, Hall-Swan S, Mitchell N, Moll M, Lizée G, Kavraki LE. BMC Mol Cell Biol 20 42 (2019)
  6. Antagonistic control of Caenorhabditis elegans germline stem cell proliferation and differentiation by PUF proteins FBF-1 and FBF-2. Wang X, Ellenbecker M, Hickey B, Day NJ, Osterli E, Terzo M, Voronina E. Elife 9 e52788 (2020)
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  8. Allantodapsone is a Pan-Inhibitor of Staphylococcus aureus Adhesion to Fibrinogen, Loricrin, and Cytokeratin 10. Prencipe F, Alsibaee A, Khaddem Z, Norton P, Towell AM, Ali AFM, Reid G, Fleury OM, Foster TJ, Geoghegan JA, Rozas I, Brennan MP. Microbiol Spectr 10 e0117521 (2022)


Reviews citing this publication (23)

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  13. Multi-disciplinary antimicrobial strategies for improving orthopaedic implants to prevent prosthetic joint infections in hip and knee. Getzlaf MA, Lewallen EA, Kremers HM, Jones DL, Bonin CA, Dudakovic A, Thaler R, Cohen RC, Lewallen DG, van Wijnen AJ. J Orthop Res 34 177-186 (2016)
  14. Polyproline and triple helix motifs in host-pathogen recognition. Berisio R, Vitagliano L. Curr Protein Pept Sci 13 855-865 (2012)
  15. Exploring Staphylococcus aureus pathways to disease for vaccine development. DeDent A, Kim HK, Missiakas D, Schneewind O. Semin Immunopathol 34 317-333 (2012)
  16. Fatal attraction: how bacterial adhesins affect host signaling and what we can learn from them. Stones DH, Krachler AM. Int J Mol Sci 16 2626-2640 (2015)
  17. Structure, Function, and Assembly of Adhesive Organelles by Uropathogenic Bacteria. Chahales P, Thanassi DG. Microbiol Spectr 3 (2015)
  18. Staphylococcal Biofilms in Atopic Dermatitis. Gonzalez T, Biagini Myers JM, Herr AB, Khurana Hershey GK. Curr Allergy Asthma Rep 17 81 (2017)
  19. Colonization and Infection of Indwelling Medical Devices by Staphylococcus aureus with an Emphasis on Orthopedic Implants. Pietrocola G, Campoccia D, Motta C, Montanaro L, Arciola CR, Speziale P. Int J Mol Sci 23 5958 (2022)
  20. Targeting fundamental pathways to disrupt Staphylococcus aureus survival: clinical implications of recent discoveries. Thomsen IP, Liu GY. JCI Insight 3 98216 (2018)
  21. Staphylococcal Vaccine Antigens related to biofilm formation. Mirzaei B, Babaei R, Valinejad S. Hum Vaccin Immunother 17 293-303 (2021)
  22. Monoclonal Antibodies Targeting Surface-Exposed and Secreted Proteins from Staphylococci. Speziale P, Pietrocola G. Vaccines (Basel) 9 459 (2021)
  23. Bacteria in Fluid Flow. Padron GC, Shuppara AM, Palalay JS, Sharma A, Sanfilippo JE. J Bacteriol 205 e0040022 (2023)

Articles citing this publication (65)

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