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Inflammation and Retinal Disease: Complement Biology and Pathology pp 25–47Cite as

Multiple Interactions of Complement Factor H with Its Ligands in Solution: A Progress Report

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Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 703))

Abstract

Factor H (FH) is the major regulator of the central complement protein C3b in the alternative pathway of complement activation, and is comprised of 20 SCR domains. A FH Tyr402His polymorphism in SCR-7 is associated with age-related macular degeneration (AMD) and leads to deposition of complement in drusen. The unravelling of how FH interacts with five major physiological and patho-physiological ligands is complicated by the weak nature of these interactions, coupled with the multivalency of FH. Using multiple biophysical methods, we summarise our recent results for these five FH ligands: (1) FH by itself shows a folded-back SCR domain structure in solution, and self-associates in a manner dependent on electrostatic forces. (2) FH activity is inhibited by zinc, which causes FH to aggregate. The onset of FH-zinc aggregation for zinc concentrations above 20 μM appears to be enhanced with the His402 allotype, and may be relevant to AMD. (3) The FH and C-reactive protein (CRP) interaction has been controversial; however our new work resolves earlier discrepancies. The FH-CRP interaction is only observed when native CRP is at high acute-phase concentration levels, and CRP binds weakly to the His402 FH allotype to suggest a molecular mechanism that leads to AMD. (4) Heparin is an analogue of the polyanionic host cell surface, and FH forms higher oligomers with larger heparin fragments, suggesting a mechanism for more effective FH regulation. (5) The interaction of C3b with FH also depends on buffer, and FH forms multimers with the C3d fragment of C3b. This FH-C3d interaction at high FH concentration may also facilitate complement regulation. Overall, our results to date suggest that the FH interactions involving zinc and native CRP have the closest relevance for explaining the onset of AMD.

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Notes

  1. 1.

    FH and ligand concentrations are reported in both mg/ml and μM units in this review. Units of μM permit comparison with dissociation constant KD values reported in μM units. For a 1:1 FH-ligand equilibrium, the KD value is given by [FH][ligand]/[complex], and KD corresponds to the FH concentration at which the complex is 50% dissociated.

  2. 2.

    There are literature discrepancies in the determination of FH concentrations. Recent mass spectrometry shows that eight of the nine putative N-glycosylation sites are occupied (Fenaille et al. 2007). From this and the FH sequence, the FH molecular mass is calculated as 154.4 kDa and the FH absorption coefficient at 280 nm (1%, 1 cm path length) is revised to be 16.2. Other groups reported a high absorption coefficient of 19.5 (Hakobyan et al. 2008a) or lower ones of 14.2 and 12.4 (Sim and DiScipio 1982; Pangburn et al. 2009). The value of 16.2 used in our work is conveniently close to the mean of these three experimental determinations.

  3. 3.

    The determination of the FH SCR-6/8 solution structure, its dimerisation and its interaction with heparin dp10 (Fernando et al. 2007) was not discussed in the subsequent high resolution crystal structure study of SCR-6/8 with the heparin analogue SOS (Prosser et al. 2007). Three authors of the second study were also co-authors of the first study. The two SCR-6/8 structures were very similar, but this was not acknowledged in the second study. The second study also suggested that heparin dp18 and dp24 formed an extended 1:1 complex with SCR-6/8. These further conclusions did not consider SCR-6/8 dimerisation or heparin-induced changes described in the first study. To date, corrections requested by the journal editor from the authors of the second study to clarify the relationship to the first study have not been published.

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Acknowledgements

We thank University College London, the Biotechnology and Biological Sciences Research Council, the Mercer Fund of the Fight For Sight Charity, the Henry Smith Charity and the Higher Education Commission of Pakistan for studentship and grant funding. We are particularly grateful to Dr Imre Lengyel and Prof Alan Bird of the UCL Institute of Ophthalmology for useful discussions in relation to AMD, and Jayesh Gor in the UCL Structural Immunology group and Dr Theyencheri Narayanan, Dr Anuj Shukla and Dr Shirley Callow at ESRF for invaluable instrumental support.

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  1. Department of Structural and Molecular Biology, University College London, London, UK

    Stephen J. Perkins

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  1. Stephen J. Perkins
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  2. Ruodan Nan
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  3. Azubuike I. Okemefuna
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  4. Keying Li
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  5. Sanaullah Khan
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  6. Ami Miller
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Correspondence to Stephen J. Perkins .

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Editors and Affiliations

  1. Department Of Pathology Laboratory Of, Medicine, University Of Pennsylvania, Johnson Pavilion 410, Philadelphia, 19104, USA

    John D. Lambris

  2. , Department of Ophthalmology and Visual S, University of Illinois at Chicago, Chicago, 62269-3745, USA

    Anthony P. Adamis

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Perkins, S.J., Nan, R., Okemefuna, A.I., Li, K., Khan, S., Miller, A. (2010). Multiple Interactions of Complement Factor H with Its Ligands in Solution: A Progress Report. In: Lambris, J., Adamis, A. (eds) Inflammation and Retinal Disease: Complement Biology and Pathology. Advances in Experimental Medicine and Biology, vol 703. Springer, New York, NY. https://doi.org/10.1007/978-1-4419-5635-4_3

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