A recombinant two-module form of human properdin is an inhibitor of the complement alternative pathway

Kouser, Lubna, Abdul-Aziz, Munirah, Tsolaki, Anthony G., Singhal, Dipti, Schwaeble, Wilhelm J., Urban, Britta ORCID: https://orcid.org/0000-0002-4197-8393, Khan, Haseeb A., Sim, Robert B. and Kishore, Uday (2016) 'A recombinant two-module form of human properdin is an inhibitor of the complement alternative pathway'. Molecular Immunology, Vol 73, pp. 76-87.

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Abstract

Properdin upregulates the alternative complement pathway by binding and stabilising the C3 convertase complex (C3bBb). Properdin is a soluble glycoprotein and its flexible rod-like 53 kDa monomers form cyclic polymers (dimers, trimers, tetramers and pentamers). The properdin monomer consists of seven thrombospondin type I repeats (TSR 0–6), which are similar and homologous to domains found in circumsporozoite and thrombospondin-related anonymous proteins of Plasmodium species, ETP100 of Eimeria tenella, various complement components C6-C9, and thrombospondin I and II. Using deletion constructs, TSR4 and TSR5 of human properdin were implicated in C3b binding and stabilising C3 convertase. However, individually expressed TSR4 or TSR5 failed to bind properdin ligands. Here, we have expressed and characterized biologically active TSR4 and TSR5 together (TSR4 + 5) in tandem in Escherichia coli, fused to maltose-binding protein. MBP-TSR4 + 5 bind solid-phase C3b, sulfatides and glycosaminoglycans. In addition, functionally active recombinant TSR4 + 5 modules inhibit the alternative pathway of complement.

Item Type:	Article
Subjects:	QU Biochemistry > Proteins. Amino Acids. Peptides > QU 55 Proteins QW Microbiology and Immunology > Bacteria > QW 138 Enterobacteriaceae WH Hemic and Lymphatic Systems > Hematologic Diseases. Immunologic Factors. Blood Banks > WH 400 Fluid elements. Plasma. Serum. Blood proteins. Blood protein disorders
Faculty: Department:	Biological Sciences > Department of Tropical Disease Biology
Digital Object Identifer (DOI):	https://doi.org/10.1016/j.molimm.2016.03.005
Depositing User:	Jessica Jones
Date Deposited:	13 Apr 2016 11:18
Last Modified:	19 Nov 2024 15:03
URI:	https://archive.lstmed.ac.uk/id/eprint/5842

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