Please use this identifier to cite or link to this item: http://bura.brunel.ac.uk/handle/2438/12361
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dc.contributor.authorKouser, L-
dc.contributor.authorAbdul-Aziz, M-
dc.contributor.authorTsolaki, AG-
dc.contributor.authorSinghal, D-
dc.contributor.authorSchwaeble, WJ-
dc.contributor.authorUrban, BC-
dc.contributor.authorKhan, HA-
dc.contributor.authorSim, RB-
dc.contributor.authorKishore, U-
dc.date.accessioned2016-03-16T15:52:29Z-
dc.date.available2016-03-16T15:52:29Z-
dc.date.issued2016-
dc.identifier.citationMolecular Immunology, 73: pp. 76 - 87, (2016)en_US
dc.identifier.issn0161-5890-
dc.identifier.urihttps://bura.brunel.ac.uk/handle/2438/12361-
dc.description.abstractProperdin upregulates the alternative complement pathway by binding and stabilising the C3 convertase complex (C3bBb). Properdin is a soluble glycoprotein and its flexible rod-like 53kDa 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 E. 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.en_US
dc.description.sponsorshipBrunel University London, Deanship of Scientific Scientific Research at King Saud Universityen_US
dc.language.isoenen_US
dc.publisherElsevieren_US
dc.rights© 2016 The Authors. Published by Elsevier Ltd. This is an open access article under the CC BY-NC-NDlicense (http://creativecommons.org/licenses/by-nc-nd/4.0/).-
dc.subjectComplementen_US
dc.subjectAlternative pathwayen_US
dc.subjectProperdinen_US
dc.subjectThrombospondinen_US
dc.subjectRecombinanten_US
dc.titleA recombinant two-module form of human properdin is an inhibitor of the complement alternative pathwayen_US
dc.typeArticleen_US
dc.contributor.sponsorLK, AT and UK thank Brunel University London for strategic Infrastructure funding. HAK acknowledges the Deanship of Scientific Research at King Saud University for funding via Group No.RGP-009.-
dc.identifier.doihttps://doi.org/10.1016/j.molimm.2016.03.005-
dc.relation.isPartOfMolecular Immunology-
pubs.publication-statusPublished-
dc.identifier.eissn1872-9142-
Appears in Collections:Dept of Life Sciences Research Papers

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