Girija, Umakhanth Venkatraman, Mitchell, Daniel Anthony, Roscher, Silke and Wallis, Russell. (2011) Carbohydrate recognition and complement activation by rat ficolin-B. European Journal of Immunology, Vol.41 (No.1). pp. 214-223. ISSN 0014-2980

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Abstract

Ficolins are innate immune components that bind to PAMPs and structures on apoptotic cells. Humans produce two serum forms (L-and H-ficolin) and a leukocyte-associated form (M-ficolin), whereas rodents and most other mammals produce ficolins-A and -B, orthologues of L-and M-ficolin, respectively. All three human ficolins, together with mouse and rat ficolin-A, associate with mannan-binding lectin-associated serine proteases (MASPs) and activate the lectin pathway of complement on PAMPs. By contrast, mouse ficolin-B does not bind MASPs and cannot activate complement. Because of these striking differences together with the lack of functional information for other ficolin-B orthologues, we have characterized rat ficolin-B, and compared its physical and biochemical properties with its serum counterpart. The data show that both rat ficolins have archetypal structures consisting of oligomers of a trimeric subunit. Ficolin-B recognized mainly sialyated sugars, characteristic of exogenous and endogenous ligands, whereas ficolin-A had a surprisingly narrow specificity, binding strongly to only one of 320 structures tested: an N-acetylated trisaccharide. Surprisingly, rat ficolin-B activated MASP-2 comparable to ficolin-A. Mutagenesis data reveal that lack of activity in mouse ficolin-B is probably caused by a single amino acid change in the putative MASP-binding site that blocks the ficolin-MASP interaction.

Item Type:	Journal Article
Subjects:	R Medicine > R Medicine (General)
Divisions:	Faculty of Medicine > Warwick Medical School > Clinical Sciences Research Institute (CSRI) Faculty of Medicine > Warwick Medical School
Journal or Publication Title:	European Journal of Immunology
Publisher:	Wiley - V C H Verlag GmbH & Co. KGaA
ISSN:	0014-2980
Date:	January 2011
Volume:	Vol.41
Number:	No.1
Page Range:	pp. 214-223
Identification Number:	10.1002/eji.201040612
Status:	Peer Reviewed
Publication Status:	Published
Access rights to Published version:	Restricted or Subscription Access
Funder:	Medical Research Council (Great Britain) (MRC), Wellcome Trust , National Institute of General Medical Sciences (NIGMS)
Grant number:	G0501425 (MRC), 077400 (Wellcome Trust), GM62116 (NIGMS)
URI:	http://wrap.warwick.ac.uk/id/eprint/41616

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