Abstract
The ficolins are soluble pattern recognition molecules in the lectin pathway of complement, but the spectrum and mode of interaction with pathogens are largely unknown. In this study, we investigated the binding properties of the murine serum ficolin-A towards a panel of different clinical relevant microorganisms (N = 45) and compared the binding profile with human serum ficolin-2 and ficolin-3. Ficolin-A was able to bind Gram-positive bacteria strains including E. faecalis, L. monocytogenes and some S. aureus strains, but not to the investigated S. agalactiae (Group B streptococcus) strains. Regarding Gram-negative bacteria ficolin-A was able to bind to some E. coli and P. aeruginosa strains, but not to the investigated Salmonella strains. Of particular interest ficolin-A bound strongly to the pathogenic E. coli, O157:H7 and O149 strains, but it did not bind to the non-pathogenic E. coli, ATCC 25922 strain. Additionally, ficolin-A was able to bind purified LPS from these pathogenic strains. Furthermore, ficolin-A bound to a clinical isolate of the fungus A. fumigatus. In general ficolin-2 showed similar selective binding spectrum towards pathogenic microorganisms as observed for ficolin-A indicating specific pathophysiological roles of these molecules in host defence. In contrast, ficolin-3 did not bind to any of the investigated microorganisms and the anti-microbial role of ficolin-3 still remains elusive.
Highlights
The ficolins are recognition molecules in the lectin pathway of the complement system that bind to specific structures on microorganisms and self cellular debris enabling quick and simple aggregation and opsonization of hazardous material [1,2].The ficolins are highly oligomerized glycoproteins containing both collagen-like (CL) and fibrinogen-like (FBG) regions
In this study we investigated the binding of the mouse ficolin-A to a number of different clinical relevant microbial strains and compared this binding profile to human serum ficolin-2 and ficolin-3
The same issue may be relevant for other bacteria strains as the Group B Streptococci that previously has been shown to bind ficolin-2 [16], where we could only confirm a weaker binding to these strains
Summary
The ficolins are recognition molecules in the lectin pathway of the complement system that bind to specific structures on microorganisms and self cellular debris enabling quick and simple aggregation and opsonization of hazardous material [1,2].The ficolins are highly oligomerized glycoproteins containing both collagen-like (CL) and fibrinogen-like (FBG) regions. The ficolins are recognition molecules in the lectin pathway of the complement system that bind to specific structures on microorganisms and self cellular debris enabling quick and simple aggregation and opsonization of hazardous material [1,2]. As seen for mannose-binding lectin (MBL), the CL region is able to associate with the MBL/ficolin associated serine proteases (MASPs), which activate the lectin pathway of the complement system [1]. Through the FBG domain they bind structures such as N-acetylglucosamine (GlcNAc), N-acetyl-galactosamine (GalNAc), and acetylated compounds located on the target cell [6,7]. Two ficolin molecules have been identified in mice termed ficolin-A and ficolin-B. The mouse homologue of the human ficolin-3 gene is identified as a pseudogene in mice and rats [15]
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