The interaction pattern of murine serum ficolin-A with microorganisms
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The interaction pattern of murine serum ficolin-A with microorganisms. / Hummelshøj, Tina; Ma, Ying Jie; Munthe-Fog, Lea; Bjarnsholt, Thomas; Moser, Claus; Skjødt, Mikkel-Ole; Romani, Luigina; Fujita, Teizo; Endo, Yuichi; Garred, Peter.
In: P L o S One, Vol. 7, No. 5, 2012, p. 1-12.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - The interaction pattern of murine serum ficolin-A with microorganisms
AU - Hummelshøj, Tina
AU - Ma, Ying Jie
AU - Munthe-Fog, Lea
AU - Bjarnsholt, Thomas
AU - Moser, Claus
AU - Skjødt, Mikkel-Ole
AU - Romani, Luigina
AU - Fujita, Teizo
AU - Endo, Yuichi
AU - Garred, Peter
PY - 2012
Y1 - 2012
N2 - 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.
AB - 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.
KW - Animals
KW - Bacteria
KW - Fungi
KW - Humans
KW - Lectins
KW - Lipopolysaccharides
KW - Mice
KW - Protein Binding
U2 - 10.1371/journal.pone.0038196
DO - 10.1371/journal.pone.0038196
M3 - Journal article
C2 - 22666482
VL - 7
SP - 1
EP - 12
JO - PLoS ONE
JF - PLoS ONE
SN - 1932-6203
IS - 5
ER -
ID: 46134226