The interaction pattern of murine serum ficolin-A with microorganisms.

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...

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Autores principales:	Tina Hummelshøj, Ying Jie Ma, Lea Munthe-Fog, Thomas Bjarnsholt, Claus Moser, Mikkel-Ole Skjoedt, Luigina Romani, Teizo Fujita, Yuichi Endo, Peter Garred
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/73cd62120b7a48b98f1d4da3093f8e91
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spelling	oai:doaj.org-article:73cd62120b7a48b98f1d4da3093f8e912021-11-18T07:16:51ZThe interaction pattern of murine serum ficolin-A with microorganisms.1932-620310.1371/journal.pone.0038196https://doaj.org/article/73cd62120b7a48b98f1d4da3093f8e912012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22666482/?tool=EBIhttps://doaj.org/toc/1932-6203The 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.Tina HummelshøjYing Jie MaLea Munthe-FogThomas BjarnsholtClaus MoserMikkel-Ole SkjoedtLuigina RomaniTeizo FujitaYuichi EndoPeter GarredPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 5, p e38196 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Tina Hummelshøj Ying Jie Ma Lea Munthe-Fog Thomas Bjarnsholt Claus Moser Mikkel-Ole Skjoedt Luigina Romani Teizo Fujita Yuichi Endo Peter Garred The interaction pattern of murine serum ficolin-A with microorganisms.
description	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.
format	article
author	Tina Hummelshøj Ying Jie Ma Lea Munthe-Fog Thomas Bjarnsholt Claus Moser Mikkel-Ole Skjoedt Luigina Romani Teizo Fujita Yuichi Endo Peter Garred
author_facet	Tina Hummelshøj Ying Jie Ma Lea Munthe-Fog Thomas Bjarnsholt Claus Moser Mikkel-Ole Skjoedt Luigina Romani Teizo Fujita Yuichi Endo Peter Garred
author_sort	Tina Hummelshøj
title	The interaction pattern of murine serum ficolin-A with microorganisms.
title_short	The interaction pattern of murine serum ficolin-A with microorganisms.
title_full	The interaction pattern of murine serum ficolin-A with microorganisms.
title_fullStr	The interaction pattern of murine serum ficolin-A with microorganisms.
title_full_unstemmed	The interaction pattern of murine serum ficolin-A with microorganisms.
title_sort	interaction pattern of murine serum ficolin-a with microorganisms.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/73cd62120b7a48b98f1d4da3093f8e91
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The interaction pattern of murine serum ficolin-A with microorganisms.

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