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• W100306963 abstract "Ficolins are members of the collectin family of proteins which in human and mice are able to recognize pathogen associated molecular patterns (PAMPs) on microbial surfaces. Ficolins trigger the activation of the innate immune system by initiating the complement cascade in serum upon binding to their specific PAMPs. Our group recently published the first observation on the cellular localization of mouse ficolin-B. In contrast to the human ortholog M-ficolin which is secreted, ficolin-B was only detected intracellularly in peritoneal macrophages (Runza et al., 2006). Investigations on the expression profile in our laboratory indicated that ficolin-B expression is down-regulated upon maturation of myeloid cells such as macrophages, granulocytes, and bone marrow-derived dendritic cells suggesting a critical role of ficolin-B during early stages of cell activation upon pathogen encounter. In contrast to others who have shown that ficolin-B does not associate to serine proteases and, therefore, is unable to activate the complement system (Endo et al., 2005) unpublished findings by our group show complement activation by ficolin-B. However, the biological relevance of these findings and the function of mouse ficolin-B upon bacterial challenge remains to be elucidated. An established method for the recombinant production of ficolin-B in an eukaryotic (insect) expression (DS2 cells) system exists in our lab. This method is, however, expensive and time consuming. The first goal of this work was to establish an alternative expression system in E. coli to produce recombinant ficolin-B without tag. The biological activity of the E. coli-expressed ficolin-B was to be compared to the activity of the DS2-expressed ficolin-B. The protein should then be used to immunize rats to generate monoclonal antibodies.In the second part of the project functional characterization of ficolin-B through mutational analysis should be tested. Ficolin-B muteins are expected to define the differences in fine specificity as shown by Xenopus, mouse, and human ficolins and, as such, bring evidence for adaptive changes during evolution. Ficolin-B has a conserved collagen binding site (Girija et al., 2007) that has been linked to important functions such as lectin pathway activation and collaboration with the blood coagulation system by interacting with serine proteases like MASPs (Endo et al., 2010). Weak adjacent sites of the MASP binding domain may enhance or decrease affinity for binding, but little is known about the biological role of this affinity modulation. The aim was to alter the biological activity of ficolin-B by introduction of a single amino acid mutation in the collagen like domain. Protein biochemical and chromatographic studies were performed to compare the ficolin-B wild type and mutant forms." @default.
• W100306963 created "2016-06-24" @default.
• W100306963 creator A5039834954 @default.
• W100306963 date "2011-11-16" @default.
• W100306963 modified "2023-09-27" @default.
• W100306963 title "Biochemical and functional studies on mouse ficolin-B, a novel pattern recognition molecule of the innate immune system" @default.
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