Recognition of acetylated oligosaccharides by human L-ficolin
نویسندگان
چکیده
منابع مشابه
Human L-Ficolin (Ficolin-2) and Its Clinical Significance
Human L-ficolin (P35, ficolin-2) is synthesised in the liver and secreted into the bloodstream where it is one of the major pattern recognition molecules of plasma/serum. Like other ficolins, it consists of a collagen-like tail region linked to a fibrinogen-related globular head; a basic triplet subunit arises via a collagen-like triple helix, and this then forms higher multimers (typically a 1...
متن کاملHuman L-ficolin recognizes phosphocholine moieties of pneumococcal teichoic acid.
Human L-ficolin is a soluble protein of the innate immune system able to sense pathogens through its fibrinogen (FBG) recognition domains and to trigger activation of the lectin complement pathway through associated serine proteases. L-Ficolin has been previously shown to recognize pneumococcal clinical isolates, but its ligands and especially its molecular specificity remain to be identified. ...
متن کاملCarbohydrate recognition and complement activation by rat ficolin-B
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 le...
متن کاملOligosaccharides in molecular recognition.
The development, organization and growth of complex organisms as well as their interactions with the environment involve an intricate array of molecular recognition events. There is an increased awareness of the involvement of oligosaccharides in many of these processes. In this article, studies of oligosaccharide antigenicity, and the way these have been interpreted with respect to oligosaccha...
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ژورنال
عنوان ژورنال: Immunology Letters
سال: 2008
ISSN: 0165-2478
DOI: 10.1016/j.imlet.2008.03.014