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Recognition of acetylated oligosaccharides by human L-ficolin
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Krarup, Anders, Mitchell, Daniel A. and Sim, Robert B. (2008) Recognition of acetylated oligosaccharides by human L-ficolin. Immunology Letters, Vol.118 (No.2). pp. 152-156. doi:10.1016/j.imlet.2008.03.014 ISSN 0165-2478.
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Official URL: http://dx.doi.org/10.1016/j.imlet.2008.03.014
Abstract
The complement system is a protein cascade capable of neutralizing invading pathogens. One of its activation pathways is the lectin pathway which is dependent on the binding of MBL or the ficolins. The specificity of L-ficolin binding has been investigated previously and it was observed that binding is dependent on acetyl groups. If this was the only requirement this would enable L-ficolin to bind to most mammalian glycosylations since they contain acetylated monosaccharides. To investigate this further L-ficolin was subjected to glycan-array analysis in which L-ficolin binding to 279 different glycans was investigated. Few of these bound L-ficolin above background level but clear structural requirements were discovered. (c) 2008 Elsevier B.V. All rights reserved.
| Item Type: | Journal Article | ||||
|---|---|---|---|---|---|
| Subjects: | Q Science > QR Microbiology > QR180 Immunology | ||||
| Divisions: | Faculty of Science, Engineering and Medicine > Medicine > Warwick Medical School > Biomedical Sciences > Translational & Experimental Medicine > Metabolic and Vascular Health (- until July 2016) Faculty of Science, Engineering and Medicine > Medicine > Warwick Medical School |
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| Journal or Publication Title: | Immunology Letters | ||||
| Publisher: | Elsevier BV | ||||
| ISSN: | 0165-2478 | ||||
| Official Date: | 30 June 2008 | ||||
| Dates: |
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| Volume: | Vol.118 | ||||
| Number: | No.2 | ||||
| Number of Pages: | 5 | ||||
| Page Range: | pp. 152-156 | ||||
| DOI: | 10.1016/j.imlet.2008.03.014 | ||||
| Status: | Peer Reviewed | ||||
| Publication Status: | Published | ||||
| Access rights to Published version: | Restricted or Subscription Access |
Data sourced from Thomson Reuters' Web of Knowledge
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