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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

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Official URL: http://dx.doi.org/10.1016/j.imlet.2008.03.014

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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 Medicine > Warwick Medical School > Biomedical Sciences > Translational & Experimental Medicine > Metabolic and Vascular Health (- until July 2016)
Faculty of Medicine > Warwick Medical School
Journal or Publication Title: Immunology Letters
Publisher: Elsevier BV
ISSN: 0165-2478
Official Date: 30 June 2008
Dates:
DateEvent
30 June 2008Published
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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