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

Research output not available from this repository, contact author.

Request Changes to record.

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:	Date Event 30 June 2008 Published
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

Request changes or add full text files to a record

Repository staff actions (login required)

View Item