FUKUSHIMA JOURNAL OF MEDICAL SCIENCE
Online ISSN : 2185-4610
Print ISSN : 0016-2590
ISSN-L : 0016-2590
Regular Papers
OPSONIC FUNCTION AND CONCENTRATION OF HUMAN SERUM FICOLIN/P35
SATOSHI TAIRANAMIO KODAMAMISAO MATSUSHITATEIZO FUJITA
Author information
JOURNAL FREE ACCESS

2000 Volume 46 Issue 1-2 Pages 13-23

Details
Abstract

Collectins, C-type (Ca2+-dependent) animallectins with both collagenous and carbohydrate recognition domains, function as opsonins against pathogens. We previously described an N-cetylglucosamine (GlcNAc)-binding lectin (ficolin/P35) with a collagen- and a fibrinogen-like sequence present in human serum. In this report we show that ficolin/P35 can serve as an opsonin and enhance the clearance of pathogens having surface GlcNAc. Ficolin/P35 bound to an Ra chemotype strain of Salmonella typhimurium (TV119) which has an exposed GlcNAc at the non-reducing termini of the polysaccharide. On the other hand, ficolin/P35 did not bind to LT2, a smooth type strain of S. typhimurium with additional O-polysaccharides covering GlcNAc. Ficolin/P35 enhanced the uptake of TV119 by monocytes or polymorphonuclear leukocytes but had no opsonic activity towards LT2. These results suggest that, like collectins, ficolin/P35 is a collagenous lectin which has a role in innate immunity against certain pathogenic organisms by acting as an opsonin.
We prepared monoclonal antibodies against ficolin/P35 and developed an enzyme-linked immunosorbent assay (ELISA) for measuring ficolin/P35 concentrations in humans. The mean serum concentration of ficolin/P35 from 130 normal individuals was estimated to be 13.7 μg/ml.

Content from these authors
© 2000 The Fukushima Society of Medical Science
Previous article Next article
feedback
Top