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Infection and Immunity, July 2000, p. 3894-3899, Vol. 68, No. 7
Immunobiology Unit, Institute of Child
Health, London WC1N 1EH,1 and Department
of Infectious Diseases and Microbiology, Imperial College School of
Medicine, St. Mary's Campus, London W2 1PG,2
United Kingdom
Received 27 January 2000/Returned for modification 13 March
2000/Accepted 6 April 2000
Mannose-binding lectin (MBL) is an important component of the
innate immune system. It binds to the arrays of sugars commonly presented by microorganisms and activates the complement system independently of antibody. Despite detailed knowledge of the
stereochemical basis of MBL binding, relatively little is known about
how bacterial surface structures influence binding of the lectin. Using
flow cytometry, we have measured the binding of MBL to a range of
mutants of Salmonella enterica serovar Typhimurium and
Neisseria gonorrhoeae which differ in the structure of
expressed lipopolysaccharide (LPS). For both organisms, the possession
of core LPS structures led to avid binding of MBL, which was abrogated
by the addition of O antigen (Salmonella serovar
Typhimurium) or sialic acid (N. gonorrhoeae). Truncation of
the LPS within the core led to lower levels of MBL binding. It was not
possible to predict the magnitude of MBL binding from the identity of
the LPS terminal sugar alone, indicating that the three-dimensional
disposition of LPS molecules is probably also of importance in
determining MBL attachment. These results further support the
hypothesis that LPS structure is a major determinant of MBL binding.
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
The Lipopolysaccharide Structures of Salmonella
enterica Serovar Typhimurium and Neisseria gonorrhoeae
Determine the Attachment of Human Mannose-Binding Lectin to
Intact Organisms
*
Corresponding author. Present address: Division of
Molecular and Genetic Medicine, F Floor, University of Sheffield
Medical School, Beech Hill Road, Sheffield S10 2RX, United Kingdom.
Phone: 44 (0114) 271 2968. Fax: 44 (0114) 273 9926. E-mail:
D.L.Jack{at}sheffield.ac.uk.
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