Document Detail


Distribution of sialic acids on mucins and gels: a defense mechanism.
MedLine Citation:
PMID:  22225812     Owner:  NLM     Status:  In-Data-Review    
Abstract/OtherAbstract:
Moist mucosal epithelial interfaces that are exposed to external environments are dominated by sugar epitopes, some of which (e.g., sialic acids) are involved in host defense. In this study, we determined the abundance and distribution of two sialic acids to assess differences in their availability to an exogenous probe in isolated mucins and mucous gels. We used atomic force microscopy to obtain force maps of human preocular mucous and purified ocular mucins by probing and locating the interactions between tip-tethered lectins Maackia amurensis and Sambucus nigra and their respective receptors, α-2,3 and α-2,6 N-acetylneuraminic (sialic) acids. The rupture force distributions were not affected by neighboring sugar-bearing molecules. Energy contours for both lectin-sugar bonds were fitted to a two-barrier model, suggesting a conformational change before dissociation. In contrast to data from purified mucin molecules, the preocular gels presented numerous large clusters (19,000 ± 4000 nm(2)) of α-2,6 sialic acids, but very few small clusters (2000 ± 500 nm(2)) of α-2,3 epitopes. This indicates that mucins, which are rich in α-2,3 sialic acids, are only partially exposed at the surface of the mucous gel. Microorganisms that recognize α-2,3 sialic acids will encounter only isolated ligands, and the adhesion of other microorganisms will be enhanced by large islands of neighboring α-2,6 sialic acids. We have unveiled an additional level of mucosal surface heterogeneity, specifically in the distribution of pro- and antiadhesive sialic acids that protect underlying epithelia from viruses and bacteria.
Authors:
S C Baos; D B Phillips; L Wildling; T J McMaster; M Berry
Publication Detail:
Type:  Journal Article     Date:  2012-01-03
Journal Detail:
Title:  Biophysical journal     Volume:  102     ISSN:  1542-0086     ISO Abbreviation:  Biophys. J.     Publication Date:  2012 Jan 
Date Detail:
Created Date:  2012-01-09     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0370626     Medline TA:  Biophys J     Country:  United States    
Other Details:
Languages:  eng     Pagination:  176-84     Citation Subset:  IM    
Copyright Information:
Copyright © 2012 Biophysical Society. Published by Elsevier Inc. All rights reserved.
Affiliation:
Academic Unit of Ophthalmology, Bristol Eye Hospital, University of Bristol, Bristol, United Kingdom; H. H. Wills Physics Laboratory, University of Bristol, Bristol, United Kingdom.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  ?-? Cross-Links Increase Fibrin Fiber Elasticity and Stiffness.
Next Document:  Direct measurement of the mechanical properties of lipid phases in supported bilayers.