Open AccessCharacterization of surface saccharides in two Corynebacterium diphtheriae strains
Author(s) -
MattosGuaraldi A.L.,
Cappelli E.A.,
Previato J.O.,
Formiga L.C.D.,
Andrade A.F.B.
Publication year - 1999
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1999.tb13369.x
Subject(s) - sialic acid , biochemistry , corynebacterium diphtheriae , lectin , chemistry , melibiose , sucrose , raffinose , biology , diphtheria , vaccination , immunology
Two Corynebacterium diphtheriae strains were analyzed by assays employing a battery of highly purified fluorescent lectins. From 22 lectins tested only seven with affinity to receptor molecules containing N ‐acetylglucosamine ( d ‐GlcNAc), N ‐acetylgalactosamine ( d ‐GalNAc), galactose ( d ‐Gal), mannose‐like ( d ‐Man‐like) and sialic acid residues showed positive fluorescent labeling. A higher reactivity of Triticum vulgaris (WGA), which binds to sialic acid and/or β‐ d ‐GlcNAc‐containing residues, and Bandeiraea simplicifolia II (BS‐II), which recognizes α and β‐ d ‐GlcNAc units, was shown by the sucrose‐ fermenting strain. Ricinus communis (RCA‐I), which recognizes d ‐Gal units in addition to both Glycine max (SBA) and Artocarpus integrifolia (Jacaline) agglutinins that bind to d ‐GalNAc‐containing residues, reacted preferentially with the sucrose‐negative strain. Canavalia ensiformis (Con A), which recognizes d ‐Man‐like receptors, reacted with both sucrose‐fermenting and non‐sucrose‐fermenting C. diphtheriae biotypes. However, higher interaction was observed with the non‐sucrose‐fermenting strain. Fluorescence of WGA binding was significantly decreased by neuraminidase treatment suggesting the presence of an exposed sialic acid moiety on C. diphtheriae surfaces. Binding assay using radiolabeled [ 125 I]WGA essentially confirmed the lectin fluorescence studies. N ‐Acetylneuraminic acid moieties were detected in whole cell hydrolysates as assessed by thin‐layer and gas‐liquid chromatography. The data indicate differences on the cell surface saccharide ligands between the sucrose‐fermenting and the non‐sucrose‐fermenting C. diphtheriae strains.