Interaction of lectins with Neisseria gonorrhoeae.

Abstract:

:Fifty-four strains of Neisseria gonorrhoeae were examined for their ability to be agglutinated by various lectins. Wheat germ agglutinin, ricin, soybean lectin, and peanut agglutinin agglutinated all strains tested. Dolichos biflorus, Sophora japonica, Maclura pomifera, Ulex Europaeus, Lens culinaris, Canavalia ensiformis, Phaseolus lunatus, and Bandeiraea simplicifolia BS I and BS II lectins either failed to agglutinate or agglutinated some strains but not others. Agglutination of gonococci by wheat germ agglutinin, ricin, and soybean lectin is sugar specific and most effectively inhibited by ligands known to interact with lectin combining sites. Lectin reactive groupings appear to be independent of antigenic determinants conferring Gc serogroup specificity. Interactions with wheat germ agglutinin and ricin suggest the occurrence of multiple beta-linked N-acetyl-D-glucosamine (D-GlcNAc) and beta-D-galactosyl (beta-D-Gal) units as common structural features of gonococcal cell envelope polysaccharide. Interactions with soybean agglutinin, peanut agglutinin, and Dolichos biflorus lectins suggest that alpha-N-acetyl-D-galactosamine (alpha-D-GalNAc) units and beta-D-Gal linked to GalNAc and (or) GlcNAc may also occur as structural features of the polysaccharide components of the cell envelope of some gonococci.

journal_name

Can J Microbiol

authors

Allen PZ,Connelly MC,Apicella MA

doi

10.1139/m80-078

subject

Has Abstract

pub_date

1980-04-01 00:00:00

pages

468-74

issue

4

eissn

0008-4166

issn

1480-3275

journal_volume

26

pub_type

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