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Pulse-chase Analysis of N-linked Sugar Chains from Glycoproteins in Mammalian Cells

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N Strömberg¹, P G Nyholm, I Pascher

¹Department of Cariology, Faculty of Odontology, University of Göteborg, Sweden.

Proceedings of the National Academy of Sciences of the United States of America

|October 15, 1991

Summary

Three P-pilus-associated G-adhesins bind differently to erythrocyte membranes based on globo-series glycosphingolipid (GSL) composition. Specific G-adhesin variants target distinct GSLs, influencing erythrocyte agglutination.

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Area of Science:

Microbiology
Biochemistry
Structural Biology

Background:

P-pilus-associated G-adhesins are lectins mediating bacterial adhesion.
Allelic variants of G-adhesins exhibit distinct cell-binding properties.
Glycosphingolipids (GSLs) on erythrocyte membranes are key determinants of host-pathogen interactions.

Purpose of the Study:

To analyze the erythrocyte agglutination properties of three G-adhesin variants.
To correlate G-adhesin binding specificity with erythrocyte glycosphingolipid composition.
To investigate the structural basis for differential G-adhesin-GSL interactions.

Main Methods:

Expression of recombinant G-adhesin variants in Escherichia coli HB101.
Erythrocyte agglutination assays using erythrocytes from various species.
Analysis of glycosphingolipid composition in erythrocyte membranes.
Molecular modeling of globo-series GSLs and their interaction with G-adhesins.

Main Results:

All three G-adhesin variants showed specificity for globo-series GSLs on artificial surfaces.
PapGJ96 agglutinated erythrocytes with globotriaosylceramide (GbO3).
PapGAD110 strongly agglutinated erythrocytes with globotetraosylceramide (GbO4).
PrsGJ96 agglutinated erythrocytes with globopentaosylceramide (GbO5).
Molecular modeling revealed distinct orientations of GSLs on the membrane surface.

Conclusions:

Differential binding of G-adhesin variants to erythrocytes is mediated by specific globo-series GSLs.
The distinct specificities arise from differences in epitope presentation of GSLs at the membrane surface.
Understanding these interactions is crucial for deciphering bacterial adhesion mechanisms.