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Glycobiology Advance Access published online on March 24, 2004
Glycobiology, doi:10.1093/glycob/cwh064
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Submitted on November 20, 2003
Revised on January 28, 2004
Accepted on February 16, 2004

© 2004 Glycobiology © Oxford University Press 2004; all rights reserved.

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Surface-layer glycoproteins: an example for the diversity of bacterial glycosylation with promising impacts on nanobiotechnology

Christina Schäffer 1 and Paul Messner 1*

1 Center for NanoBiotechnology, University of Applied Life Sciences and Natural Resources, Gregor-Mendel-Strasse 33, A-1180 Wien, Austria

* To whom correspondence should be addressed. E-mail: paul.messner{at}boku.ac.at.

Abstract

Bacterial cell surface layers, referred to simply as S-layers, have been described for all major phylogenetic groups of bacteria, which may indicate their pivotal role for a bacterium in its natural habitat. They have the unique ability to assemble into two dimensional, crystalline arrays, which completely cover the bacterial cells. Glycosylation represents the most frequent modification of S-layer proteins. S-layer glycoproteins constitute a class of glycoconjugates first isolated in the mid 1970ies, but S-layer glycoprotein research, is still being regarded an "exotic field of glycobiology", possibly because of its "non-eukaryotic" character. Extensive work during the past 30 years provided evidence of an enormous diversity of S-layer glycoproteins that have been created in nature over three billion years of prokaryotic evolution. These glycoconjugates are substantially different from eukaryotic glycoproteins, with regard to both, composition and structure; nevertheless some general structural concepts may be deduced. The awareness of the high application potential of S-layer glycoproteins, especially in combination with their intrinsic cell surface display feature, in the field of modern nanobiotechnology as a base for glycoengineering has recently led to the investigation of the S-layer protein glycosylation process at the molecular level, which has lagged behind the structural studies due to the lack of suitable molecular tools. From that work an even more interesting picture of this class of glycoconjugates is emerging. The availability of purified enzymes from S-layer glycan biosynthesis pathways exhibiting increased stabilities and/or rare sugar specificities in conjunction with preliminary genomic data on S-layer glycan biosynthesis clusters will pave the way for the rational design of S-layer neoglycoproteins.


Bacterial glycosylation, glycan diversity, glycoengineering, genomic glycosylation loci, S-layer nanoglycobiology
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