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Glycosyltransferases and their products: cryptococcal variations on fungal themes

Journal

FEMS YEAST RESEARCH
Volume 6, Issue 4, Pages 499-512

Publisher

OXFORD UNIV PRESS
DOI: 10.1111/j.1567-1364.2006.00054.x

Keywords

glycosyltransferase; glycosylation; glycan; polysaccharide; fungi; Cryptococcus

Funding

  1. NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM066303, F32GM072341, R01GM071007] Funding Source: NIH RePORTER
  2. NIGMS NIH HHS [R01 GM066303, R01 GM071007, F32 GM072341, R01 GM66303, R01 GM71007] Funding Source: Medline

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Glycosyltransferases are specific enzymes that catalyse the transfer of monosaccharide moieties to biological substrates, including proteins, lipids and carbohydrates. These enzymes are present from prokaryotes to humans, and their glycoconjugate products are often vital for survival of the organism. Many glycosyltransferases found in fungal pathogens such as Cryptococcus neoformans do not exist in mammalian systems, making them attractive potential targets for selectively toxic agents. In this article, we present the features of this diverse class of enzymes, and review the fungal glycosyltransferases that are involved in synthesis of the cell wall, the cryptococcal capsule, glycoproteins and glycolipids. We specifically focus on enzymes that have been identified or studied in C. neoformans, and we consider future directions for research on glycosyltransferases in the context of this opportunistic pathogen.

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