A Novel Xylosylphosphotransferase Activity Discovered in Cryptococcus neoformans*

  1. Tamara L. Doering‡,2
  1. From the ‡Department of Molecular Microbiology, Washington University School of Medicine, St. Louis, Missouri 63110,
  2. the §Department of Cellular and Molecular Medicine, University of Copenhagen, 2200 Copenhagen N, Denmark,
  3. the Department of Chemistry, University of New Hampshire, Durham, New Hampshire 03824, and
  4. the ‖Department of Pathology, University of Iowa Carver College of Medicine and Pathology and Laboratory Medicine, Veterans Affairs Medical Center, Iowa City, Iowa 52246
  1. ↵2 To whom correspondence should be addressed: Dept. of Molecular Microbiology, Washington University School of Medicine, 660 South Euclid Ave., Campus Box 8230, St. Louis, MO 63110-1093. Tel.: 314-747-5597; Fax: 314-362-1232; E-mail: doering{at}wustl.edu.

Abstract

Cryptococcus neoformans is a fungal pathogen that causes serious disease in immunocompromised individuals. The organism produces a distinctive polysaccharide capsule that is necessary for its virulence, a predominantly polysaccharide cell wall, and a variety of protein- and lipid-linked glycans. The glycan synthetic pathways of this pathogen are of great interest. Here we report the detection of a novel glycosylphosphotransferase activity in C. neoformans, identification of the corresponding gene, and characterization of the encoded protein. The observed activity is specific for UDP-xylose as a donor and for mannose acceptors and forms a xylose-α-1-phosphate-6-mannose linkage. This is the first report of a xylosylphosphotransferase activity in any system.

Footnotes

  • ↵1 Supported by the Danish Medical Research Council for Technology and Innovation, the Stjerne Program of Excellence, and the Copenhagen Center for Glycomics.

  • ↵* This work was supported, in whole or in part, by National Institutes of Health Grant RO1 GM071007 (in support of the studies of cryptococcal glycan synthesis in the Doering laboratory).

  • ↵Graphic The on-line version of this article (available at http://www.jbc.org) contains supplemental Table 1 and Fig. 1.

  • The nucleotide sequence(s) reported in this paper has been submitted to the Gen-BankTM/EBI Data Bank with accession number(s) GQ403790.

  • Received August 14, 2009.
  • Revision received October 27, 2009.
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  1. First Published on October 28, 2009 doi: 10.1074/jbc.M109.056226 The Journal of Biological Chemistry 284, 36118-36127.
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