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J. Biol. Chem., Vol. 279, Issue 39, 40737-40747, September 24, 2004

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Expression of Transglutaminase Substrate Activity on Candida albicans Germ Tubes through a Coiled, Disulfide-bonded N-terminal Domain of Hwp1 Requires C-terminal Glycosylphosphatidylinositol Modification^*

Janet F. Staab, Yong-Sun Bahn¶, Chia-Hui Tai||**, Paul F. Cook||, and Paula Sundstrom

From the Departments of Molecular Virology, Immunology, and Medical Genetics and Microbiology, The Ohio State University, Columbus, Ohio 43201 and the ^||Department of Chemistry and Biochemistry, University of Oklahoma, Norman, Oklahoma, 73019

By serving as a microbial substrate for epithelial cell transglutaminase, Hwp1 (Hyphal wall protein 1) of Candida albicans participates in cross-links with proteins on the mammalian mucosa. Biophysical properties of the transglutaminase substrate domain were explored using a recombinant protein representative of the N-terminal domain of Hwp1 and were similar to other transglutaminase substrates, the small proline-rich proteins of cornified envelopes found in stratified squamous epithelia. Recombinant Hwp1 lacks and structures by circular dichroism and likely exists as a disulfide-cross-linked coiled-coil. The transglutaminase substrate property prompted a unique approach for investigating the features of surface Hwp1 on germ tubes. A lysine analog, 5-(biotinamido)pentylamine, was cross-linked to germ tubes catalyzed by transglutaminase 2 prior to cell fractionation, immunoprecipitation, and detection with streptavidin conjugates. The majority of the transglutaminase-modifiable Hwp1 was covalently attached to the -glucan of hyphae by the C terminus of Hwp1 via a glycosylphosphatidylinositol remnant anchor. A putative precursor of cell wall forms of Hwp1 was identified in the cell extract and in the culture medium. Hwp1 was modified by relatively short N-linked glycans, and the molecular size of the protein was reduced by hypomannosylation when expressed in O-glycosylation mutant strains. Hwp1 combines features of mammalian transglutaminase substrate proteins with characteristics of fungal cell wall proteins to form an unconventional adhesin at the hyphal wall of C. albicans.

Received for publication, May 28, 2004 , and in revised form, July 12, 2004.

^* This work was supported by Grant DE 011375 (to P. S.) from the National Institutes of Health and Grant MCB 9729609 (to P. F. C.) from the National Science Foundation, and funds from the Grayce B. Kerr Endowment to the University of Oklahoma (to P. F. C.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains a supplemental figure.

Present address: Seattle Biomedical Research Institute, 307 West-lake Ave. N., Ste. 500, Seattle, WA 98109-5219.

^¶ Present address: Depts. of Molecular Genetics and Microbiology, Duke University Medical Center, 315 CARL Bldg., Research Dr., Durham, NC 27710.

^** Present address: ChengShiu Institute of Technology, Dept. of Chemical Engineering, 840 Cheng-Ching Road, Neausong Shiang, Kaohsiung, Taiwan, ROC.

To whom correspondence should be addressed: Dartmouth Medical School, Dept. of Microbiology and Immunology, Vail Bldg. HB7550, Hanover, NH 03755. Tel.: 603-650-1629; Fax: 603-650-1318, E-mail: Paula.Sundstrom{at}Dartmouth.edu.

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