Suvarna K, Bartiss A, Wong B; American Society for Microbiology. General Meeting.
Abstr Gen Meet Am Soc Microbiol. 1999 May 30-Jun 3; 99: 299 (abstract no. F-20).
Yale University, West Haven, CT.
Cryptococcus neoformans produces large amounts of the acyclic polyol mannitol in culture and in infected mammalian hosts. Earlier studies linked mannitol synthesis by C. neoformans with tolerance to heat, osmotic, and oxidative stresses, and with virulence in mice. Mannitol-l-phopshate dehydrogenase (MPD) has been shown to be the key step in mannitol biosynthesis in other fungi. In this study, we purified MPD from C. neoformans 1000 fold. The enzyme catalyzed NAD dependent oxidation of mannitol-1-phosphate to fructose-6-phosphate, its molecular weight was 148 kDa, and it contained four identical 36 kDa subunits. Amino acid sequence of tryptic peptides were used to synthesize degenerate primers. These primers were used to generate a hybridization probe by PCR. The probe was used to clone the full-length MPD cDNA which contained a 1083 bp ORF encoding a peptide of 361 amino acids that showed homology to medium chain alcohol/polyol dehydrogenases.
Publication Types:
Keywords:
- Amino Acid Sequence
- Animals
- Antigens, Fungal
- Cloning, Molecular
- Cryptococcosis
- Cryptococcus neoformans
- DNA, Complementary
- L-Iditol 2-Dehydrogenase
- Mannitol
- Mannitol Dehydrogenases
- Mannitol Phosphates
- Mice
- Sugar Alcohol Dehydrogenases
- Virulence
- immunology
- isolation & purification
- mannitol-1-phosphate
- mannitol-1-phosphate dehydrogenase
Other ID:
UI: 102195648
From Meeting Abstracts