C-terminal modification and cell wall association of Cryptococcus neoformans laccase

CHED 787

Jennifer K. Inlow, inlow@carbon.indstate.edu and Amanda Melberg, amelberg@mymail.indstate.edu. Department of Chemistry, Indiana State University, Terre Haute, IN 47809
Cryptococcus neoformans is a fungal pathogen that can infect the lungs of immuno-compromised individuals. Expression of the oxidoreductase laccase by this yeast contributes to its virulence. In most fungi laccase is extracellular and is excreted into the surrounding environment. However, Cryptococcus laccase has been shown to associate with the outer region of the yeast cell wall. The means of cell wall association is unknown, but experimental work has shown it is likely due to some feature of the extreme C-terminus of the enzyme. Our database searches and sequence alignments of fungal laccases indicate that Cryptoccus laccase is unique in that its C-terminal region is longer than that of others. To determine the means by which Cryptococcus laccase associates with the cell wall, we used bioinformatics algorithms to analyze the C-terminal sequence for potential GPI-anchor attachment sites and glycosylation sites. Cryptococcus laccase contains potential O-linked glycosylation sites not present in the C-terminal sequences of other fungal laccases.