Phenotypic landscape of a fungal meningitis pathogen reveals its unique biology.

is the most common cause of fungal meningitis and the top-ranked W.H.O.

Correction to: Cloning and Expression of Heterologous Cellulases and Enzymes in Aspergillus niger.

The author's family name were incorrectly published in the original version. This has been corrected to read as.

Cloning and Expression of Heterologous Cellulases and Enzymes in Aspergillus niger.

Cellulases and other enzymes are needed for saccharification of plant biomass in the biorefinery industry. Expression, characterization, and eventual large-scale production of known and novel cellulases requires the ability to express and secrete heterologous enzymes in relevant protein production platforms like Aspergillus niger. A method for cloning and expression of genes for these desirable enzymes in A.

Functional genomics of lipid metabolism in the oleaginous yeast .

The basidiomycete yeast (also known as ) accumulates high concentrations of lipids and carotenoids from diverse carbon sources. It has great potential as a model for the cellular biology of lipid droplets and for sustainable chemical production. We developed a method for high-throughput genetics (RB-TDNAseq), using sequence-barcoded T-DNA insertions.

Forward genetics screen coupled with whole-genome resequencing identifies novel gene targets for improving heterologous enzyme production in Aspergillus niger.

Plant biomass, once reduced to its composite sugars, can be converted to fuel substitutes. One means of overcoming the recalcitrance of lignocellulose is pretreatment followed by enzymatic hydrolysis. However, currently available commercial enzyme cocktails are inhibited in the presence of residual pretreatment chemicals.

Deletion of homologs of the SREBP pathway results in hyper-production of cellulases in Neurospora crassa and Trichoderma reesei.

Background: The filamentous fungus Neurospora crassa efficiently utilizes plant biomass and is a model organism for genetic, molecular and cellular biology studies. Here, a set of 567 single-gene deletion strains was assessed for cellulolytic activity as compared to the wild-type parental strain. Mutant strains included were those carrying a deletion in: (1) genes encoding proteins homologous to those implicated in the Saccharomyces cerevisiae secretion apparatus; (2) genes that are homologous to those known to differ between the Trichoderma reesei hyper-secreting strain RUT-C30 and its ancestral wild-type strain; (3) genes encoding proteins identified in the secretome of N.

A xylosylphosphotransferase of Cryptococcus neoformans acts in protein O-glycan synthesis.

Cryptococcal meningoencephalitis is an AIDS-defining illness caused by the opportunistic pathogen Cryptococcus neoformans. This organism possesses an elaborate polysaccharide capsule that is unique among pathogenic fungi, and the glycobiology of C. neoformans has been a focus of research in the field.

A novel xylosylphosphotransferase activity discovered in Cryptococcus neoformans.

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.

Glycosyltransferases and their products: cryptococcal variations on fungal themes.

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.