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Université de Fribourg

Heligmosomoides polygyrus venom allergen-like protein-4 (HpVAL-4) is a sterol binding protein

Asojo, Oluwatoyin A. ; Darwich, Rabih ; Gebremedhin, Selam ; Smant, Geert ; Lozano-Torres, José L. ; Drurey, Claire ; Pollet, Jeroen ; Maizels, Rick M. ; Schneiter, Roger ; Wilbers, Ruud H. P.

In: International Journal for Parasitology, 2018, vol. 48, no. 5, p. 359–369

Heligmosomoides polygyrus bakeri is a model parasitic hookworm used to study animal and human helminth diseases. During infection, the parasite releases excretory/secretory products that modulate the immune system of the host. The most abundant protein family in excretory/secretory products comprises the venom allergen-like proteins (VALs), which are members of the SCP/TAPS (sperm-coating ...

Université de Fribourg

Localization and functional characterization of the pathogenesis-related proteins Rbe1p and Rbt4p in Candida albicans

Bantel, Annick ; Darwiche, Rabih ; Rupp, Steffen ; Schneiter, Roger ; Sohn, Kai

In: PLOS ONE, 2018, vol. 13, no. 8, p. e0201932

Members of the Cysteine-rich secretory protein, Antigen 5 and Pathogenesis-related 1 (CAP) protein superfamily are important virulence factors in fungi but remain poorly characterized on molecular level. Here, we investigate the cellular localization and molecular function of Rbe1p and Rbt4p, two CAP family members from the human pathogen Candida albicans. We unexpectedly found that Rbe1p...

Université de Fribourg

Crystal structure of MpPR-1i, a SCP/TAPS protein from Moniliophthora perniciosa , the fungus that causes witches’ broom disease of cacao

Baroni, Renata M. ; Luo, Zhipu ; Darwiche, Rabih ; Hudspeth, Elissa M. ; Schneiter, Roger ; Pereira, Gonçalo A. G. ; Mondego, Jorge M. C. ; Asojo, Oluwatoyin A.

In: Scientific Reports, 2017, vol. 7, no. 1, p. 7818

The pathogenic fungi Moniliophthora perniciosa causes Witches’ Broom Disease (WBD) of cacao. The structure of MpPR-1i, a protein expressed by M. perniciosa when it infects cacao, are presented. This is the first reported de novo structure determined by single-wavelength anomalous dispersion phasing upon soaking with selenourea. Each monomer has flexible loop regions linking the core...

Université de Fribourg

Architecture of lipid droplets in endoplasmic reticulum is determined by phospholipid intrinsic curvature

Choudhary, Vineet ; Golani, Gonen ; Joshi, Amit S. ; Cottier, Stéphanie ; Schneiter, Roger ; Prinz, William A. ; Kozlov, Michael M.

In: Current Biology, 2018, vol. 28, no. 6, p. 915-926.e9

Lipid droplets (LDs) store fats and play critical roles in lipid and energy homeostasis. They form between the leaflets of the endoplasmic reticulum (ER) membrane and consist of a neutral lipid core wrapped in a phospholipid monolayer with proteins. Two types of ER-LD architecture are thought to exist and be essential for LD functioning. Maturing LDs either emerge from the ER into the...

Université de Fribourg

Seipin and Nem1 establish discrete ER subdomains to initiate yeast lipid droplet biogenesis

Choudhary, Vineet ; El Atab, Ola ; Mizzon, Giulia ; Prinz, William A. ; Schneiter, Roger

In: Journal of Cell Biology, 2020, vol. 219, no. 7, p. -

Lipid droplets (LDs) are fat storage organelles that originate from the endoplasmic reticulum (ER). Relatively little is known about how sites of LD formation are selected and which proteins/lipids are necessary for the process. Here, we show that LDs induced by the yeast triacylglycerol (TAG)-synthases Lro1 and Dga1 are formed at discrete ER subdomains defined by seipin (Fld1), and a...

Université de Fribourg

Lipid droplet biogenesis from specialized ER subdomains

Choudhary, Vineet ; Schneiter, Roger

In: Microbial Cell, 2020, vol. 7, no. 8, p. 218–221

Lipid droplets (LDs) are cellular compartments dedicated to the storage of metabolic energy in the form of neutral lipids, commonly known as “fat”. The biogenesis of LDs takes place in the endoplasmic reticulum (ER), but its spatial and temporal organization is poorly understood. How exactly sites of LD formation are selected and the succession of proteins and lipids needed to mediate...

Université de Fribourg

The caveolin-binding motif of the pathogen-related yeast protein Pry1, a member of the CAP protein superfamily, is required for in vivo export of cholesteryl acetate

Choudhary, Vineet ; Darwiche, Rabih ; Gfeller, David ; Zoete, Vincent ; Michielin, Olivier ; Schneiter, Roger

In: Journal of Lipid Research, 2014, vol. 55, no. 5, p. 883-894

Proteins belonging to the CAP superfamily are present in all kingdoms of life and have been implicated in different physiological processes. Their molecular mode of action, however, is poorly understood. Saccharomyces cerevisiae expresses three members of this superfamily, pathogen-related yeast (Pry)1, -2, and -3. We have recently shown that Pry function is required for the secretion of...

Université de Fribourg

Pathogen-Related Yeast (PRY) proteins and members of the CAP superfamily are secreted sterol-binding proteins

Choudhary, Vineet ; Schneiter, Roger

In: Proceedings of the National Academy of Sciences of the United States of America - PNAS, 2012, vol. 109, no. 42, p. 16882-16887

Sterols and related membrane-perturbing agents are subject to a quality control cycle. Compounds that fail to pass this control are acetylated and secreted into the culture media, whereas lipids that pass the cycle are deacetylated and retained within the cell. Here we describe the identification of a family of conserved proteins, the Pathogen-Related Yeast (PRY) proteins, as a class of...

Université de Fribourg

Monitoring sterol uptake, acetylation, and export in yeast

Choudhary, Vineet ; Schneiter, Roger

In: Methods in Molecular Biology, 2009, vol. 580, p. 221-232

Sterols are essential lipid components of eukaryotic membranes. They are synthesized in the endoplasmatic reticulum (ER) from where they are efficiently transported to the plasma membrane, which harbors ~90% of the free sterol pool of the cell. The molecular mechanisms that govern this lipid transport, however, are not well characterized and are challenging to analyze. Saccharomyces cerevisiae...

Université de Fribourg

The yeast cell wall protein Pry3 inhibits mating through highly conserved residues within the CAP domain

Cottier, Stéphanie ; Darwiche, Rabih ; Meyenhofer, Felix ; Debelyy, Mykhaylo O. ; Schneiter, Roger

In: Biology Open, 2020, vol. 9, no. 6, p. bio053470

Members of the CAP/SCP/TAPS superfamily have been implicated in many different physiological processes, including pathogen defense, sperm maturation and fertilization. The mode of action of this class of proteins, however, remains poorly understood. The genome of Saccharomyces cerevisiae encodes three CAP superfamily members, Pry1-3. We have previously shown that Pry1 function is required...