Vaccine Immunotherapy for Celiac Disease.

Autoimmune and allergic disorders are highly prevalent conditions in which an altered or abnormal immune response is mounted against self- or environmental antigens, respectively. Antigen-based immunotherapy is a therapeutic option aimed at restoring the specific immune tolerance toward pathogenic antigens while leaving the rest of the immune system unaffected. This strategy proved efficacy especially in allergic diseases, including asthma, allergic rhinitis, and food allergies, but still has shortcomings for the treatment of autoimmune diseases.

Sphingolipid metabolic flow controls phosphoinositide turnover at the -Golgi network.

Sphingolipids are membrane lipids globally required for eukaryotic life. The sphingolipid content varies among endomembranes with pre- and post-Golgi compartments being poor and rich in sphingolipids, respectively. Due to this different sphingolipid content, pre- and post-Golgi membranes serve different cellular functions.

Gliadin-Specific CD8 T Cell Responses Restricted by HLA Class I A*0101 and B*0801 Molecules in Celiac Disease Patients.

Initial studies associated the HLA class I A*01 and B*08 alleles with celiac disease (CD) susceptibility. Subsequent analyses showed a primary association with HLA class II alleles encoding for the HLA DQ2.5 molecule.

Glycosphingolipid-Protein Interaction in Signal Transduction.

Glycosphingolipids (GSLs) are a class of ceramide-based glycolipids essential for embryo development in mammals. The synthesis of specific GSLs depends on the expression of distinctive sets of GSL synthesizing enzymes that is tightly regulated during development. Several reports have described how cell surface receptors can be kept in a resting state or activate alternative signalling events as a consequence of their interaction with GSLs.

Autophagosome-lysosome fusion triggers a lysosomal response mediated by TLR9 and controlled by OCRL.

Phosphoinositides (PtdIns) control fundamental cell processes, and inherited defects of PtdIns kinases or phosphatases cause severe human diseases, including Lowe syndrome due to mutations in OCRL, which encodes a PtdIns(4,5)P2 5-phosphatase. Here we unveil a lysosomal response to the arrival of autophagosomal cargo in which OCRL plays a key part. We identify mitochondrial DNA and TLR9 as the cargo and the receptor that triggers and mediates, respectively, this response.

A near-infrared fluorescence assay method to detect patulin in food.

Patulin (PAT) is a toxic secondary metabolite (mycotoxin) of different fungal species belonging to the genera Penicillium, Aspergillus, and Byssochlamys. They can grow on a large variety of food, including fruits, grains, and cheese. The amount of PAT in apple derivative products is a crucial issue because it is the measure of the quality of both the used raw products and the performed production process.

A Golgi-based KDELR-dependent signalling pathway controls extracellular matrix degradation.

We recently identified an endomembrane-based signalling cascade that is activated by the KDEL receptor (KDELR) on the Golgi complex. At the Golgi, the KDELR acts as a traffic sensor (presumably via binding to chaperones that leave the ER) and triggers signalling pathways that balance membrane fluxes between ER and Golgi. One such pathway relies on Gq and Src.

Ferric microperoxidase-11 catalyzes peroxynitrite isomerization.

Microperoxidase-11 (MP11) is an undecapeptide derived from horse heart cytochrome c offering the possibility to study the reactivity of the heme group relatively unshielded by the protein. Here, the peroxynitrite isomerization to NO3(-) catalyzed by ferric MP11 (MP11-Fe(III)) is reported. Data were obtained between pH3.

Outside the unusual cell wall of the hyperthermophilic archaeon Aeropyrum pernix K1.

In contrast to the extensively studied eukaryal and bacterial protein secretion systems, comparatively less is known about how and which proteins cross the archaeal cell membrane. To identify secreted proteins of the hyperthermophilic archaeon Aeropyrum pernix K1 we used a proteomics approach to analyze the extracellular and cell surface protein fractions. The experimentally obtained data comprising 107 proteins were compared with the in silico predicted secretome.