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yeast glycosylation

Benedikt Hacker, Christoph Schultheiß, Michael Döring, Ursula Kurzik-Dumke
This study provides first insights into the involvement of hNOT/ALG3, the human counterpart of the Drosophila NOT and yeast ALG3 gene, in various putative molecular networks. HNOT/ALG3 encodes two translated transcripts encoding precursor proteins differing in their N-terminus and showing 33% identity with the yeast asparagine-linked glycosylation 3 (ALG3) protein. Experimental evidence for the functional homology of the proteins of fly and man in the N-glycosylation has still to be provided. In this study, using the yeast two-hybrid technique we identify 17 molecular partners of hNOT-1/ALG3-1...
March 14, 2018: Human Molecular Genetics
Marta Cova, Borja López-Gutiérrez, Sara Artigas-Jerónimo, Aida González-Díaz, Giulia Bandini, Steven Maere, Lorenzo Carretero-Paulet, Luis Izquierdo
Apicomplexa form a phylum of obligate parasitic protozoa of great clinical and veterinary importance. These parasites synthesize glycoconjugates for their survival and infectivity, but the enzymatic steps required to generate the glycosylation precursors are not completely characterized. In particular, glucosamine-phosphate N-acetyltransferase (GNA1) activity, needed to produce the essential UDP-N-acetylglucosamine (UDP-GlcNAc) donor, has not been identified in any Apicomplexa. We scanned the genomes of Plasmodium falciparum and representatives from six additional main lineages of the phylum for proteins containing the Gcn5-related N-acetyltransferase (GNAT) domain...
March 5, 2018: Scientific Reports
Oluwatoyin A Asojo, Rabih Darwiche, Selam Gebremedhin, Geert Smant, Jose L Lozano-Torres, Claire Drurey, Jeroen Pollet, Rick M Maizels, Roger Schneiter, Ruud H P Wilbers
Heligmosomoides polygyrus bakeri is a model parasitic hookworm used to study animal and human helminth diseases. During infection, the parasite releases excretory/secretory (ES) products that modulate the immune system of the host. The most abundant protein family in ES products comprises the venom allergen-like proteins (VALs), which are members of the SCP/TAPS (Sperm-coating protein / Tpx / antigen 5 / pathogenesis related-1 / Sc7) superfamily. There are >30 secreted Heligmosomoides polygyrus VAL proteins (HpVALs) and these proteins are characterized by having either one or two 15 kDa CAP (cysteine-rich secretory protein (CRISP) / antigen 5 / pathogenesis related-1) domains...
March 2, 2018: International Journal for Parasitology
Rabih Darwiche, Fernanda Lugo, Claire Drurey, Koen Varossieau, Geert Smant, Ruud H P Wilbers, Rick M Maizels, Roger Schneiter, Oluwatoyin A Asojo
Brugia malayi is a causative agent of lymphatic filariasis, a major tropical disease. The infective L3 parasite stage releases immunomodulatory proteins including the venom allergen-like proteins (VALs), which are members of the SCP/TAPS (Sperm-coating protein / Tpx / antigen 5 / pathogenesis related-1 / Sc7) superfamily. BmVAL-1 is a major target of host immunity with >90% of infected B. malayi microfilaraemic cases being seropositive for antibodies to BmVAL-1. This study is part of ongoing efforts to characterize the structures and functions of important B...
February 28, 2018: International Journal for Parasitology
James R O Eaton, Yara Alenazi, Kamayani Singh, Graham Davies, Lucia Geis-Asteggiante, Benedikt Kessler, Carol V Robinson, Akane Kawamura, Shoumo Bhattacharya
Tick chemokine-binding proteins (evasins) are an emerging class of biologicals that target multiple chemokines and have shown anti-inflammatory activities in preclinical disease models. Using yeast surface display, we identified a CCL8-binding evasin, P672, from the tick Rhipicephalus pulchellus. We found that P672 binds CCL8 and eight other CC-class chemokines with a Kd < 10 nM and four other CC chemokines with a Kd between 10 and 100 nM, and neutralizes CCL3, CCL3L1, and CCL8 with an IC50 < 10 nM. The CC chemokine-binding profile was distinct from that of evasin 1 (EVA1), which does not bind CCL8...
February 27, 2018: Journal of Biological Chemistry
Robert Howlett, Nicholas Read, Anpu Varghese, Charles Kershaw, Y Hancock, Margaret C M Smith
Polyprenol phosphate mannose (PPM) is a lipid-linked sugar donor used by extra-cytoplasmic glycosyl tranferases in bacteria. PPM is synthesiszed by polyprenol phosphate mannose synthase, Ppm1, and in most Actinobacteria is used as the sugar donor for protein O-mannosyl transferase, Pmt, in protein glycosylation. Ppm1 and Pmt have homologues in yeasts and humans, where they are required for protein O-mannosylation. Actinobacteria also use PPM for lipoglycan biosynthesis. Here we show that ppm1 mutants of Streptomyces coelicolor have increased susceptibility to a number of antibiotics that target cell wall biosynthesis...
February 1, 2018: Microbiology
Fei Ge, Longbao Zhu, Anna Aang, Ping Song, Wanzhen Li, Yugui Tao, Guocheng Du
Yeast has been increasingly used as a host for the expression of enzymes. Compared to other expression systems, the yeast expression system has many advantages including its suitability for large-scale fermentation and its ability to modify enzymes. When expressed in yeast, many recombinant enzymes are N-glycosylated, and this may play an important role in their activity, thermostability and secretion. Although the mechanism underlying this process is not clear, the regulation of N-glycosylation by introducing or eliminating N-glycosylation at specific sites has developed into an important strategy for improving the production or catalytic properties of recombinant enzymes...
February 15, 2018: Biotechnology Letters
Tao Zuo, Jinshuai Shan, Yang Liu, Rong Xie, Xiaochun Yu, Chen Wu
N-Acetylgalactosaminyltransferase-14 (GALNT14) is a member of acetylgalactosaminyltransferases family. We have shown that GALNT14 could promote breast cancer cell invasion. However, the underlying molecular mechanism is unclear. Here, using yeast two hybrid, we find that EGF-containing fibulin-like extracellular matrix protein 2 (EFEMP2) interacts with GALNT14. Both in vitro and in vivo binding assays show that EFEMP2 is associated with GALNT14. Moreover, we find that GALNT14 mediates glycosylation of EFEMP2...
February 7, 2018: Translational Oncology
Kuo-Ming Yu, Johnson Yiu-Nam Lau, Manson Fok, Yuk-Keung Yeung, Siu-Ping Fok, Felix Shek, Wing-Tak Wong, Qui-Lim Choo
Current source of recombinant human interleukin-11 (rhIL-11) is isolated from a fusion protein expressed by E. coli that requires additional enterokinase to remove linked protein, resulting in product heterogeneity of N-terminal sequence. Due to lack of glycosylation, rhIL-11 is suitable to be expressed by yeast cells. However, the only available yeast-derived rhIL-11 presents an obstacle in low production yield, as well as an unamiable process, such as the use of reverse-phase chromatography employing plenty of toxic organic solvents...
February 2, 2018: Protein Expression and Purification
Adriana Carolina Gonzalez, Michaela Schweizer, Sebastian Jagdmann, Christian Bernreuther, Thomas Reinheckel, Paul Saftig, Markus Damme
Variants in the phospholipase D3 (PLD3) gene have genetically been linked to late-onset Alzheimer's disease. We present a detailed biochemical analysis of PLD3 and reveal its endogenous localization in endosomes and lysosomes. PLD3 reaches lysosomes as a type II transmembrane protein via a (for mammalian cells) uncommon intracellular biosynthetic route that depends on the ESCRT (endosomal sorting complex required for transport) machinery. PLD3 is sorted into intraluminal vesicles of multivesicular endosomes, and ESCRT-dependent sorting correlates with ubiquitination...
January 23, 2018: Cell Reports
Lucía Feijoo-Siota, José Luis R Rama, Angeles Sánchez-Pérez, Tomás G Villa
Galium verum, also known as Lady's Bedstraw or Cheese Rennet, is a herbaceous perennial plant traditionally used in cheese-making. We used RACE PCR to isolate novel enzymes from Galium verum with the ability to clot milk. This approach generated two cDNA sequences (named preprogaline A and B) encoding proteins displaying the typical plant aspartic protease primary structure. Preprogaline B was expressed in the yeast Pichia pastoris, after deleting and replacing its original signal peptide with the yeast α-factor signal peptide from Saccharomyces cerevisiae...
January 12, 2018: Journal of Biotechnology
Meysam Rezaie, Saeed Aminzadeh, Farid Heidari, Masoud Mashhadi Akbar Boojar, Ali Asghar Karkhane
Background: Typically, non-cellulytic glucanase, including fungi and yeast cell wall hydrolyzing enzymes, are release by some symbiotic fungi and plants during the mycoparasitic fungi attack on plants. These enzymes are known as the defense mechanisms of plants. This study intends to investigate the biochemical properties of β-1,6-glucanase (bg16M) from native thermophilic bacteria, Cohnella A01. Methods: bg16M gene was cloned and expressed in E. coli BL21 (DE3)...
January 13, 2018: Iranian Biomedical Journal
Bruce L Granger
Yeast wall protein 1 (Ywp1) is an abundant glycoprotein of the cell wall of the yeast form of Candida albicans, the most prevalent fungal pathogen of humans. Antibodies that bind to the polypeptide backbone of isolated Ywp1 show little binding to intact yeast cells, presumably because the Ywp1 epitopes are masked by the polysaccharides of the mannoproteins that form the outer layer of the cell wall. Rare cells do exhibit much greater anti-Ywp1 binding, however, and one of these was isolated and characterized...
2018: PloS One
Chiu-Ping Liu, Tsung-I Tsai, Ting Cheng, Vidya S Shivatare, Chung-Yi Wu, Chung-Yi Wu, Chi-Huey Wong
Monoclonal antibodies (mAbs) have been developed as therapeutics, especially for the treatment of cancer, inflammation, and infectious diseases. Because the glycosylation of mAbs in the Fc region influences their interaction with effector cells that kill antibody-targeted cells, and the current method of antibody production is relatively expensive, efforts have been directed toward the development of alternative expressing systems capable of large-scale production of mAbs with desirable glycoforms. In this study, we demonstrate that the mAb trastuzumab expressed in glycoengineered P...
January 8, 2018: Proceedings of the National Academy of Sciences of the United States of America
Rebekka Wild, Julia Kowal, Jillianne Eyring, Elsy M Ngwa, Markus Aebi, Kaspar P Locher
Oligosaccharyltransferase (OST) is an essential membrane protein complex in the Endoplasmic Reticulum, where it transfers an oligosaccharide from a dolichol-pyrophosphate-activated donor to glycosylation sites of secretory proteins. We here describe the atomic structure of yeast OST determined by cryo-EM, revealing a conserved subunit arrangement. The active site of the catalytic STT3 subunit points away from the center of the complex, allowing unhindered access to substrates. The dolichol-pyrophosphate moiety binds to a lipid-exposed groove of STT3, while two non-catalytic subunits and an ordered N-glycan form a membrane-proximal pocket for the oligosaccharide...
January 4, 2018: Science
Eun Jung Thak, Jungho Kim, Dong-Jik Lee, Jeong Yoon Kim, Hyun Ah Kang
Protein glycosylation, the most universal and diverse post-translational modification, can affect protein secretion, stability, and immunogenicity. The structures of glycans attached to proteins are quite diverse among different organisms and even within yeast species. In yeast, protein glycosylation plays key roles in the quality control of secretory proteins, and particularly in maintaining cell wall integrity. Moreover, in pathogenic yeasts, glycans assembled on cell-surface glycoproteins can mediate their interactions with host cells...
January 2018: Journal of Microbiology / the Microbiological Society of Korea
Andrew L Garfoot, Kristie D Goughenour, Marcel Wüthrich, Murugesan V S Rajaram, Larry S Schlesinger, Bruce S Klein, Chad A Rappleye
The ability to grow at mammalian body temperatures is critical for pathogen infection of humans. For the thermally dimorphic fungal pathogen Histoplasma capsulatum, elevated temperature is required for differentiation of mycelia or conidia into yeast cells, a step critical for invasion and replication within phagocytic immune cells. Posttranslational glycosylation of extracellular proteins characterizes factors produced by the pathogenic yeast cells but not those of avirulent mycelia, correlating glycosylation with infection...
January 2, 2018: MBio
Sheng-Tao Li, Ning Wang, Xin-Xin Xu, Morihisa Fujita, Hideki Nakanishi, Toshihiko Kitajima, Neta Dean, Xiao-Dong Gao
Asparagine (N)-linked glycosylation requires the ordered, stepwise synthesis of lipid-linked oligosaccharide (LLO) precursor Glc3Man9GlcNAc2-pyrophosphate-dolichol (Glc3Man9Gn2-PDol) on the endoplasmic reticulum. The fourth and fifth step of LLO synthesis are catalyzed by Alg2, an unusual mannosyltransferase (MTase) with two different MTase activities; Alg2 adds both an α1,3- and α1,6-mannose onto ManGlcNAc2-PDol to form the trimannosyl core Man3GlcNAc2-PDol. The biochemical properties of Alg2 are controversial and remain undefined...
December 22, 2017: FASEB Journal: Official Publication of the Federation of American Societies for Experimental Biology
Rubini Kannangara, Lina Siukstaite, Jonas Borch-Jensen, Bjørn Madsen, Kenneth T Kongstad, Dan Staerk, Mads Bennedsen, Finn T Okkels, Silas A Rasmussen, Thomas O Larsen, Rasmus J N Frandsen, Birger Lindberg Møller
Carminic acid, a glucosylated anthraquinone found in scale insects like Dactylopius coccus, has since ancient times been used as a red colorant in various applications. Here we show that a membrane-bound C-glucosyltransferase, isolated from D. coccus and designated DcUGT2, catalyzes the glucosylation of flavokermesic acid and kermesic acid into their respective C-glucosides dcII and carminic acid. DcUGT2 is predicted to be a type I integral endoplasmic reticulum (ER) membrane protein, containing a cleavable N-terminal signal peptide and a C-terminal transmembrane helix that anchors the protein to the ER, followed by a short cytoplasmic tail...
December 7, 2017: Nature Communications
Silvia Boschi Bazan, Barbara Walch-Rückheim, Manfred J Schmitt, Frank Breinig
Activated dendritic cells (DC) induce and polarize T-cell responses by expression of distinct maturation markers and cytokines. This study systematically investigated the capacity of different biotechnically relevant yeast species and strains including Saccharomyces cerevisiae, Schizosaccharomyces pombe, Kluyveromyces lactis, Pichia pastoris, Hansenula polymorpha, Yarrowia lipolytica, and Candida glabrata to initiate maturation of human DC. As important prerequisite for T-cell activation, all yeasts were shown to effectively induce, though to a different extent, the expression of the activation marker CD83, the co-stimulatory molecules CD80, CD86, CD54, CD58, and CD40, as well as the antigen-presenting molecules MHCs I and II...
November 21, 2017: Medical Microbiology and Immunology
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