Relevant bibliographies by topics / Phosphatidyl-myo-Inositol Mannosides

Contents

  1. Journal articles
  2. Dissertations / Theses

Academic literature on the topic 'Phosphatidyl-myo-Inositol Mannosides'

Author: Grafiati
Published: 17 May 2025

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'Phosphatidyl-myo-Inositol Mannosides.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "Phosphatidyl-myo-Inositol Mannosides"

1

Scherman, Hataichanok, Devinder Kaur, Ha Pham, Henrieta Škovierová, Mary Jackson, and Patrick J. Brennan. "Identification of a Polyprenylphosphomannosyl Synthase Involved in the Synthesis of Mycobacterial Mannosides." Journal of Bacteriology 191, no. 21 (August 28, 2009): 6769–72. http://dx.doi.org/10.1128/jb.00431-09.

Full text
Abstract:
ABSTRACT We report on the identification of a glycosyltransferase (GT) from Mycobacterium tuberculosis H37Rv, Rv3779, of the membranous GT-C superfamily responsible for the direct synthesis of polyprenyl-phospho-mannopyranose and thus indirectly for lipoarabinomannan, lipomannan, and the higher-order phosphatidyl-myo-inositol mannosides.
APA, Harvard, Vancouver, ISO, and other styles
2

Sancho-Vaello, Enea, David Albesa-Jové, Ane Rodrigo-Unzueta, and Marcelo E. Guerin. "Structural basis of phosphatidyl-myo-inositol mannosides biosynthesis in mycobacteria." Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids 1862, no. 11 (November 2017): 1355–67. http://dx.doi.org/10.1016/j.bbalip.2016.11.002.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Gilleron, Martine, Buko Lindner, and Germain Puzo. "MS/MS Approach for Characterization of the Fatty Acid Distribution on Mycobacterial Phosphatidyl-myo-inositol Mannosides." Analytical Chemistry 78, no. 24 (December 2006): 8543–48. http://dx.doi.org/10.1021/ac061574a.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Front, Sophie, Nathalie Court, Marie-Laure Bourigault, Stéphanie Rose, Bernhard Ryffel, François Erard, Valérie F. J. Quesniaux, and Olivier R. Martin. "Phosphatidyl myo-Inositol Mannosides Mimics Built on an Acyclic or Heterocyclic Core: Synthesis and Anti-inflammatory Properties." ChemMedChem 6, no. 11 (September 7, 2011): 2081–93. http://dx.doi.org/10.1002/cmdc.201100291.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Omahdi, Zakaria, Yuto Horikawa, Masamichi Nagae, Kenji Toyonaga, Akihiro Imamura, Koichi Takato, Takamasa Teramoto, Hideharu Ishida, Yoshimitsu Kakuta, and Sho Yamasaki. "Structural insight into the recognition of pathogen-derived phosphoglycolipids by C-type lectin receptor DCAR." Journal of Biological Chemistry 295, no. 17 (March 5, 2020): 5807–17. http://dx.doi.org/10.1074/jbc.ra120.012491.

Full text
Abstract:
The C-type lectin receptors (CLRs) form a family of pattern recognition receptors that recognize numerous pathogens, such as bacteria and fungi, and trigger innate immune responses. The extracellular carbohydrate-recognition domain (CRD) of CLRs forms a globular structure that can coordinate a Ca2+ ion, allowing receptor interactions with sugar-containing ligands. Although well-conserved, the CRD fold can also display differences that directly affect the specificity of the receptors for their ligands. Here, we report crystal structures at 1.8–2.3 Å resolutions of the CRD of murine dendritic cell-immunoactivating receptor (DCAR, or Clec4b1), the CLR that binds phosphoglycolipids such as acylated phosphatidyl-myo-inositol mannosides (AcPIMs) of mycobacteria. Using mutagenesis analysis, we identified critical residues, Ala136 and Gln198, on the surface surrounding the ligand-binding site of DCAR, as well as an atypical Ca2+-binding motif (Glu-Pro-Ser/EPS168–170). By chemically synthesizing a water-soluble ligand analog, inositol-monophosphate dimannose (IPM2), we confirmed the direct interaction of DCAR with the polar moiety of AcPIMs by biolayer interferometry and co-crystallization approaches. We also observed a hydrophobic groove extending from the ligand-binding site that is in a suitable position to interact with the lipid portion of whole AcPIMs. These results suggest that the hydroxyl group-binding ability and hydrophobic groove of DCAR mediate its specific binding to pathogen-derived phosphoglycolipids such as mycobacterial AcPIMs.
APA, Harvard, Vancouver, ISO, and other styles
6

Schami, Alyssa, Wei Ke, Anna Allué-Guardia, Angélica M. Olmo-Fontánez, John Chan, and Jordi B. Torrelles. "The Rv2623-Rv1747 interaction influences phosphatidyl-myo-inositol levels on the cell envelope of Mycobacterium tuberculosis." Journal of Immunology 208, no. 1_Supplement (May 1, 2022): 58.19. http://dx.doi.org/10.4049/jimmunol.208.supp.58.19.

Full text
Abstract:
Abstract Mycobacterium tuberculosis (M.tb), the causative agent of tuberculosis (TB), has a complex cell envelope that provides a barrier of protection to various environments. Peripheral lipids on the M.tb cell envelope act as virulent factors influencing the host immune response to infection. Of these, some phosphatidyl-myo-inositol mannosides (PIMs) and their associated lipoglycans (lipomannan; mannose-capped lipoarabinomannan) influence M.tb-host interactions by increasing phagocytosis, blocking the maturation of M.tb-containing phagosomes, and increasing the anti-inflammatory response of infected macrophages. However, there is limited knowledge regarding how M.tb regulates PIMs levels, and how this regulation influences infection outcomes. In our previous studies, we hypothesized that Rv2623 and Rv1747 work together to regulate PIMs on the M.tb cell surface. Indeed, deleting the universal stress protein Rv2623 increases PIMs levels, growth, and virulence in vivo; while deleting the ABC transporter Rv1747 decreases PIMs levels. Here we investigate the mechanistic regulation of M.tb PIMs levels and its impact on growth and pathogenesis in vitro by assessing multiple M.tb strains with Rv2623 or Rv1747 mutated at different amino acids. Depending on the mutation, Rv2623 interacts with Rv1747 to modulate M.tb cell envelope PIMs levels at different degrees. Mutants with increased PIMs levels have increased growth in macrophages, and PIMs levels on the M.tb cell envelope may also correlate to resistance to certain anti-TB drugs. Overall, our data indicate that Rv2623 negatively regulates Rv1747 to modulate PIMs levels on the M.tb cell envelope, ultimately influencing growth and M.tb-host interactions in vitro and in vivo. Supported by grants from NIH/NIAID (1R01AI146340-01A1)
APA, Harvard, Vancouver, ISO, and other styles
7

Torrelles, Jordi B., Abul K. Azad, and Larry S. Schlesinger. "Fine Discrimination in the Recognition of Individual Species of Phosphatidyl-myo-Inositol Mannosides fromMycobacterium tuberculosisby C-Type Lectin Pattern Recognition Receptors." Journal of Immunology 177, no. 3 (July 18, 2006): 1805–16. http://dx.doi.org/10.4049/jimmunol.177.3.1805.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Cala-De Paepe, Diane, Emilie Layre, Gaëlle Giacometti, Luis F. Garcia-Alles, Lucia Mori, Daniel Hanau, Gennaro de Libero, Henri de la Salle, Germain Puzo, and Martine Gilleron. "Deciphering the Role of CD1e Protein in Mycobacterial Phosphatidyl-myo-inositol Mannosides (PIM) Processing for Presentation by CD1b to T Lymphocytes." Journal of Biological Chemistry 287, no. 37 (July 10, 2012): 31494–502. http://dx.doi.org/10.1074/jbc.m112.386300.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

Rhoades, Elizabeth R., Angela S. Archambault, Rebecca Greendyke, Fong-Fu Hsu, Cassandra Streeter, and Thomas F. Byrd. "Mycobacterium abscessusGlycopeptidolipids Mask Underlying Cell Wall Phosphatidyl-myo-Inositol Mannosides Blocking Induction of Human Macrophage TNF-α by Preventing Interaction with TLR2." Journal of Immunology 183, no. 3 (July 13, 2009): 1997–2007. http://dx.doi.org/10.4049/jimmunol.0802181.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

Patel, Onisha, Rajini Brammananth, Weiwen Dai, Santosh Panjikar, Ross L. Coppel, Isabelle S. Lucet, and Paul K. Crellin. "Crystal structure of the putative cell-wall lipoglycan biosynthesis protein LmcA from Mycobacterium smegmatis." Acta Crystallographica Section D Structural Biology 78, no. 4 (March 11, 2022): 494–508. http://dx.doi.org/10.1107/s2059798322001772.

Full text
Abstract:
The bacterial genus Mycobacterium includes important pathogens, most notably M. tuberculosis, which infects one-quarter of the entire human population, resulting in around 1.4 million deaths from tuberculosis each year. Mycobacteria, and the closely related corynebacteria, synthesize a class of abundant glycolipids, the phosphatidyl-myo-inositol mannosides (PIMs). PIMs serve as membrane anchors for hyperglycosylated species, lipomannan (LM) and lipoarabinomannan (LAM), which are surface-exposed and modulate the host immune response. Previously, in studies using the model species Corynebacterium glutamicum, NCgl2760 was identified as a novel membrane protein that is required for the synthesis of full-length LM and LAM. Here, the first crystal structure of its ortholog in Mycobacterium smegmatis, MSMEG_0317, is reported at 1.8 Å resolution. The structure revealed an elongated β-barrel fold enclosing two distinct cavities and one α-helix extending away from the β-barrel core, resembling a `cone with a flake' arrangement. Through xenon derivatization and structural comparison with AlphaFold2-derived predictions of the M. tuberculosis homolog Rv0227c, structural elements were identified that may undergo conformational changes to switch from `closed' to `open' conformations, allowing cavity access. An AlphaFold2-derived NCgl2760 model predicted a smaller β-barrel core with an enclosed central cavity, suggesting that all three proteins, which were collectively termed LmcA, may have a common mechanism of ligand binding through these cavities. These findings provide new structural insights into the biosynthetic pathway for a family of surface lipoglycans with important roles in mycobacterial pathogenesis.
APA, Harvard, Vancouver, ISO, and other styles
More sources

Dissertations / Theses on the topic "Phosphatidyl-myo-Inositol Mannosides"

1

Piechowiak, Julien. "Conception et synthèse de molécules ciblant la biosynthèse des PIMs." Electronic Thesis or Diss., Orléans, 2025. https://theses.univ-orleans.fr/prive/accesESR/2025ORLE1004_va.pdf.

Full text
Abstract:
Mycobacterium tuberculosis (M.tb) est le second agent infectieux le plus mortel au monde. Le traitement contre cette mycobactérie nécessite la prise quotidienne de deux à quatre médicaments par jour pendant six mois. Ces dernières années, une augmentation alarmante des cas de tuberculoses multirésistantes a été observée rendant la découverte de nouveaux traitements cruciale. Les médicaments antituberculeux actuels ciblent différents processus biologiques, mais aucune molécule n'a été développée pour cibler la biosynthèse des PIMs. Les PIMs (Phosphatidyl-myo-Inositol Mannosides) sont des constituants essentiels de la paroi cellulaire des mycobactéries et les précurseurs de deux lipoglycanes majeurs impliqués dans les interactions hôte-pathogène. L'acyltransférase PatA, qui catalyse le transfert d'un groupe palmitoyle sur la position 6 du mannose lié à l'inositol dans PIM1 et PIM2, est essentielle pour la croissance des mycobactéries. Par conséquent, dans le but de développer des inhibiteurs de PatA, nous avons réalisé la synthèse d'une bibliothèque de molécules basées sur un motif mannopyranosyle. En outre, les structures présentent différents groupes (octyle, carbonate, carbamate, phosphonate, triazole, galactoside) sur l'aglycone dans le but de mimer la partie phosphatidyle et différents groupes (fluor, sulfonamide, phosphonate) sur la position 6 du mannose afin de mimer soit le substrat soit l'état de transition tétraédrique de la réaction d'acylation. L'activité inhibitrice de ces composés sur PatA a été évaluée et les concentrations minimales inhibitrices (MIC) ont été déterminées sur M.tb
Mycobacterium tuberculosis (M.tb) is the second most deadly infectious agent in the world. Drug treatment requires daily dosage of two to four drugs over six months. Most recently, there has been an alarming rise of multi-drug resistant tuberculosis (TB), making the discovery of new drugs crucial. Current anti-TB drugs target diverse biological processes, but no molecules are designed to target PIMs biosynthesis. PIMs (Phosphatidyl-myo-Inositol Mannosides) are essential constituents of mycobacteria cell wall and the precursors of two major lipoglycans implicated in host-pathogen interactions. The acyltransferase PatA, catalyzing the transfer of a palmitoyl moiety to the 6-position of the mannose linked to inositol in PIM1 or PIM2, is essential for mycobacteria growth. Therefore, with the aim of developing PatA inhibitors, we synthesized a panel of molecules based on a mannopyranosyl scaffold. In addition, the structures present different groups (octyl, carbonate, carbamate, phosphonate, triazole, galactoside) on the aglycone to mimic the phosphatidyl part and different groups (fluorine, sulfonamide, phosphonate) on the 6-position of mannose in order to mimic either the substrate or the acylation tetrahedral transition state. The inhibitory activity of these compounds on PatA was evaluated and the Minimum Inhibitory Concentrations (MIC) were determined on M.tb
APA, Harvard, Vancouver, ISO, and other styles
You might also be interested in the extended bibliographies on the topic 'Phosphatidyl-myo-Inositol Mannosides' for particular source types:
Journal articles
We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!

To the bibliography