S16 and T18 mannosylation sites of LppX are not essential for its activity in phthiocerol dimycocerosates localization at the surface of Mycobacterium tuberculosis
| Autor: | Laila Sago, Anna E. Grzegorzewicz, Michael R. McNeil, Mary Jackson, Cécile Labarre, Nicolas Bayan, Nathalie Dautin, Niloofar Mohiman |
|---|---|
| Přispěvatelé: | Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Univ. Paris-Sud, Universite Paris-Saclay, 91198 ´ Gif-sur-Yvette, France, Mycobacteria Research Laboratories, Colorado State University [Fort Collins] (CSU), Institute for Integrative Biology of the Cell [Gif-sur-Yvette] (I2BC), Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS) |
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
Glycosylation
glycosylation Virulence macromolecular substances Microbiology Virulence factor Corynebacterium glutamicum Mycobacterium Mycobacterium tuberculosis 03 medical and health sciences chemistry.chemical_compound phthiocerol dimycocerosates Molecular Biology 030304 developmental biology 0303 health sciences biology 030306 microbiology Mycobacterium smegmatis [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biology General Medicine biology.organism_classification 3. Good health carbohydrates (lipids) chemistry Biochemistry Mannosylation lipids (amino acids peptides and proteins) |
| Zdroj: | Research in Microbiology Research in Microbiology, Elsevier, In press, ⟨10.1016/j.resmic.2021.103874⟩ Research in Microbiology, In press, ⟨10.1016/j.resmic.2021.103874⟩ |
| ISSN: | 0923-2508 |
| DOI: | 10.1016/j.resmic.2021.103874⟩ |
| Popis: | International audience; LppX is an important virulence factor essential for surface localization of phthiocerol dimycocerosates (DIM) in Mycobacterium tuberculosis. Based on Concanavalin A recognition, M. tuberculosis LppX (LppX-tb) was initially proposed to be glycosylated in M. tuberculosis and more recently this glycosylation was characterized by mass spectrometry analysis on LppX-tb expressed and purified from Corynebacterium glutamicum. Here, using this model organism and Mycobacterium smegmatis, we show that S16 and T18 residues of LppX-tb are indeed glycosylated with several hexoses units. Interestingly this glycosylation is strictly dependent on the mannosyl transferase PMT which, in M. tuberculosis, has been reported to be crucial for virulence. Using a site directed mutagenesis approach, we were able to show that the absence of S16 and T18 glycosylation does not alter phthiocerol dimycocerosates (DIM) localization in M. tuberculosis. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect