RapamycinFungusV1, Main, Exploration, bibRecord, 001491

Regulated expression of the Leishmania major surface virulence factor lipophosphoglycan using conditionally destabilized fusion proteins.

Identifieur interne : 001491 ( Main/Exploration ); précédent : 001490; suivant : 001492

Regulated expression of the Leishmania major surface virulence factor lipophosphoglycan using conditionally destabilized fusion proteins.

Auteurs : Luciana Madeira Da Silva [États-Unis] ; Katherine L. Owens ; Silvane M F. Murta ; Stephen M. Beverley

Source :

Proceedings of the National Academy of Sciences of the United States of America [ 1091-6490 ] ; 2009.

RBID : pubmed:19383793

Descripteurs français

KwdFr :
- Animaux (MeSH), Facteurs de virulence (biosynthèse), Glycosphingolipides (biosynthèse), Intramolecular transferases (métabolisme), Leishmania major (effets des médicaments et des substances chimiques), Leishmania major (génétique), Leishmania major (métabolisme), Protéines de fusion recombinantes (génétique), Protéines de fusion recombinantes (métabolisme), Protéines de liaison au tacrolimus (génétique), Protéines de liaison au tacrolimus (métabolisme), Régulation négative (MeSH), Sirolimus (pharmacologie), Structure tertiaire des protéines (MeSH).
MESH :
- biosynthèse : Facteurs de virulence, Glycosphingolipides.
- effets des médicaments et des substances chimiques : Leishmania major.
- génétique : Leishmania major, Protéines de fusion recombinantes, Protéines de liaison au tacrolimus.
- métabolisme : Intramolecular transferases, Leishmania major, Protéines de fusion recombinantes, Protéines de liaison au tacrolimus.
- pharmacologie : Sirolimus.
- Animaux, Régulation négative, Structure tertiaire des protéines.

English descriptors

KwdEn :
- Animals (MeSH), Down-Regulation (MeSH), Glycosphingolipids (biosynthesis), Intramolecular Transferases (metabolism), Leishmania major (drug effects), Leishmania major (genetics), Leishmania major (metabolism), Protein Structure, Tertiary (MeSH), Recombinant Fusion Proteins (genetics), Recombinant Fusion Proteins (metabolism), Sirolimus (pharmacology), Tacrolimus Binding Proteins (genetics), Tacrolimus Binding Proteins (metabolism), Virulence Factors (biosynthesis).
MESH :
- chemical , biosynthesis : Glycosphingolipids, Virulence Factors.
- chemical , genetics : Recombinant Fusion Proteins, Tacrolimus Binding Proteins.
- chemical , metabolism : Intramolecular Transferases, Recombinant Fusion Proteins, Tacrolimus Binding Proteins.
- drug effects : Leishmania major.
- genetics : Leishmania major.
- metabolism : Leishmania major.
- chemical , pharmacology : Sirolimus.
- Animals, Down-Regulation, Protein Structure, Tertiary.

Abstract

Surface glycoconjugates play important roles in the infectious cycle of Leishmania major, including the abundant lipophosphoglycan (LPG) implicated in parasite survival in the sand fly vector and the initial stages of establishment in the mammalian host macrophage. We describe a system for inducible expression of LPG, applying a novel protein-based system that allows controlled degradation of a key LPG biosynthetic enzyme, UDP-galactopyranose mutase (UGM). This methodology relies on a mutated FK506-binding protein (FKBP) destabilizing domain (dd) fused to the protein of interest; in the absence of rapamycin analogs, such as Shld1, the dd domain is destabilized, leading to proteasomal degradation, whereas drug treatment confers stabilization. Tests in L. major using dd fusions to a panel of reporters and cellular proteins confirmed its functionality, with a high degree of regulation and low background, and we established the kinetics of protein activation and/or loss. Two inexpensive and widely available ligands, FK506 and rapamycin, functioned similarly to Shld1, without effect on Leishmania growth or differentiation. We generated parasites lacking UGM through deletion of the GLF gene and substitution with a ddGLF fusion construct, either as chromosomal knockins or through episomal complementation; these showed little or no LPG expression in the absence of inducer, whereas in its presence, high levels of LPG were attained rapidly. Complement lysis tests confirmed the correct integrity of the Leishmania LPG coat. These data suggest that the dd approach has great promise in the study of LPG and other pathways relevant to parasite survival and virulence.

DOI: 10.1073/pnas.0901698106
PubMed: 19383793
PubMed Central: PMC2678649

Affiliations:

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 001515
to stream Main, to step Curation: 001515

Le document en format XML

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<front><div type="abstract" xml:lang="en">Surface glycoconjugates play important roles in the infectious cycle of Leishmania major, including the abundant lipophosphoglycan (LPG) implicated in parasite survival in the sand fly vector and the initial stages of establishment in the mammalian host macrophage. We describe a system for inducible expression of LPG, applying a novel protein-based system that allows controlled degradation of a key LPG biosynthetic enzyme, UDP-galactopyranose mutase (UGM). This methodology relies on a mutated FK506-binding protein (FKBP) destabilizing domain (dd) fused to the protein of interest; in the absence of rapamycin analogs, such as Shld1, the dd domain is destabilized, leading to proteasomal degradation, whereas drug treatment confers stabilization. Tests in L. major using dd fusions to a panel of reporters and cellular proteins confirmed its functionality, with a high degree of regulation and low background, and we established the kinetics of protein activation and/or loss. Two inexpensive and widely available ligands, FK506 and rapamycin, functioned similarly to Shld1, without effect on Leishmania growth or differentiation. We generated parasites lacking UGM through deletion of the GLF gene and substitution with a ddGLF fusion construct, either as chromosomal knockins or through episomal complementation; these showed little or no LPG expression in the absence of inducer, whereas in its presence, high levels of LPG were attained rapidly. Complement lysis tests confirmed the correct integrity of the Leishmania LPG coat. These data suggest that the dd approach has great promise in the study of LPG and other pathways relevant to parasite survival and virulence.</div>
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	Serveur d'exploration sur la rapamycine et les champignons
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Regulated expression of the Leishmania major surface virulence factor lipophosphoglycan using conditionally destabilized fusion proteins.

Regulated expression of the Leishmania major surface virulence factor lipophosphoglycan using conditionally destabilized fusion proteins.

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