PoplarV1, Main, Exploration, bibRecord, 004786

Overexpression, purification, and refolding of a Porphyromonas gingivalis cysteine protease from Escherichia coli.

Identifieur interne : 004786 ( Main/Exploration ); précédent : 004785; suivant : 004787

Overexpression, purification, and refolding of a Porphyromonas gingivalis cysteine protease from Escherichia coli.

Auteurs : M B Margetts [Australie] ; I G Barr ; E A Webb

Source :

Protein expression and purification [ 1046-5928 ] ; 2000.

RBID : pubmed:10733878

Descripteurs français

English descriptors

KwdEn :
- Adhesins, Bacterial (MeSH), Blotting, Western (MeSH), Cysteine Endopeptidases (chemistry), Cysteine Endopeptidases (genetics), Cysteine Endopeptidases (metabolism), Electrophoresis, Polyacrylamide Gel (MeSH), Escherichia coli (chemistry), Escherichia coli (genetics), Escherichia coli (metabolism), Gingipain Cysteine Endopeptidases (MeSH), Hemagglutinins (chemistry), Hemagglutinins (genetics), Hemagglutinins (metabolism), Immune Sera (MeSH), Inclusion Bodies (chemistry), Porphyromonas gingivalis (chemistry), Protein Folding (MeSH), Protein Renaturation (MeSH), Protein Structure, Tertiary (MeSH), Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Recombinant Proteins (immunology), Recombinant Proteins (metabolism).
MESH :
- chemical , chemistry : Cysteine Endopeptidases, Hemagglutinins, Recombinant Proteins.
- chemical , genetics : Cysteine Endopeptidases, Hemagglutinins, Recombinant Proteins.
- chemical , immunology : Recombinant Proteins.
- chemical , metabolism : Cysteine Endopeptidases, Hemagglutinins, Recombinant Proteins.
- chemical : Adhesins, Bacterial, Gingipain Cysteine Endopeptidases, Immune Sera.
- chemistry : Escherichia coli, Inclusion Bodies, Porphyromonas gingivalis.
- genetics : Escherichia coli.
- metabolism : Escherichia coli.
- Blotting, Western, Electrophoresis, Polyacrylamide Gel, Protein Folding, Protein Renaturation, Protein Structure, Tertiary.

Abstract

This paper describes the overexpression of the Rgp-1 (arginine) protease domain from Porphyromonas gingivalis. This protease and the related Kgp (lysine) protease, both of which display trypsin-like specificity, have been implicated as major virulence factors and may play a significant role in the etiology of periodontal disease. Both Rgp-1 and Kgp are initially translated as polyproteins, each containing a protease domain and multiple adhesin domains. The Rgp-1 protease domain was expressed in E. coli, purified, refolded, and assayed for activity. These expression studies demonstrated that prior to the formation of inclusion bodies in the E. coli cytoplasm, the protease was proteolytically active and could hydrolyze a specific synthetic substrate. When the Rgp-1 protease domain was purified from inclusion bodies and refolded, it was found to be autolytically active and displayed specific catalytic activity. This is the first report on the expression and purification of active Rgp-1 from E. coli. Polyclonal antisera raised against recombinant protein recognized the native form of the protease in the P. gingivalis strain W50, indicating that the recombinant protein contained some of the antigenic determinants of the native protease.

DOI: 10.1006/prep.2000.1193
PubMed: 10733878

Affiliations:

Australie

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Le document en format XML

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<term>Cysteine Endopeptidases (genetics)</term>
<term>Cysteine Endopeptidases (metabolism)</term>
<term>Electrophoresis, Polyacrylamide Gel (MeSH)</term>
<term>Escherichia coli (chemistry)</term>
<term>Escherichia coli (genetics)</term>
<term>Escherichia coli (metabolism)</term>
<term>Gingipain Cysteine Endopeptidases (MeSH)</term>
<term>Hemagglutinins (chemistry)</term>
<term>Hemagglutinins (genetics)</term>
<term>Hemagglutinins (metabolism)</term>
<term>Immune Sera (MeSH)</term>
<term>Inclusion Bodies (chemistry)</term>
<term>Porphyromonas gingivalis (chemistry)</term>
<term>Protein Folding (MeSH)</term>
<term>Protein Renaturation (MeSH)</term>
<term>Protein Structure, Tertiary (MeSH)</term>
<term>Recombinant Proteins (chemistry)</term>
<term>Recombinant Proteins (genetics)</term>
<term>Recombinant Proteins (immunology)</term>
<term>Recombinant Proteins (metabolism)</term>
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<term>Corps d'inclusion (composition chimique)</term>
<term>Cysteine endopeptidases (composition chimique)</term>
<term>Cysteine endopeptidases (génétique)</term>
<term>Cysteine endopeptidases (métabolisme)</term>
<term>Escherichia coli (composition chimique)</term>
<term>Escherichia coli (génétique)</term>
<term>Escherichia coli (métabolisme)</term>
<term>Hémagglutinines (composition chimique)</term>
<term>Hémagglutinines (génétique)</term>
<term>Hémagglutinines (métabolisme)</term>
<term>Pliage des protéines (MeSH)</term>
<term>Porphyromonas gingivalis (composition chimique)</term>
<term>Protéines recombinantes (composition chimique)</term>
<term>Protéines recombinantes (génétique)</term>
<term>Protéines recombinantes (immunologie)</term>
<term>Protéines recombinantes (métabolisme)</term>
<term>Renaturation des protéines (MeSH)</term>
<term>Structure tertiaire des protéines (MeSH)</term>
<term>Sérums immuns (MeSH)</term>
<term>Technique de Western (MeSH)</term>
<term>Électrophorèse sur gel de polyacrylamide (MeSH)</term>
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<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cysteine Endopeptidases</term>
<term>Hemagglutinins</term>
<term>Recombinant Proteins</term>
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<term>Hemagglutinins</term>
<term>Recombinant Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" xml:lang="en"><term>Adhesins, Bacterial</term>
<term>Gingipain Cysteine Endopeptidases</term>
<term>Immune Sera</term>
</keywords>
<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Escherichia coli</term>
<term>Inclusion Bodies</term>
<term>Porphyromonas gingivalis</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Corps d'inclusion</term>
<term>Cysteine endopeptidases</term>
<term>Escherichia coli</term>
<term>Hémagglutinines</term>
<term>Porphyromonas gingivalis</term>
<term>Protéines recombinantes</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Escherichia coli</term>
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<term>Escherichia coli</term>
<term>Hémagglutinines</term>
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</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cysteine endopeptidases</term>
<term>Escherichia coli</term>
<term>Hémagglutinines</term>
<term>Protéines recombinantes</term>
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<term>Electrophoresis, Polyacrylamide Gel</term>
<term>Protein Folding</term>
<term>Protein Renaturation</term>
<term>Protein Structure, Tertiary</term>
</keywords>
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<term>Pliage des protéines</term>
<term>Renaturation des protéines</term>
<term>Structure tertiaire des protéines</term>
<term>Sérums immuns</term>
<term>Technique de Western</term>
<term>Électrophorèse sur gel de polyacrylamide</term>
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<front><div type="abstract" xml:lang="en">This paper describes the overexpression of the Rgp-1 (arginine) protease domain from Porphyromonas gingivalis. This protease and the related Kgp (lysine) protease, both of which display trypsin-like specificity, have been implicated as major virulence factors and may play a significant role in the etiology of periodontal disease. Both Rgp-1 and Kgp are initially translated as polyproteins, each containing a protease domain and multiple adhesin domains. The Rgp-1 protease domain was expressed in E. coli, purified, refolded, and assayed for activity. These expression studies demonstrated that prior to the formation of inclusion bodies in the E. coli cytoplasm, the protease was proteolytically active and could hydrolyze a specific synthetic substrate. When the Rgp-1 protease domain was purified from inclusion bodies and refolded, it was found to be autolytically active and displayed specific catalytic activity. This is the first report on the expression and purification of active Rgp-1 from E. coli. Polyclonal antisera raised against recombinant protein recognized the native form of the protease in the P. gingivalis strain W50, indicating that the recombinant protein contained some of the antigenic determinants of the native protease.</div>
</front>
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<Abstract><AbstractText>This paper describes the overexpression of the Rgp-1 (arginine) protease domain from Porphyromonas gingivalis. This protease and the related Kgp (lysine) protease, both of which display trypsin-like specificity, have been implicated as major virulence factors and may play a significant role in the etiology of periodontal disease. Both Rgp-1 and Kgp are initially translated as polyproteins, each containing a protease domain and multiple adhesin domains. The Rgp-1 protease domain was expressed in E. coli, purified, refolded, and assayed for activity. These expression studies demonstrated that prior to the formation of inclusion bodies in the E. coli cytoplasm, the protease was proteolytically active and could hydrolyze a specific synthetic substrate. When the Rgp-1 protease domain was purified from inclusion bodies and refolded, it was found to be autolytically active and displayed specific catalytic activity. This is the first report on the expression and purification of active Rgp-1 from E. coli. Polyclonal antisera raised against recombinant protein recognized the native form of the protease in the P. gingivalis strain W50, indicating that the recombinant protein contained some of the antigenic determinants of the native protease.</AbstractText>
<CopyrightInformation>Copyright 2000 Academic Press.</CopyrightInformation>
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Overexpression, purification, and refolding of a Porphyromonas gingivalis cysteine protease from Escherichia coli.

Overexpression, purification, and refolding of a Porphyromonas gingivalis cysteine protease from Escherichia coli.

Source :

Descripteurs français

English descriptors

Abstract

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

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki