ArticleThe Biochemical journal2004
Functional refolding of the Campylobacter jejuni MOMP (major outer membrane protein) porin by GroEL from the same species.
Article in The Biochemical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 17 citations in OpenAlex.
- Pathogenicity and virulence ofVirulence · 2024Review
- Comparative Proteomic Analysis of Psychrophilic vs. Mesophilic Bacterial Species Reveals Different Strategies to Achieve Temperature Adaptation.Frontiers in microbiology · 2022Article
- Antimicrobial and Virulence-Modulating Effects of Clove Essential Oil on the Foodborne Pathogen Campylobacter jejuni.Applied and environmental microbiology · 2016Article
- Folding of newly translated membrane protein CCR5 is assisted by the chaperonin GroEL-GroES.Scientific reports · 2015Article
- Molecular mechanisms and biological role of Campylobacter jejuni attachment to host cells.European journal of microbiology & immunology · 2012Review
- Identification of in vivo HSP90-interacting proteins reveals modularity of HSP90 complexes is dependent on the environment in psychrophilic bacteria.Cell stress & chaperones · 2011Article
- Junctin and triadin each activate skeletal ryanodine receptors but junctin alone mediates functional interactions with calsequestrin.The international journal of biochemistry & cell biology · 2009Article
- Examination of Campylobacter jejuni putative adhesins leads to the identification of a new protein, designated FlpA, required for chicken colonization.Infection and immunity · 2009Article
- Genomic differences between Campylobacter jejuni isolates identify surface membrane and flagellar function gene products potentially important for colonizing the chicken intestine.Functional & integrative genomics · 2008Article
- GroEL as a molecular scaffold for structural analysis of the anthrax toxin pore.Nature structural & molecular biology · 2008Article
- Misfolding of a bacterial autotransporter.Protein science : a publication of the Protein Society · 2005Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Functional and structural studies of outer membrane proteins from Gram-negative bacteria are frequently carried out using refolded proteins. Recombinant proteins are produced in Escherichia coli as inclusion bodies and then tediously refolded by dilution in buffered detergent solutions. In the present work, we obtained the refolding of MOMP (major outer membrane protein) from Campylobacter assisted by the molecular chaperone GroEL. Refolded MOMP recovered its native pore-forming activity when reconstituted in planar lipid bilayers. Both proteins were purified from the Campylobacter jejuni strain 85H. The purity of GroEL was assessed by silver staining and MS. Its native ultrastructure was observed by the use of transmission electron microscopy. Denaturation of MOMP was performed in urea at 65 degrees C followed by dialysis against 100 mM acetic acid, and was assessed by CD analysis. MOMP refolding reached a maximum efficiency in the presence of GroEL (at a MOMP/GroEL molar ratio of 9:1) and ATP. Under these conditions, 95% of denatured MOMP was refolded after a 15 min incubation. This approach represents an alternative method in studies of membrane protein refolding.
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