ArticleThe Biochemical journal2004
Functional analysis of the CXXC motif using phage antibodies that cross-react with protein disulphide-isomerase family proteins.
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 7 papers.
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Who cites it
7 citing papers in PubMed, 26 citations in OpenAlex.
- Evolutionary Aspects of Selenium Binding Protein (SBP).Journal of molecular evolution · 2023Article
- Identification and functional analysis of cadmium-binding protein in the visceral mass of Crassostrea gigas.Scientific reports · 2021Article
- Quantitative Analyses of the Yeast Oxidative Protein Folding PathwayAntioxidants & redox signaling · 2019Article
- Conserved Residues LysFrontiers in molecular biosciences · 2018Article
- Protein disulfide isomerase in thrombosis and vascular inflammation.Journal of thrombosis and haemostasis : JTH · 2013Review
- Article
- Identification and enzymatic activities of four protein disulfide isomerase (PDI) isoforms of Leishmania amazonensis.Parasitology research · 2008Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Polyclonal antibodies that had been raised against particular PDI (protein disulphide-isomerase) family proteins did not cross-react with other PDI family proteins. To evade immune tolerance to the important self-motif Cys-Xaa-Xaa-Cys, which is present in PDI family proteins, we used the phage display library [established by Griffiths, Williams, Hartley, Tomlinson, Waterhouse, Crosby, Kontermann, Jones, Low, Allison et al. (1994) EMBO J. 13, 3245-3260] to isolate successfully the phage antibodies that can cross-react with human and bovine PDIs, human P5, human PDI-related protein and yeast PDI. By measuring the binding of scFv (single-chain antibody fragment of variable region) to synthetic peptides and to mutants of PDI family proteins in a surface plasmon resonance apparatus, we identified clones that recognized sequences containing the CGHC motif or the CGHCK sequence. By using the isolated phage antibodies, we demonstrated for the first time that a lysine residue following the CXXC motif significantly increases the isomerase activities of PDI family proteins. Moreover, we demonstrated that the affinity of isolated scFvs for mutant PDI family proteins is proportional to the isomerase activities of their active sites.
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