Preparation and properties of recombinant Clostridium ramosum IgA proteinase. Isolation of Fc-SC and Fab fragments of human secretory IgA
Jazyk angličtina Země Spojené státy americké Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
33895263
DOI
10.1016/j.pep.2021.105891
PII: S1046-5928(21)00074-7
Knihovny.cz E-zdroje
- Klíčová slova
- Clostridium ramosum, Enzymatic activity, IgA proteinase, Storage conditions,
- MeSH
- bakteriální proteiny chemie genetika MeSH
- Firmicutes enzymologie genetika MeSH
- imunoglobulin A sekreční chemie MeSH
- imunoglobuliny - Fab fragmenty * chemie izolace a purifikace MeSH
- imunoglobuliny - Fc fragmenty * chemie izolace a purifikace MeSH
- lidé MeSH
- proteasy chemie genetika MeSH
- rekombinantní proteiny chemie genetika MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- bakteriální proteiny MeSH
- imunoglobulin A sekreční MeSH
- imunoglobuliny - Fab fragmenty * MeSH
- imunoglobuliny - Fc fragmenty * MeSH
- proteasy MeSH
- rekombinantní proteiny MeSH
Immunoglobulin A (IgA) proteinase from Clostridium ramosum is the enzyme which cleaves IgA of both subclasses; in contrast, the other bacterial proteinases cleave only IgA1 proteins. Previous reports characterized the activity of proteinase naturally secreted by C. ramosum specific for the normal human serum IgA of IgA1 and IgA2m(1) subclasses and also for secretory IgA (SIgA). Its amino acid sequence was determined, and the recombinant proteinase which cleaved IgA of both subclasses was prepared. Here we report the optimized expression, purification, storage conditions and activity testing against purified human milk SIgA. The recombinant C. ramosum IgA proteinase isolated in the high degree of purity exhibited almost complete cleavage of SIgA of both subclasses. The proteinase remained active upon storage for more than 10 month at -20 °C without substantial loss of enzymatic activity. Purified SIgA fragments are suitable for studies of all antigen-binding and Fc-dependent functions of SIgA involved in the protection against infections with mucosal pathogens.
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