Epitope mapping of Borrelia burgdorferi OspC protein in homodimeric fold
Jazyk angličtina Země Spojené státy americké Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
28142214
PubMed Central
PMC5368064
DOI
10.1002/pro.3125
Knihovny.cz E-zdroje
- Klíčová slova
- Borrelia burgdorferi, OspC, epitope mapping, immunoprecipitation, monoclonal antibody, outer surface protein C, protein alignment,
- MeSH
- antigeny bakteriální chemie genetika imunologie MeSH
- Borrelia burgdorferi chemie genetika imunologie MeSH
- mapování epitopu * MeSH
- multimerizace proteinu * MeSH
- myši inbrední BALB C MeSH
- myší monoklonální protilátky chemie imunologie MeSH
- myši MeSH
- proteiny vnější bakteriální membrány chemie genetika imunologie MeSH
- sbalování proteinů MeSH
- zvířata MeSH
- Check Tag
- myši MeSH
- ženské pohlaví MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- antigeny bakteriální MeSH
- myší monoklonální protilátky MeSH
- OspC protein MeSH Prohlížeč
- proteiny vnější bakteriální membrány MeSH
In current work, we used recombinant OspC protein derived from B. afzelii strain BRZ31 in the native homodimeric fold for mice immunization and following selection process to produce three mouse monoclonal antibodies able to bind to variable parts of up to five different OspC proteins. Applying the combination of mass spectrometry assisted epitope mapping and affinity based theoretical prediction we have localized regions responsible for antigen-antibody interactions and approximate epitopes' amino acid composition. Two mAbs (3F4 and 2A9) binds to linear epitopes located in previously described immunogenic regions in the exposed part of OspC protein. The third mAb (2D1) recognises highly conserved discontinuous epitope close to the ligand binding domain 1.
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