Monoclonal antibody 4B1 influences the p K a of Glu325 in lactose permease (LacY) from Escherichia coli : evidence from SEIRAS
| Autor: | Petra Hellwig, H. Ronald Kaback, Natalia Ermolova, Ana Filipa Santos Seica, Fatima Omeis |
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| Přispěvatelé: | Chimie de la matière complexe (CMC), Université de Strasbourg (UNISTRA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS) |
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
Lactose permease
Biophysics medicine.disease_cause Biochemistry 03 medical and health sciences chemistry.chemical_compound Structural Biology Genetics medicine membrane protein surface-enhanced infrared absorption spectroscopy Binding site Lactose Molecular Biology Escherichia coli 030304 developmental biology 0303 health sciences 030302 biochemistry & molecular biology monoclonal antibody 4B1 Cell Biology Periplasmic space carbohydrates (lipids) chemistry Symporter bacteria Efflux [CHIM.OTHE]Chemical Sciences/Other Conformational epitope |
| Zdroj: | FEBS Letters FEBS Letters, Wiley, 2020, 594 (20), pp.3356-3362. ⟨10.1002/1873-3468.13907⟩ |
| ISSN: | 0014-5793 1873-3468 |
| Popis: | The monoclonal antibody 4B1 binds to a conformational epitope on the periplasmic side of lactose permease (LacY) of Escherichia coli and inhibits H+ /lactose symport and lactose efflux under nonenergized conditions. At the same time, ligand binding and translocation reactions that do not involve net H+ translocation remain unaffected by 4B1. In this study, surface-enhanced infrared absorption spectroscopy applied to the immobilized LacY was used to study the pH-dependent changes in LacY and to access in situ the effect of the 4B1 antibody on the pKa of Glu325, the primary functional H+ -binding site in LacY. A small shift of the pK value from 10.5 to 9.5 was identified that can be corroborated with the inactivation of LacY upon 4B1 binding. |
| Databáze: | OpenAIRE |
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