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- W4296502103 endingPage "102403" @default.
- W4296502103 startingPage "102403" @default.
- W4296502103 abstract "Trypanosomes cause the devastating disease trypanosomiasis, in which the action of trans-sialidase (TS) enzymes harbored on their surface is a key virulence factor. TS enzymes are N-glycosylated, but the biological functions of their glycans have remained elusive. In this study, we investigated the influence of N-glycans on the enzymatic activity and structural stability of TconTS1, a recombinant TS from the African parasite Trypanosoma congolense. We expressed the enzyme in Chinese hamster ovary Lec1 cells, which produce high-mannose type N-glycans similar to the TS N-glycosylation pattern in vivo. Our MALDI-TOF mass spectrometry data revealed that up to eight putative N-glycosylation sites were glycosylated. In addition, we determined that N-glycan removal via endoglycosidase Hf treatment of TconTS1 led to a decrease in substrate affinity relative to the untreated enzyme but had no impact on the conversion rate. Furthermore, we observed no changes in secondary structure elements of hypoglycosylated TconTS1 in CD experiments. Finally, our molecular dynamics simulations provided evidence for interactions between monosaccharide units of the highly flexible N-glycans and some conserved amino acids located at the catalytic site. These interactions led to conformational changes, possibly enhancing substrate accessibility and enzyme-substrate complex stability. The here-observed modulation of catalytic activity via N-glycans represents a so-far-unknown structure-function relationship potentially inherent in several members of the TS enzyme family." @default.
- W4296502103 created "2022-09-21" @default.
- W4296502103 creator A5029370722 @default.
- W4296502103 creator A5034922405 @default.
- W4296502103 creator A5051745954 @default.
- W4296502103 creator A5057938346 @default.
- W4296502103 creator A5061433578 @default.
- W4296502103 creator A5070167637 @default.
- W4296502103 creator A5074413996 @default.
- W4296502103 date "2022-10-01" @default.
- W4296502103 modified "2023-10-16" @default.
- W4296502103 title "N-glycosylation modulates enzymatic activity of Trypanosoma congolense trans-sialidase" @default.
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