| Autor: |
Heise T; Institute for Molecules and Materials, Radboud University Nijmegen , Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands., Büll C; Department of Radiation Oncology, Radiotherapy & OncoImmunology Laboratory, Radboudumc , Geert Grooteplein Zuid 32, 6525 GA Nijmegen, The Netherlands., Beurskens DM; Department of Biochemistry, Cardiovascular Research Institute Maastricht (CARIM), Maastricht University , Universiteitssingel 50, 6229 ER Maastricht, The Netherlands., Rossing E; Institute for Molecules and Materials, Radboud University Nijmegen , Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands., de Jonge MI; Laboratory of Pediatric Infectious Diseases, Radboud Center for Infectious Diseases, Radboudumc , Geert Grooteplein Zuid 32, 6525 GA Nijmegen, The Netherlands., Adema GJ; Department of Radiation Oncology, Radiotherapy & OncoImmunology Laboratory, Radboudumc , Geert Grooteplein Zuid 32, 6525 GA Nijmegen, The Netherlands., Boltje TJ; Institute for Molecules and Materials, Radboud University Nijmegen , Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands., Langereis JD; Laboratory of Pediatric Infectious Diseases, Radboud Center for Infectious Diseases, Radboudumc , Geert Grooteplein Zuid 32, 6525 GA Nijmegen, The Netherlands. |
| Abstrakt: |
Metabolic incorporation of azide- or alkyne-modified sialic acids into the cellular glycosylation pathway enables the study of sialoglycan expression, localization, and trafficking via bioorthogonal chemistry. Herein, we report that such modifications of the sialic acid sugar can have a profound influence on their hydrolysis by neuraminidases (sialidase). Azidoacetyl (Az)-modified sialic acids were prone to neuraminidase cleavage, whereas propargyloxycarbonyl (Poc)-modified sialic acids were largely resistant to cleavage. Because the influenza virus infection cycle depends on the hydrolysis of host-cell-surface sialic acids, influenza cell-to-cell transmission was strongly reduced in Poc sialic acid glycoengineered host cells. The use of Poc sialic acids may disturb biological processes involving neuraminidase cleavage but also provides perspective for use in applications in which sialic acid hydrolysis is not desired, such as antibody modification, viral infection, etc. |
