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Biochem Biophys Res Commun. 2009 Feb 13;379(3):749-53. Epub 2009 Jan 6.
Active 1918 pandemic flu viral neuraminidase has distinct N-glycan profile and is resistant to trypsin digestion.
Wu ZL, Ethen C, Hickey GE, Jiang W. - R&D Systems, Inc., 614 Mckinley Place NE, Minneapolis, MN 55413, USA. Leon.wu@rndsystems.com
The 1918 pandemic flu virus caused one of the most deadly pandemics in human history. To search for unique structural features of the neuraminidase from this virus that might have contributed to its unusual virulence, we expressed this enzyme.
The purified enzyme appeared as a monomer, a dimer and a tetramer, with only the tetramer being active and therefore biologically relevant.
The monomer and the dimer could not be oligomerized into the tetramer in solution, suggesting that some unique structural features were required for oligomerization and activation.
These features could be related to N-glycosylation, because the tetramer displayed different N-glycans than the monomer and the dimer.
Furthermore, the tetramer was found to be resistant to trypsin digestion, which may give the virus the capability to invade tissues that are normally not infected by influenza viruses and make the virus more robust for infection.
PMID: 19133226 [PubMed - indexed for MEDLINE]
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Active 1918 pandemic flu viral neuraminidase has distinct N-glycan profile and is resistant to trypsin digestion.
Wu ZL, Ethen C, Hickey GE, Jiang W. - R&D Systems, Inc., 614 Mckinley Place NE, Minneapolis, MN 55413, USA. Leon.wu@rndsystems.com
The 1918 pandemic flu virus caused one of the most deadly pandemics in human history. To search for unique structural features of the neuraminidase from this virus that might have contributed to its unusual virulence, we expressed this enzyme.
The purified enzyme appeared as a monomer, a dimer and a tetramer, with only the tetramer being active and therefore biologically relevant.
The monomer and the dimer could not be oligomerized into the tetramer in solution, suggesting that some unique structural features were required for oligomerization and activation.
These features could be related to N-glycosylation, because the tetramer displayed different N-glycans than the monomer and the dimer.
Furthermore, the tetramer was found to be resistant to trypsin digestion, which may give the virus the capability to invade tissues that are normally not infected by influenza viruses and make the virus more robust for infection.
PMID: 19133226 [PubMed - indexed for MEDLINE]
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