Role of N-linked glycosylation of the Hendra virus fusion protein |
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Authors: | Carter James Richard Pager Cara Theresia Fowler Stephen Derrick Dutch Rebecca Ellis |
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Institution: | Department of Molecular and Cellular Biochemistry University of Kentucky, 800 Rose Street, UKMC MN606 Lexington, KY 40536-0298, USA. |
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Abstract: | The Hendra virus fusion (F) protein contains five potential sites for N-linked glycosylation in the ectodomain. Examination of F protein mutants with single asparagine-to-alanine mutations indicated that two sites in the F(2) subunit (N67 and N99) and two sites in the F(1) subunit (N414 and N464) normally undergo N-linked glycosylation. While N-linked modification at N414 is critical for protein folding and transport, F proteins lacking carbohydrates at N67, N99, or N464 remained fusogenically active. As N464 lies within heptad repeat B, these results contrast with those seen for several paramyxovirus F proteins. |
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