TY - JOUR
T1 - Role of N-linked glycosylation of the Hendra virus fusion protein
AU - Carter, James Richard
AU - Pager, Cara Theresia
AU - Fowler, Stephen Derrick
AU - Dutch, Rebecca Ellis
PY - 2005/6
Y1 - 2005/6
N2 - 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 F1 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.
AB - 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 F1 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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U2 - 10.1128/JVI.79.12.7922-7925.2005
DO - 10.1128/JVI.79.12.7922-7925.2005
M3 - Article
C2 - 15919949
AN - SCOPUS:19944415289
SN - 0022-538X
VL - 79
SP - 7922
EP - 7925
JO - Journal of Virology
JF - Journal of Virology
IS - 12
ER -