Journal
JOURNAL OF VIROLOGY
Volume 79, Issue 12, Pages 7922-7925Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.79.12.7922-7925.2005
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Funding
- NIAID NIH HHS [R01 AI051517] Funding Source: Medline
- PHS HHS [A151517] Funding Source: Medline
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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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