scholarly journals C-Terminal Tyrosine Residues Modulate the Fusion Activity of the Hendra Virus Fusion Protein

Biochemistry ◽  
2011 ◽  
Vol 50 (6) ◽  
pp. 945-952 ◽  
Author(s):  
Andreea Popa ◽  
Cara Teresia Pager ◽  
Rebecca Ellis Dutch
2005 ◽  
Vol 79 (12) ◽  
pp. 7922-7925 ◽  
Author(s):  
James Richard Carter ◽  
Cara Theresia Pager ◽  
Stephen Derrick Fowler ◽  
Rebecca Ellis Dutch

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 F2 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.


2012 ◽  
Vol 86 (6) ◽  
pp. 3003-3013 ◽  
Author(s):  
E. C. Smith ◽  
M. R. Culler ◽  
L. M. Hellman ◽  
M. G. Fried ◽  
T. P. Creamer ◽  
...  

2012 ◽  
Vol 86 (6) ◽  
pp. 3014-3026 ◽  
Author(s):  
A. Popa ◽  
J. R. Carter ◽  
S. E. Smith ◽  
L. Hellman ◽  
M. G. Fried ◽  
...  

FEBS Letters ◽  
2014 ◽  
Vol 589 (1) ◽  
pp. 152-158 ◽  
Author(s):  
Yuto Satoh ◽  
Mitsuhiro Hirose ◽  
Hiroko Shogaki ◽  
Hiroshi Wakimoto ◽  
Yoshinori Kitagawa ◽  
...  

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