Direct Evidence that the N-Terminal Heptad Repeat of Sendai Virus Fusion Protein Participates in Membrane Fusion

1999 ◽  
Vol 292 (3) ◽  
pp. 531-546 ◽  
Author(s):  
Jimut Kanti Ghosh ◽  
Yechiel Shai
Keyword(s):  
Fusion Protein ◽  
Membrane Fusion ◽  
Direct Evidence ◽  
Sendai Virus ◽  
Heptad Repeat ◽  
Virus Fusion

scholarly journals Mutation of the TYTLE Motif in the Cytoplasmic Tail of the Sendai Virus Fusion Protein Deeply Affects Viral Assembly and Particle Production

PLoS ONE ◽  
2013 ◽  
Vol 8 (12) ◽  
pp. e78074 ◽  
Author(s):  
Manel Essaidi-Laziosi ◽  
Anastasia Shevtsova ◽  
Denis Gerlier ◽  
Laurent Roux
Keyword(s):  
Fusion Protein ◽  
Particle Production ◽  
Sendai Virus ◽  
Cytoplasmic Tail ◽  
Viral Assembly ◽  
Virus Fusion

scholarly journals An effective strategy for recapitulating N-terminal heptad repeat trimers in enveloped virus surface glycoproteins for therapeutic applications

2016 ◽  
Vol 7 (3) ◽  
pp. 2145-2150 ◽  
Author(s):  
Wenqing Lai ◽  
Chao Wang ◽  
Fei Yu ◽  
Lu Lu ◽  
Qian Wang ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Membrane Fusion ◽  
Heptad Repeat ◽  
Effective Strategy ◽  
Virus Surface ◽  
Efficient Strategy ◽  
Therapeutic Applications ◽  
Enveloped Virus ◽  
Membrane Fusion Protein ◽  
Hiv 1

We report an efficient strategy to recapitulate NHR α-helical trimers in the HIV-1 membrane fusion protein as promising antiviral therapeutics.

scholarly journals A Histidine Switch in Hemagglutinin-Neuraminidase Triggers Paramyxovirus-Cell Membrane Fusion

2008 ◽  
Vol 83 (4) ◽  
pp. 1727-1741 ◽  
Author(s):  
Anuja Krishnan ◽  
Santosh K. Verma ◽  
Prashant Mani ◽  
Rahul Gupta ◽  
Suman Kundu ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Membrane Fusion ◽  
Fusion Proteins ◽  
Sendai Virus ◽  
Biological Activities ◽  
Viral Envelope ◽  
Attachment Protein ◽  
Histidine Residues ◽  
Human Parainfluenza Virus ◽  
Mimicking Peptides

ABSTRACT Most paramyxovirus fusion proteins require coexpression of and activation by a homotypic attachment protein, hemagglutinin-neuraminidase (HN), to promote membrane fusion. However, the molecular mechanism of the activation remains unknown. We previously showed that the incorporation of a monohistidylated lipid into F-virosome (Sendai viral envelope containing only fusion protein) enhanced its fusion to hepatocytes, suggesting that the histidine residue in the lipid accelerated membrane fusion. Therefore, we explored whether a histidine moiety in HN could similarly direct activation of the fusion protein. In membrane fusion assays, the histidine substitution mutants of HN (H247A of Sendai virus and H245A of human parainfluenza virus 3) had impaired membrane fusion promotion activity without significant changes in other biological activities. Synthetic 30-mer peptides corresponding to regions of the two HN proteins containing these histidine residues rescued the fusion promoting activity of the mutants, whereas peptides with histidine residues substituted by alanine did not. These histidine-containing peptides also activated F-virosome fusion with hepatocytes both in the presence and in the absence of mutant HN in the virosome. We provide evidence that the HN-mimicking peptides promote membrane fusion, revealing a specific histidine “switch” in HN that triggers fusion.

scholarly journals Sequence Determination of the Sendai Virus Fusion Protein Gene

1985 ◽  
Vol 66 (2) ◽  
pp. 317-331 ◽  
Author(s):  
B. M. Blumberg ◽  
C. Giorgi ◽  
K. Rose ◽  
D. Kolakofsky
Keyword(s):  
Fusion Protein ◽  
Protein Gene ◽  
Sendai Virus ◽  
Sequence Determination ◽  
Virus Fusion

scholarly journals Functions of the Stem Region of the Semliki Forest Virus Fusion Protein during Virus Fusion and Assembly

2006 ◽  
Vol 80 (22) ◽  
pp. 11362-11369 ◽  
Author(s):  
Maofu Liao ◽  
Margaret Kielian
Keyword(s):  
Fusion Protein ◽  
Membrane Fusion ◽  
Semliki Forest Virus ◽  
Virus Assembly ◽  
Protein A ◽  
Stem Length ◽  
Membrane Fusion Protein ◽  
Virus Fusion ◽  
Target Membrane ◽  
Domain Iii

ABSTRACT Membrane fusion of the alphaviruses is mediated by the E1 protein, a class II virus membrane fusion protein. During fusion, E1 dissociates from its heterodimer interaction with the E2 protein and forms a target membrane-inserted E1 homotrimer. The structure of the homotrimer is that of a trimeric hairpin in which E1 domain III and the stem region fold back toward the target membrane-inserted fusion peptide loop. The E1 stem region has a strictly conserved length and several highly conserved residues, suggesting the possibility of specific stem interactions along the trimer core and an important role in driving membrane fusion. Mutagenesis studies of the alphavirus Semliki Forest virus (SFV) here demonstrated that there was a strong requirement for the E1 stem in virus assembly and budding, probably reflecting its importance in lateral interactions of the envelope proteins. Surprisingly, however, neither the conserved length nor any specific residues of the stem were required for membrane fusion. Although the highest fusion activity was observed with wild-type E1, efficient fusion was mediated by stem mutants containing a variety of substitutions or deletions. A minimal stem length was required but could be conferred by a series of alanine residues. The lack of a specific stem sequence requirement during SFV fusion suggests that the interaction of domain III with the trimer core can provide sufficient driving force to mediate membrane merger.

scholarly journals Role of N-Linked Glycosylation of the Hendra Virus Fusion Protein

2005 ◽  
Vol 79 (12) ◽  
pp. 7922-7925 ◽  
Author(s):  
James Richard Carter ◽  
Cara Theresia Pager ◽  
Stephen Derrick Fowler ◽  
Rebecca Ellis Dutch
Keyword(s):  
Protein Folding ◽  
Fusion Protein ◽  
Hendra Virus ◽  
Heptad Repeat ◽  
F Protein ◽  
Virus Fusion ◽  
Protein Mutants

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.

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