Role of basic residues in the proteolytic activation of Sendai virus fusion glycoprotein

Heminway, B. R.; Yu, Yang; Tanaka, Yoshikazu; Panin, Milita; Huang, Yung T.; Galinski, Mark S.

doi:10.1016/0168-1702(94)00102-i

Cited by 6 publications

(8 citation statements)

References 38 publications

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“…Alternatively, the insertion of cleavage site I may alter the local structure of the F SeV proteolytic processing region, thereby facilitating the projection of cleavage site II (KKRKRR) from the surface of the F prefusion structure to bind to target cell GAGs. This hypothesis is supported by previous findings which suggest that the sequence surrounding the F SeV cleavage site is important for fusion (13).…”

Section: Discussionsupporting

confidence: 81%

Insertion of the Two Cleavage Sites of the Respiratory Syncytial Virus Fusion Protein in Sendai Virus Fusion Protein Leads to Enhanced Cell-Cell Fusion and a Decreased Dependency on the HN Attachment Protein for Activity

Rawling

Garcı́a-Barreno

Melero

2008

J Virol

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Section: Discussionsupporting

confidence: 81%

Insertion of the Two Cleavage Sites of the Respiratory Syncytial Virus Fusion Protein in Sendai Virus Fusion Protein Leads to Enhanced Cell-Cell Fusion and a Decreased Dependency on the HN Attachment Protein for Activity

Rawling

Garcı́a-Barreno

Melero

2008

J Virol

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“…F16 may have the advantage of not only blocking virus-GAG interactions but may also contain sufficient hydrophobic finger sequence to inhibit membrane insertion events and interactions with Rho-A that are thought to be essential for virus-membrane fusion (50,51). Along these lines, it is also possible that extracellular proteases removed the basic residues from the carboxy terminus of RSV-F 2 , as is the case for fusion proteins of virulent strains of Sendai and Newcastle disease virus (28,49,60). Therefore, attachment and infectivity would not be mediated by interactions between GAGs and the region represented by peptides F15 and F78, because this portion of the protein may be missing in the mature, fully processed virion, and as a result F15 and F78 would not be effective inhibitors.…”

Section: Discussionmentioning

confidence: 99%

Identification of Linear Heparin-Binding Peptides Derived from Human Respiratory Syncytial Virus Fusion Glycoprotein That Inhibit Infectivity

Crim

Audet

Feldman

et al. 2007

J Virol

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“…To investigate whether the mutational effects of the HRA residues were influenced by extracellular cleavage, we generated an SeV F protein in which its cleavage site was mutated to R-Q-K-R (designated Fcl) (see Materials and Methods), which is similar to another SeV F protein construct that is intracellularly cleaved (26). The 10 HRA mutations that did not previously eliminate cell surface expression ( Fig.…”

Section: The Hra Mutations Dramatically Alter the Fusogenicity Of Thementioning

confidence: 99%

Spring-Loaded Heptad Repeat Residues Regulate the Expression and Activation of Paramyxovirus Fusion Protein

Luque

Russell

2007

J Virol

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During viral entry, the paramyxovirus fusion (F) protein fuses the viral envelope to a cellular membrane. Similar to other class I viral fusion glycoproteins, the F protein has two heptad repeat regions (HRA and HRB) that are important in membrane fusion and can be targeted by antiviral inhibitors. Upon activation of the F protein, HRA refolds from a spring-loaded, crumpled structure into a coiled coil that inserts a hydrophobic fusion peptide into the target membrane and binds to the HRB helices to form a fusogenic hairpin. To investigate how F protein conformational changes are regulated, we mutated in the Sendai virus F protein a highly conserved 10-residue sequence in HRA that undergoes major structural changes during protein refolding. Nine of the 15 mutations studied caused significant defects in F protein expression, processing, and fusogenicity. Conversely, the remaining six mutations enhanced the fusogenicity of the F protein, most likely by helping spring the HRA coil. Two of the residues that were neither located at "a" or "d" positions in the heptad repeat nor conserved among the paramyxoviruses were key regulators of the folding and fusion activity of the F protein, showing that residues not expected to be important in coiled-coil formation may play important roles in regulating membrane fusion. Overall, the data support the hypothesis that regions in the F protein that undergo dramatic changes in secondary and tertiary structure between the prefusion and hairpin conformations regulate F protein expression and activation.

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Role of basic residues in the proteolytic activation of Sendai virus fusion glycoprotein

Cited by 6 publications

References 38 publications

Insertion of the Two Cleavage Sites of the Respiratory Syncytial Virus Fusion Protein in Sendai Virus Fusion Protein Leads to Enhanced Cell-Cell Fusion and a Decreased Dependency on the HN Attachment Protein for Activity

Insertion of the Two Cleavage Sites of the Respiratory Syncytial Virus Fusion Protein in Sendai Virus Fusion Protein Leads to Enhanced Cell-Cell Fusion and a Decreased Dependency on the HN Attachment Protein for Activity

Identification of Linear Heparin-Binding Peptides Derived from Human Respiratory Syncytial Virus Fusion Glycoprotein That Inhibit Infectivity

Spring-Loaded Heptad Repeat Residues Regulate the Expression and Activation of Paramyxovirus Fusion Protein

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