Identification of regions on the fusion protein of human parainfluenza virus type 2 which are required for haemagglutinin-neuraminidase proteins to promote cell fusion.

Tsurudome, Masato; Ito, Morihiro; Nishio, Machiko; Kawano, Mitsuo; Okamoto, Kousuke; Kusagawa, Shigeru; Komada, Hiroshi; Ito, Yasuhiko

doi:10.1099/0022-1317-79-2-279

Cited by 40 publications

(44 citation statements)

References 44 publications

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“…The MuV HN mutant E105L was not affected in its ability to activate MuV F, but the mutant lost its ability to activate PIV5 F. On the other hand, the mutation of the corresponding residue of PIV5 HN (D88) had no effect on activation of PIV5 F. Notably, a negatively charged residue is present across all rubulavirus HN proteins that are known be involved in heterotypic paramyxovirus F-HN interactions (Fig. 3A), such as hPIV2 HN being able to substitute for hPIV4a HN or SV41 HN and MuV HN being able to substitute for hPIV2 HN (68,69). However, for NDV HN (an avulavirus), the corresponding residue (L97) was found to be important for F activation, and the NDV HN L97A mutant maintained its ability to interact with NDV F (62).…”

Section: Discussionmentioning

confidence: 99%

Fusion Activation through Attachment Protein Stalk Domains Indicates a Conserved Core Mechanism of Paramyxovirus Entry into Cells

Bose

Song

Jardetzky

et al. 2014

J Virol

113

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Paramyxoviruses are a large family of membrane-enveloped negative-stranded RNA viruses causing important diseases in humans and animals. Two viral integral membrane glycoproteins (fusion [F] and attachment [HN, H, or G]) mediate a concerted process of host receptor recognition, followed by the fusion of viral and cellular membranes, resulting in viral nucleocapsid entry into the cytoplasm. However, the sequence of events that closely links the timing of receptor recognition by HN, H, or G and the "triggering" interaction of the attachment protein with F is unclear. F activation results in F undergoing a series of irreversible conformational rearrangements to bring about membrane merger and virus entry. By extensive study of properties of multiple paramyxovirus HN proteins, we show that key features of F activation, including the F-activating regions of HN proteins, flexibility within this F-activating region, and changes in globular head-stalk interactions are highly conserved. These results, together with functionally active "headless" mumps and Newcastle disease virus HN proteins, provide insights into the F-triggering process. Based on these data and very recently published data for morbillivirus H and henipavirus G proteins, we extend our recently proposed "stalk exposure model" to other paramyxoviruses and propose an "induced fit" hypothesis for F-HN/H/G interactions as conserved core mechanisms of paramyxovirus-mediated membrane fusion. HN, H, or G]) mediate a concerted process of host receptor recognition, followed by the fusion of viral and cellular membranes. We describe here the molecular mechanism by which HN activates the F protein such that virus-cell fusion is controlled and occurs at the right time and the right place. We extend our recently proposed "stalk exposure model" first proposed for parainfluenza virus 5 to other paramyxoviruses and propose an "induced fit" hypothesis for F-HN/H/G interactions as conserved core mechanisms of paramyxovirusmediated membrane fusion. IMPORTANCE Paramyxoviruses are a large family of membrane-enveloped negative-stranded RNA viruses causing important diseases in humans and animals. Two viral integral membrane glycoproteins (fusion [F] and attachment [

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Section: Discussionmentioning

confidence: 99%

Fusion Activation through Attachment Protein Stalk Domains Indicates a Conserved Core Mechanism of Paramyxovirus Entry into Cells

Bose

Song

Jardetzky

et al. 2014

J Virol

113

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“…Analysis of several different chimeric HN proteins showed that specificity for the homologous F protein is determined by the stalk region of the HN spike (8,11,44,51,53). Similarly, analysis of chimeric F proteins indicated that specificity for the homologous HN/H protein is determined by the N-terminal half of the cysteine-rich domain in F and/or the heptad repeat closest to the membrane in the stalk of F (50,55).…”

Section: Discussionmentioning

confidence: 99%

Addition of N-Glycans in the Stalk of the Newcastle Disease Virus HN Protein Blocks Its Interaction with the F Protein and Prevents Fusion

Melanson

Iorio

2006

J Virol

111

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“…Introduction of mutation-generating synthetic oligonucleotides into the target recombinant plasmid was performed by using the U.S.E. Mutagenesis Kit (Amersham Pharmacia Biotech AB, Uppsala, Sweden) as specified by the manufacturer, as described previously (28,50).…”

Section: Cellsmentioning

confidence: 99%

“…In support of this idea, it has been demonstrated that homotypic HN and F proteins are physically associated with each other in the virus-infected cells or in the plasmid-transfected cells (11,44,58). Furthermore, analyses using chimeric proteins have indicated that the HN-F interaction may take place between the stalk region of the HN protein (10,12,46,51) and the middle region (including the HR3 domain and part of the cysteine-rich domain) of F1 (50). However, the mechanism by which the HN protein promotes the fusing function of the F protein and triggers the conformational change of the F protein is still unclear.…”

mentioning

confidence: 99%

Hemagglutinin-Neuraminidase-Independent Fusion Activity of Simian Virus 5 Fusion (F) Protein: Difference in Conformation between Fusogenic and Nonfusogenic F Proteins on the Cell Surface

Tsurudome

Ito

Nishio

et al. 2001

J Virol

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The subfamily Paramyxovirinae of the family Paramyxoviridae contains three genera, Respirovirus, Rubulavirus, and Morbillivirus (9, 31, 40). Two kinds of glycoproteins, hemagglutinin-neuraminidase (HN) and fusion (F) protein, are inserted in the viral envelope of the members of the genera Respirovirus and Rubulavirus. The HN protein is responsible for binding to sialic acid-containing cellular molecules and for enzymatic cleavage of the sialoconjugate, while the F protein is involved in envelope-to-cell and cell-to-cell fusion (cell fusion) (9, 31).The F protein is activated from a precursor (F0) when cleaved by cellular protease(s) and forms a disulfide-bonded subunit structure consisting of F1 and F2, which is a prerequisite for the fusion process (22,42). The well-conserved hydrophobic domain (fusion peptide) at the amino terminus of F1 is exposed by the cleavage (25,29) and is considered likely to be directly involved in the fusion event (17, 37). The cleavage also results in a conformational change of the F protein (13,25,29,54). Three heptad repeat (HR) domains are found in the F1 ectodomain (6, 18). The HR1 domain is immediately next to the carboxyl terminus of the fusion peptide, while the HR2 domain is close to the transmembrane domain. The HR3 domain is located between the FR1 and HR2 domains (18) and is followed by a highly conserved stretch of eight cysteine residues (the cysteine-rich domain) (6). Crystallographic analyses have shown that polypeptide fragments representing the

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Identification of regions on the fusion protein of human parainfluenza virus type 2 which are required for haemagglutinin-neuraminidase proteins to promote cell fusion.

Cited by 40 publications

References 44 publications

Fusion Activation through Attachment Protein Stalk Domains Indicates a Conserved Core Mechanism of Paramyxovirus Entry into Cells

Fusion Activation through Attachment Protein Stalk Domains Indicates a Conserved Core Mechanism of Paramyxovirus Entry into Cells

Addition of N-Glycans in the Stalk of the Newcastle Disease Virus HN Protein Blocks Its Interaction with the F Protein and Prevents Fusion

Hemagglutinin-Neuraminidase-Independent Fusion Activity of Simian Virus 5 Fusion (F) Protein: Difference in Conformation between Fusogenic and Nonfusogenic F Proteins on the Cell Surface

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