The fusion and hemagglutinin-neuraminidase glycoproteins of human parainfluenza virus 3 are both required for fusion

Sn, Ebata; Mj, Côté; Kang, C. Yong; Dimock, Kenneth

doi:10.1016/0042-6822(91)90162-5

Cited by 69 publications

(45 citation statements)

References 25 publications

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“…Evidence from a number of recent studies suggests that HN, in addition to F protein, is required for the induction of fusion by paramyxoviruses (Sakai & Shibuta, 1989;Ebata et al, 1991 ;Morrison et al, 1991 ;Moscona & Peluso, 199 I), although there is also evidence to the contrary (Markwell et al, 1985;Paterson et al, 1985;Olmstead et al, 1986;Alkhatib et al, 1990). The reasons for the discrepancy in the findings of these groups is unclear, but our data are consistent with H N being required for the induction of cell fusion and apparently for more than merely bringing the two membranes into close proximity to one another.…”

Section: Discussionmentioning

confidence: 99%

Inhibition of fusion by neutralizing monoclonal antibodies to the haemagglutinin-neuraminidase glycoprotein of Newcastle disease virus

Iorio

Glickman²,

Sheehan³

1992

Journal of General Virology

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The majority of neutralizing monoclonal antibodies (MAbs) to the haemagglutinin-neuraminidase (HN) glycoprotein of Newcastle disease virus prevent attachment of the virus to cellular receptors and inhibits virion-induced fusion from without (FFWO) and fusion from within (FFWI) mediated by the virus glycoprotein-laden infected cell surface. For these antibodies, the inhibition of fusion is presumed to be the result of the prevention of HN-mediated bridging of potential fusion partners. MAbs against antigenic sites 3 and 4 neutralize virus infectivity, but by a mechanism other than the prevention of attachment, the exact nature of which remains to be established. Antibodies to both of these sites effectively inhibit virion-induced FFWO, even when the inducing virus is not infectious. This is consistent with the mechanism of neutralization of these MAbs involving the inhibition of an early, post-attachment step in infection. MAbs to site 3 also inhibit FFWI, but those to site 4 do not, even when added at high concentrations. This suggests that the requirement for HN may be different in the two modes of fusion. The epitopes recognized by MAbs to sites 3 and 4 have been delineated by the identification of individual nucleotide substitutions in the HN genes of neutralization escape variants. Some of the deduced amino acid substitutions result in additional N-linked glycosylation sites in HN, which are utilized and presumably account for the escape from neutralization.

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Section: Discussionmentioning

confidence: 99%

Inhibition of fusion by neutralizing monoclonal antibodies to the haemagglutinin-neuraminidase glycoprotein of Newcastle disease virus

Iorio

Glickman²,

Sheehan³

1992

Journal of General Virology

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“…Although the F protein seems to play a pivotal role in cell fusion, accumulated data suggest that a promoting function of the homologous HN protein is required for cell fusion by human parainfluenza virus type 2 (PIV-2) (Hu et al, 1992), PIV-3 (Ebata et al, 1991), bovine PIV-3 (Sakai & Shibuta, 1989), PIV-4A (Nishio et al, 1994), mumps virus (MuV) (Tanabayashi et al, 1992), Newcastle disease virus (NDV) (Morrison et al, 1991), simian virus 5 (SV-5) (Heminway et al, 1994), SV-41 (Tsurudome et al, 1995) and PIV-1\Sendai virus (Bousse et al, 1994). Therefore, it has been supposed that a virus typespecific functional interaction between homologous HN and F proteins takes place during the fusion process (Heminway et al,Fig.…”

Section: Introductionmentioning

confidence: 99%

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

Ito

Nishio

et al. 1998

Journal of General Virology

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“…Alternatively, it has been shown that the coexpression of the HA and F proteins was necessary for cell fusion [5,13,20,26,27,29]. Consequently, several models have been suggested that the HA protein was significant in triggering cell fusion [18,27].…”

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confidence: 99%

The Nucleotide and Predicted Amino Acid Sequence of the Fusion Protein of Recent Isolates of Canine Distemper Virus in Japan.

Iwatsuki

Miyashita

Yoshida

et al. 1998

The Journal of Veterinary Medical Science

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ABSTRACT. Analysis of the molecular properties of fusion (F) proteins of field isolates of canine distemper virus (CDV) by immunoprecipitation analysis revealed an identical molecular mass of F protein of 3 field isolates as well as the Onderstepoort laboratory strain. Sequencing showed that the F gene of a field isolate (the Yanaka strain) shared 90.1% and 95.7% identities with the Onderstepoort strain at nucleotide and amino acid levels, respectively. All of the 13 cysteine residues and 4 potential asparagine-linked glycosylation sites were completely conserved amongst these strains. These results indicate that the F proteins is much less heterogeneous than that observed in the hemagglutinin proteins of CDV.-KEY WORDS: CDV, field isolate, fusion protein.

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The fusion and hemagglutinin-neuraminidase glycoproteins of human parainfluenza virus 3 are both required for fusion

Cited by 69 publications

References 25 publications

Inhibition of fusion by neutralizing monoclonal antibodies to the haemagglutinin-neuraminidase glycoprotein of Newcastle disease virus

Inhibition of fusion by neutralizing monoclonal antibodies to the haemagglutinin-neuraminidase glycoprotein of Newcastle disease virus

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

The Nucleotide and Predicted Amino Acid Sequence of the Fusion Protein of Recent Isolates of Canine Distemper Virus in Japan.

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