The hemagglutinin-neuraminidase glycoproteins of human parainfluenza virus type 1 and Sendai virus have high structure-function similarity with limited antigenic cross-reactivity
References (44)
- et al.
Electrophoretic analysis of iodine-labeled influenza virus RNA segments
Anal. Biochem.
(1980) - et al.
Sequence determination of the Sendai virus HN gene and its comparison to the influenza virus glycoproteins
Cell
(1985) - et al.
Monoclonal antibodies to the P Protein of Sendai virus define its structure and role in transcription
Virology
(1985) - et al.
Purification of large double-stranded cDNA fragments
- et al.
Homopolymeric tailing
Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes
Cell
(1986)- et al.
First-strand cDNA synthesis primed with oligo(dT)
- et al.
Synthesis of ds-cDNA involving addition of dCMP tails to allow cloning of 5′-terminal mRNA sequences
- et al.
Molecular cloning and sequence determination of the fusion protein gene of human parainfluenza virus type 1
Virology
(1988) - et al.
Sequence of the hemagglutinin gene from influenza virus A/Seal/Mass/1/80
Virology
(1983)
The HN glycoprotein of Sendai virus: Analysis of site(s) involved in hemagglutinating and neuraminidase activities
Virology
Distinct functions of antigenic sites of the HN glycoprotein of Sendai virus
Virology
Monoclonal antibodies reveal extensive antigenic differences between the hemagglutinin-neuraminidase glycoproteins of human and bovine parainfluenza 3 viruses
Virology
Alterations in the hemagglutinin associated with adaptation of influenza B virus to growth in eggs
Virology
Localization of the functional sites on the HN glycoprotein of Sendai virus by sequence analysis of antigenic and temperature-sensitive mutants
Virology
Influenza virus neuraminidase and neuraminidase-inhibition test procedures
Bull. WH0
Buffer gradient gels and 35S label as an aid to rapid DNA sequence determination
Newly recognized myxoviruses from children with respiratory disease
N. Engl. J. Med.
Parainfluenza viruses
Conserved epitopes on the hemagglutinin-neuraminidase proteins of human and bovine parainfluenza type 3 viruses: Nucleotide sequence analysis of variants selected with monoclonal antibodies
J. Virol.
Antigenic and structural properties of the hemagglutinin-neuraminidase glycoprotein of the human parainfluenza virus type 3: Sequence analysis of variants selected with monoclonal antibodies which inhibit infectivity, hemagglutination, and neuraminidase activities
J. Virol.
Attenuation of bovine parainfluenza virus type 3 in nonhuman primates and its ability to confer immunity to human parainfluenza virus type 3 challenge
J. Infect. Dis.
Cited by (84)
Timing is everything: Fine-tuned molecular machines orchestrate paramyxovirus entry
2015, VirologyCitation Excerpt :In NDV HN and hPIV3 HN, evidence has been presented of a second sialic acid binding site, which lacks neuraminidase activity (Bousse et al., 2004; Mahon et al., 2011; Porotto et al., 2012b; Zaitsev et al., 2004). An atomic structure of the globular head domain of NDV HN from a low virulence (lentogenic) strain (Ulster) (Yuan et al., 2012) showed a longer C-terminal extension (Gorman et al., 1990; Nagai et al., 1976; Sakaguchi et al., 1989) that was found to be involved in auto-inhibition of receptor binding by obscuring both the primary and secondary sialic acid receptor binding sites of NDV HN (Yuan et al., 2012). Proteolytic cleavage of this C-terminal extension is required for receptor binding and fusion in these NDV strains (Yuan et al., 2012).
Sendai virus-based RSV vaccine protects against RSV challenge in an in vivo maternal antibody model
2014, VaccineCitation Excerpt :A study was designed and approved by Institutional Review Boards to collect sera from inpatient infants at Le Bonheur Children's Hospital (Memphis, TN) for testing in RSV-specific and SeV-specific neutralization antibody assays. SeV-specific antibodies are present among maternal antibodies, because most humans are exposed repeatedly to hPIV-1, a virus closely related to SeV [36]. In Table 1 are shown neutralization titers from 14 representative serum samples in age groups 0 to ≤2 months, 2 to ≤4 months, and 4 to ≤6 months.
Distinctive and critical roles for cellular immunity and immune-inflammatory response in the immunopathology of Sendai virus infection in mice
2011, Microbes and InfectionCitation Excerpt :The occurrence of this “cytokine storm” is thought to contribute to the severity of the disease caused by these viruses [3–6]. Sendai virus (SeV) is the murine counterpart of human parainfluenza virus 1 (HPIV1) and these two viruses share high-sequence homology and antigenic cross-reactivity [7,8]. SeV was reported to infect nonhuman primates, and theoretically can cause zoonotic disease in humans [9].
Phenotypes and functions of persistent Sendai virus-induced antibody forming cells and CD8<sup>+</sup> T cells in diffuse nasal-associated lymphoid tissue typify lymphocyte responses of the gut
2011, VirologyCitation Excerpt :Sendai virus (SeV), a natural pathogen of mice (Faisca and Desmecht, 2007) is endemic in many parts of the world, yet there have been no confirmed reports of SeV-mediated disease in humans. Based on sequence homology SeV is closely related to hPIV-1 (McCarthy and Goodman, 2010; Power et al., 1992; Gorman et al., 1990; Lyn et al., 1991). The two viruses are also well related in terms of B and T cell cross-reactivities (Dave et al., 1994; Smith et al., 1994).
Robust IgA and IgG-producing antibody forming cells in the diffuse-NALT and lungs of Sendai virus-vaccinated cotton rats associate with rapid protection against human parainfluenza virus-type 1
2010, VaccineCitation Excerpt :Whereas SeV was originally thought to be the etiologic agent of human disease [6,7], researchers have since determined that it is a pathogen of mice and not of humans [8]. During laboratory studies of SeV, the profound sequence and antigenic similarities between SeV and hPIV-1 were recognized [9–12], as was the potential for SeV to serve as a Jennerian (xenotropic) vaccine for protection against hPIV-1. SeV has been shown to grow transiently in the upper and lower respiratory tract of non-human primates, conferring complete protection against hPIV-1 challenge with no evidence of adverse events [13,14].