Antigenic Characterization of the Nucleoprotein and Matrix Protein of Influenza C Virus with Monoclonal Antibodies

Sugawara, Kanetsu; Nishimura, Hidekazu; Hongō, Seiji; Kitame, Fumio; Nakamura, Kenzo

doi:10.1099/0022-1317-72-1-103

Cited by 36 publications

(33 citation statements)

References 43 publications

(31 reference statements)

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“…The latter finding provided evidence for the requirement of nuclear function for influenza C virus replication. In addition, the association of M1 with the nucleoli was observed in the C/Yamagata/1/88-infected cells, a phenomenon that remains to be elucidated with respect to viral replication (Sugawara et al, 1991).…”

Section: Characteristics Of the M1 And Cm2 Proteins 31 M1 Proteinmentioning

confidence: 96%

“…Furthermore, Yokota et al identified the M1 protein synthesized in C/Ann Arbor/1/50-infected MDCK cells (Yokota et al, 1981). To characterize the protein, the monoclonal antibodies against M1 have been produced (Sugawara et al, 1991). Using a panel of the nine MAbs against M1, the M1 protein was shown to contain two non-overlapping antigenic regions that are highly resistant to conformational changes, and to exhibit no antigenic variations among 23 influenza C virus strains isolated over 41 year period.…”

Section: Characteristics Of the M1 And Cm2 Proteins 31 M1 Proteinmentioning

confidence: 99%

“…HEF, which has receptor-binding, receptor-destroying and fusion activities, forms a spike on the virion (Herrler & Klenk, 1991). NP participates in forming ribonucleoproteins (RNPs) with viral RNA (vRNA), PB2, PB1 and P3 (Crescenzo-Chaigne et al, 1999;Crescenzo-Chaigne & van der Werf, 2001;Nakada et al, 1984;Sugawara et al, 1991;. M1 is abundantly present beneath the envelope, which gives rigidity to the virion.…”

Section: Introductionmentioning

confidence: 99%

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Influenza C Virus: Structure and Function of M Gene and Its Products

Muraki¹

2012

Molecular Virology

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Section: Characteristics Of the M1 And Cm2 Proteins 31 M1 Proteinmentioning

confidence: 96%

Section: Characteristics Of the M1 And Cm2 Proteins 31 M1 Proteinmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Influenza C Virus: Structure and Function of M Gene and Its Products

Muraki¹

2012

Molecular Virology

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“…Their specificity was confirmed by radioimmunoprecipitation using lysates of [aSS]methionine-labelled HMV-II cells infected with C/AA/50 or C/MS/80 as antigens as described by Sugawara et al (1991) …”

mentioning

confidence: 99%

“…MAbs against the HE protein of C/AA/50 or C/Mississippi/I/80 (C/MS/80) virus were produced according to methods of Hongo et al (1986) and Sugawara et al (1991). Their specificity was confirmed by radioimmunoprecipitation using lysates of [aSS]methionine-labelled HMV-II cells infected with C/AA/50 or C/MS/80 as antigens as described by Sugawara et al (1991) …”

mentioning

confidence: 99%

Construction of an antigenic map of the haemagglutinin-esterase protein of influenza C virus

Sugawara

Nishimura

Hongō

et al. 1993

Journal of General Virology

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Four different antigenic sites (A-l, A-2, B-I, B-2) have been identified previously on the haemagglutininesterase (HE) glycoprotein of influenza C/Ann Arbor/I/50 virus with seven monoclonal antibodies (MAbs). In this study we produced 30 additional anti-HE MAbs, nine of which demonstrated at least one of the following activities: haemagglutination inhibition, receptor-destroying enzyme inhibition, haemolysis inhibition, and neutralization (group A). The remaining had none of these activities (group B). These antibodies, and those previously isolated, were used to construct a more complete antigenic map of the HE molecule.Operational and topological analyses showed that a minimum of nine non-overlapping or partially overlapping antigenic sites were present on the HE protein, five recognized by group A MAbs (A-1 to A-5) and four by group B (B-1 to B-4). Among these antigenic sites, site A-5 was unique in that MAbs to this site inhibited the receptor-destroying activity without influencing the receptor-binding activity, which supports the idea that the sites responsible for these two functions are separate. It was also found that several group B MAbs were crossreactive with host cell antigens.

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Role of Individual Oligosaccharide Chains in Antigenic Properties, Intracellular Transport, and Biological Activities of Influenza C Virus Hemagglutinin-Esterase Protein

et al. 2001

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The hemagglutinin-esterase (HE) glycoprotein of influenza C virus is composed of three domains: a stem domain active in membrane fusion (F), an acetylesterase domain (E), and a receptor-binding domain (R). The protein contains eight N-linked glycosylation sites, four (positions 26, 395, 552, and 603) in the F domain, three (positions 61, 131, and 144) in the E domain, and one (position 189) in the R domain. Here, we investigated the role of the individual oligosaccharide chains in antigenic properties, intracellular transport, and biological activities of the HE protein by eliminating each of the glycosylation sites by site-specific mutagenesis. Comparison of electrophoretic mobility between the wild-type and the mutant proteins showed that while seven of the glycosylation sites are used, one (position 131) is not. Analysis of reactivity of the mutants with anti-HE monoclonal antibodies demonstrated that glycosylation at position 144 is essential for the formation of conformation-dependent epitopes. It was also evident that glycosylation at the two sites in the F domain (positions 26 and 603), in addition to that in the E domain (position 144), is required for the HE molecule to be transported from the endoplasmic reticulum and that mutant HEs lacking one of these three sites failed to undergo the trimer assembly. Removal of an oligosaccharide chain at position 144 or 189 resulted in a decrease in the esterase activity. By contrast, two mutants lacking an oligosaccharide chain at position 26 or 603, which were defective not only in cell surface expression but in trimerization, possessed full-enzyme activity, suggesting that the HE monomers present within the cell have acetylesterase activity. Fusion activity of cells expressing each of mutant HEs was found to be comparable with the ability of the protein to be transported to the cell surface, suggesting that there is no specific oligosaccharide chain that plays a critical role in promoting membrane fusion.

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Antigenic Characterization of the Nucleoprotein and Matrix Protein of Influenza C Virus with Monoclonal Antibodies

Cited by 36 publications

References 43 publications

Influenza C Virus: Structure and Function of M Gene and Its Products

Influenza C Virus: Structure and Function of M Gene and Its Products

Construction of an antigenic map of the haemagglutinin-esterase protein of influenza C virus

Role of Individual Oligosaccharide Chains in Antigenic Properties, Intracellular Transport, and Biological Activities of Influenza C Virus Hemagglutinin-Esterase Protein

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