Characterization of neuraminidases from myxoviruses

Drzeniek, R.; Seto, J. T.; Rott, R.

doi:10.1016/0926-6593(66)90015-4

Cited by 110 publications

(30 citation statements)

References 15 publications

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“…It is also intriguing that ~-NA did not modulate transcription (Fig. 4b) since NA is an integral (Drzeniek et al, 1966) and possibly a transmembrane protein (Fields et aL, 1981). However, Fields et al (1981) suggest that the NA of A/PR/8/34 is inserted into the virus envelope in the opposite orientation to HA with its NH 2 terminus projecting into the particle.…”

Section: Discussionmentioning

confidence: 99%

Studies on the Mechanism of Neutralization of Influenza Virus by Antibody: Evidence that Neutralizing Antibody (Anti-haemagglutinin) Inactivates Influenza Virus in vivo by Inhibiting Virion Transcriptase Activity

Possee¹,

Schild²,

Dimmock³

1982

Journal of General Virology

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SUMMARYInfluenza viruses, which had lost up to 99.999% infectivity by incubation with antibody (ix) specific for the haemagglutinin (HA) or with monoclon~1 u-HA, attached on to and penetrated chick embryo fibroblast (CEF) cells to the same extent as non-neutralized virus. Neutralized virus was also uncoated efficiently as shown by the accumulation of virion RNA in the nucleus-and virion envelope in the cytoplasm. Polyacrylamide gel electrophoresis of virion RNA segments recovered from the nucleus or cytoplasm of cells inoculated with neutralized or non-neutralized virus showed that antibody did not potentiate degradation of RNA. However, these RNAs were not expressed since virus-induced proteins were not detected in cells to which neutralized virus had been added. Assay of virion transcriptase of neutralized virus in vitro showed that its activity was reduced up to sevenfold compared with non-neutralized virus, and annealing studies showed that no detectable transcription took place in vivo with neutralized virus. These studies support the conclusion that antibody directed specifically against the HA protein on the outer surface of the influenza virus particle neutralizes infectivity by inactivating virion transcriptase activity and it is suggested that antibody to HA brings about allosteric rearrangements in the HA molecule which are transmitted across the virus envelope to the interior of the particle.

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Section: Discussionmentioning

confidence: 99%

Studies on the Mechanism of Neutralization of Influenza Virus by Antibody: Evidence that Neutralizing Antibody (Anti-haemagglutinin) Inactivates Influenza Virus in vivo by Inhibiting Virion Transcriptase Activity

Possee¹,

Schild²,

Dimmock³

1982

Journal of General Virology

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“…The surface antigens, hemagglutinin and neuraminidase, are glycoproteins coded for by genes 4 and 5 or 6 (depending on the strain), respectively (Palese and Schulman, 1976b;Scholtissek et al, 1976). Although both surface antigens change independently, the hemagglutinin (HA) is the antigen against which neutralizing antibodies are directed (Laver and Kilbourne, 1966;Drzenick, Seto and Rott, 1966). The hemagglutinin is responsible for attachment to virus receptors (Hirst, 1942) and is involved in the initial stages of infection (Lazarowtiz and Choppin, 1975;Klenk et al, 1975).…”

Section: Introductionmentioning

confidence: 99%

Complete structure of the hemagglutinin gene from the human influenza A/Victoria/3/75 (H3N2) strain as determined from cloned DNA

Jou

Verhoeyen

Devos

et al. 1980

Cell

219

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SummaryThe complete sequence of a hemagglutinin (HA) gene of a recent human influenza A strain, A/Victoria/3/75, is 1768 nucleotides long and contains the information for 567 amino acids. It codes for a signal peptide of 16 amino acids, the HA1 chain of the mature hemagglutinin of 329 amino acids, a connecting region between HA1 and HA2 consisting of a single arginine residue and the HA2 portion of 221 amino acids. The sequence is compared with the hemagglutinin of two members of other subtypes, the human H2 strain A/Jap/305/57 and the avian Havl strain A/FPV/Rostock/34, and with one of the same H3 subtype, A/Memphis/3/72. To align the HA1 chain of different major subtypes several deletions/insertions of single amino acids must be invoked, but two more extensive differences are found at both ends, one leading to an extension of the amino terminal sequence of HA1 and the other (four residues) occurring in the region processed away between HA1 and HA2. Comparison of the HA1 of two H3 strains suggests that drift probably depends on single base mutations, some of which change antigenic determinants. The HA2 region, which apparently is not involved in the immune response, is highly conserved even between different subtypes, and single base substitutions account for all the observed diversity. A hydrophobic segment of 24 residues is present in the same position close to the carboxyl terminus of HA2 in both Victoria and FPV, and presumably functions in implantation into the lipid bilayer. The many conserved features not only in HA2 but also in HA1 suggest a rather rigid architecture for the whole hemagglutinin molecule.

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“…For the characterization of Pasteurella multocida neuraminidase it was necessary to detach the enzyme from bacterial cells. Therefore, cells harvested after 66 h of inoculation were treated in different ways and NANA-degradation (%) after incubation at 37 "C for 15 min with Lineweaver & Burk (1934) and plotted (0-0) on the right ordinate and upper abscissa as already described in a previous paper (Drzeniek et al 1966). centrifuged at 31 ooo g for 20 min. The neuraminidase activity of the supernatant was measured.…”

Section: Evidence Of Neuraminidase In Pasteurellamentioning

confidence: 99%