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R M Pemberton

Publications and source records attributed to R M Pemberton.

21 records · Page 2Linked to original sources

Cytotoxic T cell specificity for respiratory syncytial virus proteins: fusion protein is an important target antigen.

We examined the specificity of BALB/c cytotoxic T (Tc) cells for respiratory syncytial virus (RSV) components, using recombinant vaccinia viruses (VV) coding for several individual RSV proteins. We found that immunization with the different VVs yielded the following Tc memory cell populations: high levels of RSV-specific Tc cells were induced with the fusion protein VV, but low levels were induced with VV coding for the RSV nucleoprotein. Tc cell recognition of attachment glycoprotein, part of the matrix molecule or 1A internal protein was poor. While high levels of fusion protein-specific Tc cells were induced by the fusion protein VV, they showed poor cross-reactivity between the A2 and 8/60 RSV strains compared with Tc cells primed by RSV infection.

Animals↗

Amantadine resistance in clinical influenza A (H3N2) and (H1N1) virus isolates.

Thirty-nine influenza A (H1N1) and (H3N2) virus isolates were examined for their susceptibility to amantadine in allantois-on-shell (AOS) cultures. A range of susceptibilities was found when isolates were titrated in the presence of 2.5 mg/l amantadine. Further titration of resistant isolates at 25 mg/l revealed one isolate which remained totally resistant at this higher concentration. A series of cloned viruses was derived from this resistant isolate, and one other partially resistant isolate, by limiting dilution AOS passage in the absence of amantadine. When these were titrated in the presence of 25 mg/l amantadine, a heterogeneity of amantadine-resistance phenotypes was observed in both sets of virus clones. Finally, chronological ordering of clinical isolates and reference strains tested in this study suggests a higher incidence of amantadine resistance amongst more recent influenza A virus isolates.

Amantadine↗

Morphology and antigenicity studies on reassortant influenza (H3N2) viruses for use in inactivated vaccines.

Three influenza A (H3N2) reassortant whole virus vaccine strains with differing antibody-inducing capacities in hamsters were investigated morphologically and antigenically. Although initial measurements of virion circumference, from electron micrographs of vaccine preparations, suggested a relationship of small virion size with low immunogenicity, subsequent immunization with, and morphological investigation of, vaccine virions separated on sucrose gradients, failed to obtain populations whose antibody-inducing capacity clearly correlated with constituent virion density, size, morphology or integrity. However, antigenic investigation using single radial haemolysis (SRH) and monoclonal antibodies revealed significant differences in antigenic specificity between the strains. Furthermore, a series of H3N2 isolates, derived using standard reassortment procedures, also showed differences in antigenic specificity in their haemagglutination-inhibition (HI) reactions with monoclonal antibodies after five passages in allantois-on-shell cultures. Variation between these isolates and their A/Victoria parent virus could be detected using SRH and hamster sera raised against each isolate. These results demonstrate variation between candidate influenza A virus vaccine strains, all possessing the same surface (H3N2) glycoproteins, expressed as a consequence of the reassortant system used for their production.

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