Comparison of the relative roles of the F and HN surface glycoproteins of the paramyxovirus simian virus 5 in inducing protective immunity

R. G. Paterson, R. A. Lamb, B. Moss, B. R. Murphy

Research output: Contribution to journalArticlepeer-review

32 Scopus citations

Abstract

To compare the relative roles of the paramyxovirus simian virus 5 (SV5) major surface glycoproteins, fusion (F) and hemagglutinin-neuraminidase (HN), in inducing protective immunity, two recombinant vaccinia viruses were constructed. The F and HN polypeptides expressed by the recombinant viruses were indistinguishable from their authentic SV5 counterparts in electrophoretic mobility, glycosylation, and, for the F protein, cleavage of the precursor, F0, to the disulfide-linked subunits F1 and F2. Injection of rabbits and hamsters with live recombinant virus elicited an antibody response to either F or HN and provided a source of monospecific polyclonal antisera to the SV5 proteins. The vaccinia virus-SV5 (vaccinia-F) recombinant induced higher levels of neutralizing antibody than did the vaccinia-HN recombinant, but animals inoculated with vaccinia-HN were better protected from challenge with SV5. Animals infected with both the vaccinia-HN and vaccinia-F viruses were nearly as well protected from challenge as were animals infected with SV5.

Original languageEnglish (US)
Pages (from-to)1972-1977
Number of pages6
JournalJournal of virology
Volume61
Issue number6
DOIs
StatePublished - 1987

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Insect Science
  • Virology

Fingerprint

Dive into the research topics of 'Comparison of the relative roles of the F and HN surface glycoproteins of the paramyxovirus simian virus 5 in inducing protective immunity'. Together they form a unique fingerprint.

Cite this