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 F (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.
MeSH Terms
Animals
Antibodies, Viral/biosynthesis
Antigens/immunology
Antigens, Viral/genetics,immunology
Cricetinae
Female
HN Protein
Immunization
Mesocricetus
Paramyxoviridae/genetics,immunology
Recombinant Proteins/genetics,immunology
Vaccines, Synthetic/immunology
Vaccinia virus/genetics
Viral Envelope Proteins/genetics,immunology
Viral Fusion Proteins/genetics,immunology
Viral Vaccines/immunology
Chemicals
Antibodies, Viral
Antigens
Antigens, Viral
HN Protein
Recombinant Proteins
Vaccines, Synthetic
Viral Envelope Proteins
Viral Fusion Proteins
Viral Vaccines
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Paterson R G
Lamb R A
Moss B
Murphy B R
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