Immunovirological studies on human respiratory syncytial virus structural proteins

Abstract

Immunovirological studies suggest that human respiratory syncytial virus may well be composed of five structural proteins as are other members of the Paramyxoviridae family: the two external membrane glycoproteins H (90 000) and Fo (F1, 49 000; F2, 20 000; disulfide linked), the internal membrane protein M (34 000), the nucleoprotein N (42 000), and a protein (78 000) designated P that could be the equivalent of the polymerase of the morbillivirus and paramyxovirus genus. Neutralizing monoclonal antibodies showed, by immunoprecipitation and immunoblotting, that the fusion protein carries neutralizing epitopes. One monoclonal antibody, which shows a high neutralizing titer, immunoblotted directly with the F1 fragment (49 000) of the fusion protein. Analysis in mice of the immunogenicity of the structural proteins separated on sodium dodecyl sulphate gels indicated that, under our conditions, only the fusion protein dimer Fo and its F1 fragment were capable of inducing neutralizing antibodies.

Identification of a Synthetic Peptide as Part of a Major Neutralization Epitope of Respiratory Syncytial Virus

“…Expression by recombinant vaccinia viruses of the major and fusion glycoproteins of RS virus (Olmsted et al, 1986) confirmed previous work carried out with MAbs and purified solubilized proteins showing the predominant role of the fusion glycoprotein in inducing immunity 0000-7711 © 1987 SGM (Anderson et al, 1986;Fernie & Gerin, 1982;Gimenez et al, 1984;Routledge et al, 1985 ;Stott et al, 1984;Taylor et al, 1984;Trudel et al, 1986;Walsh et al, 1984Walsh et al, , 1986Walsh & Hurska, 1983). This paper presents data derived from peptide mapping and amino acid analysis indicating that the major neutralization epitope is located between amino acids 164Glu to 236Glu of the mRNA-deduced sequence of the A2 strain of human RS virus.…”

“…Recently, using a neutralizing MAb produced against the Long strain of RS virus, a major and highly conserved neutralization epitope was identified which was present on human, bovine and caprine strains of RS virus but not on pneumonia virus of mice. This epitope is localized on the F 1 fragment of the fusion glycoprotein (Trudel et al, 1986(Trudel et al, , 1987.…”

“…It is composed of two disulphide-linked subunits: F1 with a reported Mr varying from 43K to 50K and F2 from 19K to 25K (Walsh et al, 1985(Walsh et al, , 1986Trudel et al, 1986).…”

“…Recently, using a neutralizing MAb produced against the Long strain of RS virus, a major and highly conserved neutralization epitope was identified which was present on human, bovine and caprine strains of RS virus but not on pneumonia virus of mice. This epitope is localized on the F 1 fragment of the fusion glycoprotein (Trudel et al, 1986(Trudel et al, , 1987.The fusion glycoprotein is found as a 125K Mr dimer on the viral envelope and is involved in cell fusion leading to the formation of syncytia and cell penetration. It is composed of two disulphide-linked subunits: F1 with a reported Mr varying from 43K to 50K and F2 from 19K to 25K (Walsh et al, 1985, 1986;Trudel et al, 1986).…”

“…This epitope is localized on the F 1 fragment of the fusion glycoprotein (Trudel et al, 1986(Trudel et al, , 1987.…”