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The respiratory syncytial virus subgroup B attachment glycoprotein: analysis of sequence, expression from a recombinant vector, and evaluation as an immunogen against homologous and heterologous subgroup virus challenge

Identifieur interne : 002075 ( Main/Exploration ); précédent : 002074; suivant : 002076

The respiratory syncytial virus subgroup B attachment glycoprotein: analysis of sequence, expression from a recombinant vector, and evaluation as an immunogen against homologous and heterologous subgroup virus challenge

Auteurs : Wayne M. Sullender [États-Unis] ; Kevin Anderson [États-Unis] ; Gail W. Wertz [États-Unis]

Source :

RBID : ISTEX:D4193B4F65402E59F3646CD5F19BF7750BFAB58A

English descriptors

Abstract

Abstract: The attachment glycoprotein G of respiratory syncytial (RS) virus is important in both the antigenic and molecular diversity of the RS viruses. Previous work has shown that the glycoprotein G of a subgroup A RS virus expressed from a recombinant vaccinia virus provides significant protection against homologous but not heterologous subgroup virus challenge. We undertook the cDNA cloning and nucleotide sequencing of the G mRNA of a subgroup B RS virus ( 8 60) to extend molecular comparisons of the G protein both within and between subgroups. We also tested the ability of a subgroup B G protein to provide protection against challenge by A or B subgroup viruses. Sequence analysis showed a deduced amino acid sequence having a single major open reading frame encoding a protein of 292 amino acids with an elevated serine and threonine (30%) and proline (9%) content. The 8 60 G differed from a subgroup A virus (A2) G protein with only a 56% amino acid identity while the 8 60 G shared a 98% amino acid identity with the G protein of another subgroup B virus (18537). The 8 60 G cDNA was placed in a vaccinia virus vector (vvGB) which was shown to express the 8 60 G protein. Cotton rats immunized intradermally with vvGB and later challenged intranasally with 8 60 RS virus had a significant reduction in viral titers in the lungs relative to control animals whereas similarly immunized animals were not protected against heterologous subgroup challenge. Our results indicate that a RS virus subunit vaccine containing the G protein would require both A and B subgroup G proteins to afford protection against viruses of both subgroups.

Url:
DOI: 10.1016/0042-6822(90)90394-7


Affiliations:


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Le document en format XML

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<div type="abstract" xml:lang="en">Abstract: The attachment glycoprotein G of respiratory syncytial (RS) virus is important in both the antigenic and molecular diversity of the RS viruses. Previous work has shown that the glycoprotein G of a subgroup A RS virus expressed from a recombinant vaccinia virus provides significant protection against homologous but not heterologous subgroup virus challenge. We undertook the cDNA cloning and nucleotide sequencing of the G mRNA of a subgroup B RS virus ( 8 60) to extend molecular comparisons of the G protein both within and between subgroups. We also tested the ability of a subgroup B G protein to provide protection against challenge by A or B subgroup viruses. Sequence analysis showed a deduced amino acid sequence having a single major open reading frame encoding a protein of 292 amino acids with an elevated serine and threonine (30%) and proline (9%) content. The 8 60 G differed from a subgroup A virus (A2) G protein with only a 56% amino acid identity while the 8 60 G shared a 98% amino acid identity with the G protein of another subgroup B virus (18537). The 8 60 G cDNA was placed in a vaccinia virus vector (vvGB) which was shown to express the 8 60 G protein. Cotton rats immunized intradermally with vvGB and later challenged intranasally with 8 60 RS virus had a significant reduction in viral titers in the lungs relative to control animals whereas similarly immunized animals were not protected against heterologous subgroup challenge. Our results indicate that a RS virus subunit vaccine containing the G protein would require both A and B subgroup G proteins to afford protection against viruses of both subgroups.</div>
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