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 : 002076The 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 :
- Virology [ 0042-6822 ] ; 1990.
English descriptors
- Teeft :
- Amino, Amino acid identity, Amino acid sequence, Amino acid sequences, Amino acids, Antibody titers, Antigenic, Antigenic differences, Attachment glycoprotein, Attachment protein, Cdna, Cdna clone, Cdna clones, Cell lysates, Chanock, Clone, Control animals, Cotton rats, Elango, Extracellular, Extracellular domain, Fusion protein, Glycoprotein, Heterologous, Heterologous subgroup, Monoclonal, Monoclonal antibodies, Monoclonal antibody, Mrna, Mufson, Nucleic, Nucleic acid, Nucleic acids, Nucleotide, Nucleotide sequences, Olmsted, Orvell, Plasmid, Potential glycosylation sites, Previous work, Primer extension sequencing, Recombinant, Recombinant vaccinia virus, Recombinant vaccinia viruses, Respiratory syncytial virus, Same subgroup, Sequencing, Significant protection, Significant reduction, Stott, Subgroup, Subgroup viruses, Subunit vaccine, Syncytial, Syncytial virus, Syncytlal, Syncytlal virus, Vaccine, Vaccinia, Vaccinia virus, Viral, Viral titers, Virus, Virus challenge, Virus subgroup, Virus subgroups, Wertz.
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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<term>Amino acids</term>
<term>Antibody titers</term>
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<term>Antigenic differences</term>
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<term>Recombinant vaccinia virus</term>
<term>Recombinant vaccinia viruses</term>
<term>Respiratory syncytial virus</term>
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<term>Significant reduction</term>
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<term>Syncytial virus</term>
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<term>Syncytlal virus</term>
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<term>Vaccinia virus</term>
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<front><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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