Mapping an antibody-binding site and a T-cell-stimulating site on the 1A protein of respiratory syncytial virus

Nicholas, Judith A.; Mitchell, Mark A.; Levely, Melissa E.; Rubino, Kathleen L.; Kinner, John H.; Harn, N K; Smith, C W

doi:10.1128/jvi.62.12.4465-4473.1988

Cited by 21 publications

(3 citation statements)

References 34 publications

(27 reference statements)

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“…In a recent study, it was shown that human post-RSV infection sera reacted with a peptide representing a hydrophilic part of the RSV subgroup A intramembranous 1A protein (17). This peptide may be subgroup specific also, because the amino acid sequence of the reactive region of the 1A protein shows considerable divergence between virus strains representing the two subgroups (P. Collins, personal communication).…”

Section: Discussionmentioning

confidence: 99%

A subgroup-specific antigenic site in the G protein of respiratory syncytial virus forms a disulfide-bonded loop

Åkerlind-Stopner

Utter

Mufson

et al. 1990

J Virol

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An antigenic site (represented by 15 amino acids, residues 174 to 188, designated peptide 12) of the large glycoprotein G of respiratory syncytial virus was demonstrated to be subgroup specific in peptide enzyme-linked immunosorbent assay tests with murine monoclonal antibodies and human postinfection sera. The role of individual amino acids in this subgroup-specific site was determined by use of single-amino-acid-deletion sets of peptides. When monoclonal antibodies were reacted with the deletion sets, a broad amino acid dependence of 11 or 12 residues, Cys-176 (Ile-175 in subgroup B) to Cys-186, was found. Human postinfection sera exhibited a narrower reaction profile (for subgroup A, Cys-182 to Trp-183; for subgroup B, Cys-176 to Lys-183). Reduction of peptides on microtiter plates by treatment with dithiothreitol completely destroyed their antigenic activity in tests with monoclonal antibodies and human postinfection sera of subgroup B. A variant of peptide 12 containing all four cysteines of the G protein (represented by 16 amino acids, residues 172 to 187, designated peptide 12var) also was subgroup specific. We concluded that the activity of the antigenic site in tests with monoclonal antibodies for subgroups A and B appears to depend on intrapeptide disulfide bonds. Reactions with postinfection sera of subgroup B also may depend on a disulfide bond. In contrast, postinfection sera of subgroup A appeared to have the capacity to identify a subgroup-specific site in a linear form of the selected 15-amino-acid-long peptide. Treatment of peptides with dithiothreitol had no effect on their antigenic activity in tests with human postinfection sera of subgroup A. These findings have relevance for molecular engineering of peptide antigens for use in respiratory syncytial virus subgroup-specific site-directed serology.

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Section: Discussionmentioning

confidence: 99%

A subgroup-specific antigenic site in the G protein of respiratory syncytial virus forms a disulfide-bonded loop

Åkerlind-Stopner

Utter

Mufson

et al. 1990

J Virol

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“…In mice, Openshaw et al [90] found T helper cell epitopes on the fusion glycoprotein and nucleoprotein, but not the G glycoprotein, SH or 1B proteins expressed from vaccinia recombinants. However, using synthetic peptides, Nicholas et al [82,83] have demonstrated two distinct T helper cell epitopes within a 16 amino acid sequence from the SH protein. Together these were capable of stimulating T cells from mice with several major histocompatibility complex haplotypes.…”

Section: Towards a Third Generationmentioning

confidence: 99%

Vaccination against respiratory syncytial virus: problems and progress

Toms

1991

FEMS Microbiology Letters

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“…T cells play a role both in viral clearance as well as in pathogenesis of the disease [8,9]. The recognition of T cell-stimulating sites on various RSV proteins [10][11][12][13] and the findings that T cells are necessary for viral clearance from the lungs of infected animals [9], suggest that these aspects of the immune response against RSV are probably important in the development of immunity and outcome of infection.…”

Section: Introductionmentioning

confidence: 99%

T cell redistribution kinetics after secondary infection of BALB/c mice with respiratory syncytial virus

Kimpen

Ogra

1993

Clinical and Experimental Immunology

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SUMMARYBALB/c mice were infected intranasally with live respiratory syncytial virus (RSV) and reinfected 4 weeks later. At regular intervals thereafter groups of animals were killed and T cell subsets were determined in blood, spleen and bronchoalveolar lavage (BAL) with flow cytometry employing T cell subset-specific MoAbs. Total lymphocyte counts in the peripheral blood decreased 1-3 days after infection, returning to preinfection levels on day 8 (/" = 00111). Simultaneously, a marked increase of lymphocytes was noted in the BAL, reaching a maximum at day 8 (/'<0 0001). Both CD4+ and CD8 + T cells decreased in the blood on day 1 -3 (P < 0 0097 and P = 0 003 respectively), and increased in the BAL progressively towards a maximum at day 8 (/'<0 0001). In BAL, CD4+ cells increased 35-fold and CD8+ cells 27-fold during the first week after reinfection. On the other hand, in the spleen a significant decline of CD4+ and CD8+ cells was noted 1 day post-infection (P = 0 0002). It is concluded that a strong T cell redistribution response among systemic and mucosal tissues occurs after reinfection with RSV. The kinetics of this response differ both quantitatively and qualitatively from the T cell response after primary infection. The magnitude of cell traffic is more pronounced in blood, spleen and BAL than after primary infection. CD4+ T cells are more intensively distributed to the lungs than after primary infection.

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Mapping an antibody-binding site and a T-cell-stimulating site on the 1A protein of respiratory syncytial virus

Cited by 21 publications

References 34 publications

A subgroup-specific antigenic site in the G protein of respiratory syncytial virus forms a disulfide-bonded loop

A subgroup-specific antigenic site in the G protein of respiratory syncytial virus forms a disulfide-bonded loop

Vaccination against respiratory syncytial virus: problems and progress

T cell redistribution kinetics after secondary infection of BALB/c mice with respiratory syncytial virus

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