Epitope specificities of human serum antibodies reactive with respiratory syncytial virus fusion protein

Robinson, B.S.; Everson, Jordan

doi:10.1007/bf01309644

Cited by 5 publications

(2 citation statements)

References 30 publications

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“…Based on the identification of distinct antigenic sites and on the diverse characteristics of the concerned epitopes into these domains, the response to infection with BRSV does not seem to be rest-ricted to a particular zone of the F protein. Our results coincide with the heterogeneity of the immune response to HRSV which was reported by several authors [18,19].…”

Section: Discussionsupporting

confidence: 95%

“…Although none of the epitopes appeared immunodominant, it is possible that certain sera contain antibodies more specific to restricted epitopes as described by Robinson and Everson [19]. Nevertheless, our study does not allow us to draw such conclusions with certainty due to a number of uncontrollable parameters (avidity of MAbs and Abs in sera, concentration of Abs in sera...) which could interfere in these assays.…”

Section: Discussionmentioning

confidence: 73%

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Antigenic analysis of the F protein of the bovine respiratory syncytial virus: identification of two distinct antigenic sites involved in fusion inhibition

Matheise

Walravens

Collard

et al. 1995

Archives of Virology

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From two independent fusions, fifteen MAbs directed to the F protein of the bovine respiratory syncytial virus (BRSV) were characterized by radio-immunoprecipitation assays. Competition binding assays among these MAbs identified two distinct antigenic sites (A and B) and one overlapping site (AB). All of the MAbs specific to epitopes belonging to site A neutralized the infectivity of the virus in vitro and recognized human and bovine RSV strains. Only two out of the five MAbs directed to epitopes of site B were neutralizing and three reacted with all of the RSV strains tested, suggesting that the epitopes constituting this domain present heterogeneous characteristics. In each of sites A and B, one of the neutralizing MAbs also inhibited cell fusion. The biological relevance of these domains was established by competing representative MAbs and sera from BRSV-infected calves.

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Section: Discussionsupporting

confidence: 95%

Section: Discussionmentioning

confidence: 73%

Antigenic analysis of the F protein of the bovine respiratory syncytial virus: identification of two distinct antigenic sites involved in fusion inhibition

Matheise

Walravens

Collard

et al. 1995

Archives of Virology

View full text Add to dashboard Cite

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Subgrouping of respiratory syncytial virus strains from Australia and Papua New Guinea by biological and antigenic characteristics

Hierholzer

Tannock

Hierholzer

et al. 1994

Archives of Virology

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Strains of respiratory syncytial virus from 3 major areas of Australia and Papua New Guinea (PNG) were analyzed for variations in their antigenic and biological properties and in the molecular weights of their major structural proteins. Seventy-eight strains from infants and young children with LRI were collected from 1981-1984. The RSV season in the Australian cities lasted from April through September, with major peaks in July of each year, while the RSV season in tropical PNG was year-round, with small peaks in March and October of each year coinciding with excessive rainfall. Fifty-six strains were analyzed in detail; 40 were typed by time-resolved fluoroimmunoassay with monoclonal antibodies as group A strains and 16 were group B; both groups were concurrent. Three children of one family had sequential RSV infections 13 months apart, and the etiologic group A strain was identical both years in terms of growth and antigenic properties with strain-specific ferret antisera; the second infection was milder in all three children. On average, the group A strains replicated considerably better than group B strains in HEp2 cells, producing 53% more syncytia and 99% higher infectious virus titers in 31% less time in culture. Ten group A and B reference strains exhibited the same growth patterns as the A and B regional strains, respectively. Differences in antigenicity as measured with hyperimmune antisera to prototype Long strain were even greater. Group A strains exhibited a mean 68% greater IFA staining than B strains, a 71% greater EIA reaction, and were neutralized to 69% higher serum titers than B strains. Again, the reference A and B strains included as controls gave patterns identical to those of the regional strains. Finally, the P phosphoprotein had consistently higher molecular weight in A strains (mean 35,900) than B strains (mean 33,100). Small variations in the sizes of the F and G glycoproteins were not sufficient to suggest grouping on this basis.

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Antibody responses against epitopes on the F protein of bovine respiratory syncytial virus differ in infected or vaccinated cattle

Schrijver¹,

Hensen²,

Langedijk³

et al. 1997

Arch. Virol.

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The fusion protein F of bovine respiratory syncytial virus (BRSV) is an important target for humoral and cellular immune responses, and antibodies against the F protein have been associated with protection. However, the F protein can induce antibodies with different biological activity, possibly related to distinct antigenic regions on the protein. Therefore, epitopes were mapped on the F protein using monoclonal antibodies. Two epitopes (A and B) were identified that induced neutralizing antibodies, and one epitope (C) that did not elicit neutralizing antibodies. Subsequently, antibody responses were analysed against these epitopes in cattle sera after natural infection, experimental infection or vaccination. After natural infection or reinfection, the antibody titres against epitope A were significantly higher than those against epitope B or C. After experimental infection and after vaccination with an inactivated vaccine, antibody titres against epitope B and C were significantly higher than after natural infection. Conversely, virus neutralizing antibody titres were significantly lower in these animals with higher antibody titres against epitopes B and C than in naturally infected cattle. Because after natural infection the epitope-specific-antibody titres against epitope A, B or C differed markedly between the cattle, the magnitude of the antibody titres against epitope A, B or C in relation to the major histocompatibility complex (MHC) genes of cattle (BoLA) was studied. The magnitude of the antibody responses against epitope A of the F protein, but not against the G protein, appeared to be associated with the bovine lymphocyte antigen (BoLA) haplotype.

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Epitope specificities of human serum antibodies reactive with respiratory syncytial virus fusion protein

Cited by 5 publications

References 30 publications

Antigenic analysis of the F protein of the bovine respiratory syncytial virus: identification of two distinct antigenic sites involved in fusion inhibition

Antigenic analysis of the F protein of the bovine respiratory syncytial virus: identification of two distinct antigenic sites involved in fusion inhibition

Subgrouping of respiratory syncytial virus strains from Australia and Papua New Guinea by biological and antigenic characteristics

Antibody responses against epitopes on the F protein of bovine respiratory syncytial virus differ in infected or vaccinated cattle

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