Challenge of BALB/c Mice with Respiratory Syncytial Virus Does Not Enhance the Th2 Pathway Induced after Immunization with a Recombinant G Fusion Protein, BBG2NA, in Aluminum Hydroxide

The polypeptide of aa 130–230 of the G protein (G2Na) of respiratory syncytial virus (RSV) was fused to BB, the albumin-binding region of streptococcal G protein, producing BBG2Na, which induced protective immune responses in rodent models. Evaluation of the immune response in mice immunized with BB...

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Veröffentlicht in:The Journal of infectious diseases 1997-09, Vol.176 (3), p.560-569
Hauptverfasser: Corvaïa, Nathalie, Tournier, Patricia, Nguyen, Thien Ngoc, Haeuw, Jean François, Power, Ultan F., Binz, Hans, Andréoni, Christine
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Sprache:eng
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Zusammenfassung:The polypeptide of aa 130–230 of the G protein (G2Na) of respiratory syncytial virus (RSV) was fused to BB, the albumin-binding region of streptococcal G protein, producing BBG2Na, which induced protective immune responses in rodent models. Evaluation of the immune response in mice immunized with BBG2Na in the adjuvant alhydrogel revealed high amounts of interleukin (IL)-5 and some IL-4 in splenocytes restimulated in vitro. This is compatible with a Th2 response. The activation of the Th2 pathway in such mice was further supported by the detection of IL-5 and G2Na-specific IgE in vivo. Of interest, in contrast to immunization with formalin-inactivated RSV, immunization of mice with BBG2Na followed by intranasal RSV challenge did not lead to increased production of IL-5- or G2Na-specific IgE. However, IgG1- and IgG2a-specific antibodies were boosted. These results demonstrate that the Th2 pathway is not enhanced by RSV challenge in BBG2Na-immunized mice.
ISSN:0022-1899
1537-6613
DOI:10.1086/514075