Short CommunicationsNeutralization Determinants of United States Bluetongue Virus Serotype Ten
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Immunisation with bacterial expressed VP2 and VP5 of bluetongue virus (BTV) protect α/β interferon-receptor knock-out (IFNAR<sup>-/-</sup>) mice from homologous lethal challenge
2014, VaccineCitation Excerpt :However, when both domains were mixed together on an equimolar basis, higher titres of neutralising antibodies were elicited. There is published evidence that neutralisation epitopes are located in the first ∼350 amino acids (domain 1) of VP2 of BTV-10 [56]. IFNAR−/− mice immunised with VP2D1 + VP2D2 and challenged with live BTV-4 survived until the end of the experiment with a transient viraemia (∼0.3–9 pfu/ml detected by RT-PCR only) which was cleared subsequently.
The immune response of ruminant livestock to bluetongue virus: From type I interferon to antibody
2014, Virus ResearchCitation Excerpt :Sheep inoculated with VP2 that is either isolated from viral particles or generated by in vitro expression produce virus neutralizing antibodies and are resistant to challenge infection with the homologous BTV serotype (Huismans and Erasmus, 1981; Huismans et al., 1987; Roy et al., 1990, 1992, 1994; Stewart et al., 2012). At least some neutralization epitopes are highly conformationally dependent, reflecting not only folding of the VP2 protein on itself but also its conformational interaction with the other outer capsid protein, VP5 (Appleton and Letchworth, 1983; Cowley and Gorman, 1987; DeMaula et al., 1993, 2000; Gould et al., 1988; Gould and Eaton, 1990; Heidner et al., 1990; Mertens et al., 1989). DeMaula et al. (2000) showed that whereas most variants that were resistant to neutralization with individual neutralizing monoclonal antibodies (MAbs) had amino acid substitutions in key regions of VP2, the VP2 of one MAb-neutralization resistant variant virus was unchanged but this virus had a substitution in VP5, confirming unambiguously the importance of the conformational interaction between VP2 and VP5 in BTV neutralization.
Protective efficacy of Bluetongue virus-like and subvirus-like particles in sheep: Presence of the serotype-specific VP2, independent of its geographic lineage, is essential for protection
2012, VaccineCitation Excerpt :The VP2 amino acid sequence similarity between the BTV-1 RSA and GRE2001/07 isolate was 82.1%. Although there were changes to the amino acid sequence, the two regions with the neutralisation epitopes in VP2 [28,29] were conserved in sequence of both BTV-1 isolates (Fig. 2). Twenty-one Karagouniko cross female sheep were divided into 3 groups (I, II and III) and immunized with BTV CLPs (Group I), BTV-1 RSA VLPs (Group II) or saline/saline plus adjuvant (Group III).
Differentiation between field and vaccine strain of bluetongue virus serotype 16
2006, Veterinary Microbiology