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We have shown previously that a type-specific neutralization domain is located within a 39 aa sequence in the fourth variable domain of gp135 in visna/maedi virus. We now show that neutralizing antibodies detected early in infection are directed to this epitope, suggesting an immunodominant nature of this domain. Ten antigenic variants were previously analysed for mutations in this region, and all but one were found to be mutated. To assess the importance of these mutations in replication and neutralization, we reconstructed several of the mutations in an infectious molecular clone and tested the resulting viruses for neutralization phenotype and replication. Mutation of a conserved cysteine was shown to alter the neutralization epitope, whilst the replication kinetics in macrophages were unchanged. Mutations modulating potential glycosylation sites were found in seven of the ten antigenic variants. A frequently occurring mutation, removing a potential glycosylation site, had no effect on its own on the neutralization phenotype of the virus. However, adding an extra potential glycosylation site in the region resulted in antigenic escape. The results indicate that the conserved cysteine plays a role in the structure of the epitope and that glycosylation may shield the principal neutralization site.


Benedikta S Haflidadóttir, Sigrídur Matthíasdóttir, Gudrún Agnarsdóttir, Sigurbjorg Torsteinsdóttir, Gudmundur Pétursson, Olafur S Andrésson, Valgerdur Andrésdóttir. Mutational analysis of a principal neutralization domain of visna/maedi virus envelope glycoprotein. The Journal of general virology. 2008 Mar;89(Pt 3):716-21

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PMID: 18272763

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