Volume 8 Supplement 1

15th International Conference on Human Retroviruses: HTLV and Related Viruses

Open Access

Role of glycosylation in bovine leukemia virus infection

  • Amel-Baya Bouzar1,
  • Alix de Brogniez1Email author,
  • Arnaud Florins1,
  • Carole François1,
  • Mathieu Boxus1 and
  • Luc Willems1
Retrovirology20118(Suppl 1):A29

https://doi.org/10.1186/1742-4690-8-S1-A29

Published: 6 June 2011

As a model for HTLV, reverse genetics can be used in the bovine leukemia virus (BLV) system to identify important mechanisms of viral persistence and pathogenesis. The question addressed here pertains to the role of glycans bound to the BLV envelope glycoprotein (SU gp51). Addition of carbohydrates to the BLV SU potentially creates a structure called « glycan shield » that confers resistance to the virus against the host immune response. On the other hand, glycosylation can also modulate attachment of the virus to the cell membrane.

To unravel the role of SU glycosylation, three complementary strategies were developed: pharmacological inhibition of different glycosylation pathways, interference with glycan attachment and site-directed mutagenesis of N-glycosylation sites in an infectious BLV provirus. Collectively, our results demonstrate that glycosylation is important for the Gp51 maturation process, for virus infection in vitro and for infectivity in vivo.

Authors’ Affiliations

(1)
Cellular and Molecular Biology, Gembloux Agro-Bio Tech, University of Liege

Copyright

© Bouzar et al; licensee BioMed Central Ltd. 2011

This article is published under license to BioMed Central Ltd. This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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