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  • Meeting abstract
  • Open Access

New insights into HTLV entry

  • 1, 2, 3Email author,
  • 4,
  • 5 and
  • 6
Retrovirology20118(Suppl 1):A183

https://doi.org/10.1186/1742-4690-8-S1-A183

Published: 6 June 2011

Keywords

  • Glucose Transporter
  • Heparan Sulfate
  • Receptor Complex
  • Sulfate Proteoglycan
  • Envelope Glycoprotein

Insight into the long-lasting mystery of the HTLV-1 entry receptor was provided over the past several years by the independent identification of three molecules required for binding and entry into cells: heparan sulfate proteoglycans (HSPG), the VEGF-165 receptor Neuropilin 1 (NRP-1) and the ubiquitous glucose transporter GLUT1. Further studies have indicated that these three molecules work together to ensure virus binding and ultimately, fusion of the viral and target cell membranes. Interaction of the virus with this receptor complex is mediated by the envelope glycoproteins (Env), which consists of a complex formed between a surface (SU, gp46) and a transmembrane (TM, gp21) subunit. Studies prior to the characterization of the HTLV-1 receptor complex identified domains and specific residues of the HTLV-1 SU involved in the Env/receptor interactions through either characterization of neutralizing antibodies or peptides or analysis of Env mutants. We will present our current model for HTLV-1 entry and revisit the data about the functional domains of the SU in regard to the recently acquired knowledge about the three receptor molecules. We will also discuss the role of these three molecules during the cell-cell and cell-free infection of T cells and dendritic cells. Finally, we will examine the similarities and differences between the distinct members of the HTLV family in their receptor usage.

Authors’ Affiliations

(1)
INSERM, U1016, Institut Cochinn, Paris, France
(2)
CNRS UMR 8104, Paris, France
(3)
Univ Paris Descartes, Paris, France
(4)
Service d’Hématologie Adulte, Hôpital Necker, Paris, France
(5)
Cancer and Inflammation Program, NCI-Frederick, Frederick, USA
(6)
Basic Research Program, SAIC-Frederick, Inc., Frederick, USA

Copyright

© Pique 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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