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Journal of Virology, November 1999, p. 9659-9663, Vol. 73, No. 11
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

The Y-S-L-I Tyrosine-Based Motif in the Cytoplasmic Domain of the Human T-Cell Leukemia Virus Type 1 Envelope Is Essential for Cell-to-Cell Transmission

Lélia Delamarre, Claudine Pique, Arielle R. Rosenberg, Vincent Blot, Marie-Pierre Grange, Isabelle Le Blanc, and Marie-Christine Dokhélar*

INSERM U332, Institut Cochin de Génétique Moléculaire, Paris, France

Received 4 March 1999/Accepted 3 August 1999

The human T-cell leukemia virus type 1 (HTLV-1) transmembrane glycoprotein has a 24-amino-acid cytoplasmic domain whose function in the viral life cycle is poorly understood. We introduced premature-stop mutations and 18 single-amino-acid substitutions into this domain and studied their effects on cell-to-cell transmission of the virus. The results show that the cytoplasmic domain is absolutely required for cell-to-cell transmission of HTLV-1, through amino acids which cluster in a Y-S-L-I tyrosine-based motif. The transmission defect in two motif mutants did not result from a defect in glycoprotein incorporation or fusion. It appears that the Y-S-L-I tyrosine-based motif of the HTLV-1 glycoprotein cytoplasmic domain has multiple functions, including involvement in virus transmission at a postfusion step.

* Corresponding author. Mailing address: INSERM U332, Institut Cochin de Génétique Moléculaire, 22 rue Méchain, 75014 Paris, France. Phone: 33 1 40 51 64 81. Fax: 33 1 40 51 77 49. E-mail: dokhelar{at}cochin.inserm.fr.

Journal of Virology, November 1999, p. 9659-9663, Vol. 73, No. 11
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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