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Journal of Virology, September 1998, p. 7609-7614, Vol. 72, No. 9
INSERM U332, ICGM, Paris, France
Received 28 January 1998/Accepted 29 May 1998
Human T-cell leukemia virus types 1 and 2 (HTLV-1 and HTLV-2) are
closely related retroviruses with nucleotide sequences that are 65%
identical. To determine whether their envelope glycoproteins function similarly and to define the molecular determinants
of HTLV-2 envelope-mediated functions, we have used
pseudotyped viruses and have introduced mutations into regions
of the HTLV-2 glycoproteins homologous to those known to be important
for HTLV-1 glycoprotein functions. The envelopes of the two viruses
could be exchanged with no loss of infectivity, suggesting that the
glycoproteins function in broadly similar ways. However,
comparative analysis of the HTLV-1 and HTLV-2 glycoproteins showed
subtle differences in the structure-function relationships of the two
surface glycoprotein (SU) subunits, even though they recognize the same
receptor. Indeed, mutations introduced at equivalent positions in the
two SU glycoproteins resulted in different phenotypes in the two
viruses. The scenario is the opposite for the transmembrane
glycoprotein (TM) subunits, in which the functional domains of the two
viruses are strictly conserved, confirming the involvement of the TM
ectodomain in postfusion events required for full infectivity of the
HTLVs. Thus, although they recognize the same receptor, the HTLV-1 and HTLV-2 SU subunits have slightly different ways of transducing the
conformational information that primes a common fusion mechanism effected by similar TM subunits.
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Analysis of Functional Conservation in the Surface and
Transmembrane Glycoprotein Subunits of Human T-Cell Leukemia Virus
Type 1 (HTLV-1) and HTLV-2
*
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.
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