Human T cell leukemia virus envelope binding and virus entry are mediated by distinct domains of the glucose transporter GLUT1.
J Biol Chem
; 280(32): 29025-9, 2005 Aug 12.
Article
in En
| MEDLINE
| ID: mdl-15955807
ABSTRACT
The glucose transporter GLUT1, a member of the multimembrane-spanning facilitative nutrient transporter family, serves as a receptor for human T cell leukemia virus (HTLV) infection. Here, we show that the 7 amino acids of the extracellular loop 6 of GLUT1 (ECL6) placed in the context of the related GLUT3 transporter were sufficient for HTLV envelope binding. Glutamate residue 426 in ECL6 was identified as critical for binding. However, binding to ECL6 was not sufficient for HTLV envelope-driven infection. Infection required two additional determinants located in ECL1 and ECL5, which otherwise did not influence HTLV envelope binding. Moreover the single N-glycosylation chain located in ECL1 was not required for HTLV infection. Therefore, binding involves a discrete determinant in the carboxyl terminal ECL6, whereas post-binding events engage extracellular sequences in the amino and carboxyl terminus of GLUT1.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Monosaccharide Transport Proteins
/
Gene Products, env
/
Retroviridae Proteins, Oncogenic
/
Deltaretrovirus
Limits:
Animals
/
Humans
Language:
En
Journal:
J Biol Chem
Year:
2005
Document type:
Article
Affiliation country: