HTLV-1 Tax-1 interacts with SNX27 to regulate cellular localization of the HTLV-1 receptor molecule, GLUT1.
Amino Acid Sequence
Gene Knockdown Techniques
Gene Products, tax
/ chemistry
Glucose Transporter Type 1
/ physiology
HEK293 Cells
HTLV-I Infections
/ genetics
Host Microbial Interactions
/ genetics
Human T-lymphotropic virus 1
/ genetics
Humans
Models, Biological
PDZ Domains
Protein Interaction Domains and Motifs
Receptors, Virus
/ physiology
Sorting Nexins
/ chemistry
Virulence
/ genetics
gag Gene Products, Human Immunodeficiency Virus
/ physiology
Journal
PloS one
ISSN: 1932-6203
Titre abrégé: PLoS One
Pays: United States
ID NLM: 101285081
Informations de publication
Date de publication:
2019
2019
Historique:
received:
04
10
2018
accepted:
06
03
2019
entrez:
22
3
2019
pubmed:
22
3
2019
medline:
18
12
2019
Statut:
epublish
Résumé
An estimated 10-20 million people worldwide are infected with human T cell leukemia virus type 1 (HTLV-1), with endemic areas of infection in Japan, Australia, the Caribbean, and Africa. HTLV-1 is the causative agent of adult T cell leukemia (ATL) and HTLV-1 associated myopathy/tropic spastic paraparesis (HAM/TSP). HTLV-1 expresses several regulatory and accessory genes that function at different stages of the virus life cycle. The regulatory gene Tax-1 is required for efficient virus replication, as it drives transcription of viral gene products, and has also been demonstrated to play a key role in the pathogenesis of the virus. Several studies have identified a PDZ binding motif (PBM) at the carboxyl terminus of Tax-1 and demonstrated the importance of this domain for HTLV-1 induced cellular transformation. Using a mass spectrometry-based proteomics approach we identified sorting nexin 27 (SNX27) as a novel interacting partner of Tax-1. Further, we demonstrated that their interaction is mediated by the Tax-1 PBM and SNX27 PDZ domains. SNX27 has been shown to promote the plasma membrane localization of glucose transport 1 (GLUT1), one of the receptor molecules of the HTLV-1 virus, and the receptor molecule required for HTLV-1 fusion and entry. We postulated that Tax-1 alters GLUT1 localization via its interaction with SNX27. We demonstrate that over expression of Tax-1 in cells causes a reduction of GLUT1 on the plasma membrane. Furthermore, we show that knockdown of SNX27 results in increased virion release and decreased HTLV-1 infectivity. Collectively, we demonstrate the first known mechanism by which HTLV-1 regulates a receptor molecule post-infection.
Identifiants
pubmed: 30897179
doi: 10.1371/journal.pone.0214059
pii: PONE-D-19-06509
pmc: PMC6428263
doi:
Substances chimiques
Gene Products, tax
0
Glucose Transporter Type 1
0
Receptors, Virus
0
SLC2A1 protein, human
0
SNX27 protein, human
0
Sorting Nexins
0
gag Gene Products, Human Immunodeficiency Virus
0
p19 protein, Human T-lymphotropic virus 1
0
tax protein, Human T-lymphotrophic virus 1
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
e0214059Subventions
Organisme : NCI NIH HHS
ID : P01 CA100730
Pays : United States
Organisme : NCI NIH HHS
ID : R01 CA063417
Pays : United States
Déclaration de conflit d'intérêts
The authors have declared that no competing interests exist.
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