HBZ upregulates myoferlin expression to facilitate HTLV-1 infection.
Journal
PLoS pathogens
ISSN: 1553-7374
Titre abrégé: PLoS Pathog
Pays: United States
ID NLM: 101238921
Informations de publication
Date de publication:
02 2023
02 2023
Historique:
received:
16
11
2022
accepted:
10
02
2023
revised:
08
03
2023
pubmed:
25
2
2023
medline:
11
3
2023
entrez:
24
2
2023
Statut:
epublish
Résumé
The complex retrovirus, human T-cell leukemia virus type 1 (HTLV-1), primarily infects CD4+ T-cells in vivo. Infectious spread within this cell population requires direct contact between virally-infected and target cells. The HTLV-1 accessory protein, HBZ, was recently shown to enhance HTLV-1 infection by activating intracellular adhesion molecule 1 (ICAM-1) expression, which promotes binding of infected cells to target cells and facilitates formation of a virological synapse. In this study we show that HBZ additionally enhances HTLV-1 infection by activating expression of myoferlin (MyoF), which functions in membrane fusion and repair and vesicle transport. Results from ChIP assays and quantitative reverse transcriptase PCR indicate that HBZ forms a complex with c-Jun or JunB at two enhancer sites within the MYOF gene and activates transcription through recruitment of the coactivator p300/CBP. In HTLV-1-infected T-cells, specific inhibition of MyoF using the drug, WJ460, or shRNA-mediated knockdown of MyoF reduced infection efficiency. This effect was associated with a decrease in cell adhesion and an intracellular reduction in the abundance of HTLV-1 envelope (Env) surface unit (SU) and transmembrane domain (TM). Lysosomal protease inhibitors partially restored SU levels in WJ460-treated cells, and SU localization to LAMP-2 sites was increased by MyoF knockdown, suggesting that MyoF restricts SU trafficking to lysosomes for degradation. Consistent with these effects, less SU was associated with cell-free virus particles. Together, these data suggest that MyoF contributes to HTLV-1 infection through modulation of Env trafficking and cell adhesion.
Identifiants
pubmed: 36827461
doi: 10.1371/journal.ppat.1011202
pii: PPATHOGENS-D-22-02001
pmc: PMC9994761
doi:
Substances chimiques
Basic-Leucine Zipper Transcription Factors
0
HBZ protein, human T-cell leukemia virus type I
0
Retroviridae Proteins
0
MYOF protein, human
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
e1011202Subventions
Organisme : NCI NIH HHS
ID : P01 CA100730
Pays : United States
Organisme : NIAID NIH HHS
ID : R15 AI133412
Pays : United States
Organisme : NIAID NIH HHS
ID : R21 AI166077
Pays : United States
Informations de copyright
Copyright: © 2023 Polakowski et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Déclaration de conflit d'intérêts
The authors have declared that no competing interests exist.
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