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Cited by 58T-cell and Retrovirus StudiesHIV Research and TreatmentHepatitis B Virus Studies

Cellular Factors Involved in HTLV-1 Entry and Pathogenicit

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Hoshino, Hiroo·2012·Frontiers in Microbiology
DOI 10.3389/fmicb.2012.00222PMC PMC3380293
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Abstract

Human T cell leukemia virus type 1 (HTLV-1) is the causative agent of adult T cell leukemia (ATL) and HTLV-1 - associated myelopathy and tropical spastic paraparesis (HAM/TSP). HTLV-1 has a preferential tropism for CD4 T cells in healthy carriers and ATL patients, while both CD4 and CD8 T cells serve as viral reservoirs in HAM/TSP patients. HTLV-1 has also been detected other cell types, including monocytes, endothelial cells, and dendritic cells. In contrast to the limited cell tropism of HTLV-1 in vivo, the HTLV receptor appears to be expressed in almost all human or animal cell lines. It remains to be examined whether this cell tropism is determined by host factors or by HTLV-1 heterogeneity. Unlike most retroviruses, cell-free virions of HTLV-1 are very poorly infectious. The lack of completely HTLV-1-resistant cells and the low infectivity of HTLV-1 have hampered research on the HTLV entry receptor. Entry of HTLV-1 into target cells is thought to involve interactions between the env (Env) glycoproteins, a surface glycoprotein (surface unit), and a transmembrane glycoprotein. Recent studies have shown that glucose transporter GLUT1, heparan sulfate proteoglycans (HSPGs), and neuropilin-1 (NRP-1) are the three proteins important for the entry of HTLV-1. Studies using adherent cell lines have shown that GLUT1 can function as a receptor for HTLV. HSPGs are required for efficient entry of HTLV-1 into primary CD4 T cells. NRP-1 is expressed in most established cell lines. Further studies have shown that these three molecules work together to promote HTLV-1 binding to cells and fusion of viral and cell membranes. The virus could first contact with HSPGs and then form complexes with NRP-1, followed by association with GLUT1. It remains to be determined whether these three molecules can explain HTLV-1 cell tropism. It also remains to be more definitively proven that these molecules are sufficient to permit HTLV-1 entry into completely HTLV-1-resistant cells.

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  • HIV-1 Env contains ~25 glycosylation sites and forms a glycan shield protecting the virus from neutralizing antibodies; HTLV-1 Env contains only five sites for N-glycan attachment.

    “Unlike HIV-1 Env, which contains ~25 glycosylation sites [101], and forms a “glycan shield” protecting the virus from neutralizing antibodies [102], HTLV-1 Env contains only five sites for N-glycan attachment [103].”

    From HIV-1 and HTLV-1 Transmission Modes: Mechanisms and Importance for Virus Spread (2022) · cites this paper as [103]

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Authors
Hoshino, H.
Affiliations
Gunma University (JP)
Corresponding author
Hoshino, Hiroo
Venue
Frontiers in Microbiology
Publisher
Frontiers Media SA
Published
2012
Volume
3
Pages
222-222
ISSN
1664-302X (ISSN-L)
DOI
10.3389/fmicb.2012.00222
PMC
PMC3380293
OpenAlex
W2048443185
Cited by
58
References
4
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FWCI
1.54
Type
journal article
Language
en
Open access
Licence
cc-by-nc
Locations
  • Frontiers in Microbiology (publishedVersion, cc-by-nc)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Topics
  • Life Sciences › Immunology and Microbiology › Immunology › T-cell and Retrovirus Studies
  • Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
  • Health Sciences › Medicine › Epidemiology › Hepatitis B Virus Studies
Keywords
HTLV-1, viral entry, cell tropism, adult T-cell leukemia/lymphoma, HAM/TSP, CD4+ T cells, CD8+ T cells, viral reservoir, GLUT1, heparan sulfate proteoglycans, neuropilin-1, envelope glycoprotein, viral fusion, retroviral pathogenesis

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