Cited by 137T-cell and Retrovirus StudiesHIV Research and TreatmentDrug Transport and Resistance Mechanisms

A putative cell surface receptor for anemia-inducing feline leukemia virus subgroup C is a member of a transporter superfamily

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Tailor, Chetankumar S., Willett, Brian J., Kabat, David·1999·Journal of Virology

Abstract

Domestic cats infected with the horizontally transmitted feline leukemia virus subgroup A (FeLV-A) often produce mutants (termed FeLV-C) that bind to a distinct cell surface receptor and cause severe aplastic anemia in vivo and erythroblast destruction in bone marrow cultures. The major determinant for FeLV-C-induced anemia has been mapped to a small region of the surface envelope glycoprotein that is responsible for its receptor binding specificity. Thus, erythroblast destruction may directly or indirectly result from FeLV-C binding to its receptor. To address these issues, we functionally cloned a putative cell surface receptor for FeLV-C (FLVCR) by using a human T-lymphocyte cDNA library in a retroviral vector. Expression of the 2.0-kbp FLVCR cDNA in naturally resistant Swiss mouse fibroblasts and Chinese hamster ovary cells caused substantial susceptibility to FeLV-C but no change in susceptibilities to FeLV-B and other retroviruses. The predicted FLVCR protein contains 555 amino acids and 12 hydrophobic potential membrane-spanning sequences. Database searches indicated that FLVCR is a member of the major-facilitator superfamily of transporters and implied that it may transport an organic anion. RNA blot analyses showed that FLVCR mRNA is expressed in multiple hematopoietic lineages rather than specifically in erythroblasts. These results suggest that the targeted destruction of erythroblasts by FeLV-C may derive from their greater sensitivity to this virus rather than from a preferential susceptibility to infection.

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Crossref · 10.1128/jvi.73.8.6500-6505.1999

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  • Heme complexes are shuttled out of mitochondria to the cytosol by FLVCR1.

    “These heme complexes are then shuttled out of the mitochondria to the cytosol by the Feline Leukemia Virus Subgroup Receptor 1 (FLVCR1) (Tailor et al., 1999) where hemoglobin in erythrocytes, or other proteins known as hemoproteins, incorporate the heme complex to confer functionality;”

    From The Role of Iron Regulation in Immunometabolism and Immune-Related Disease (2019) · cites this paper as Tailor et al., 1999

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Authors
Tailor, C. S., Willett, B. J., & Kabat, D.
Affiliations
  • Oregon Health & Science University (US)
  • University of Glasgow (GB)
Venue
Journal of Virology
Published
1999-08
Volume
73
Issue
8
Pages
6500-6505
ISSN
  • 0022-538X (ISSN-L)
  • 1098-5514
OpenAlex
W2136280576
Cited by
137
References
57
Citations by year
2026: 1 · 2025: 2 · 2024: 10 · 2023: 4 · 2022: 3 · 2021: 1 · 2020: 2 · 2019: 5 · 2018: 6 · 2017: 2 · 2016: 4 · 2015: 6 · 2014: 2 · 2013: 7 · 2012: 11
FWCI
1.83
Type
journal article
Language
en
Open access
Locations
  • Journal of Virology (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • ENLIGHTEN (Jurnal Bimbingan dan Konseling Islam) (acceptedVersion)
Funders
  • National Institutes of Health (5r01ca025810-23)
  • National Cancer Institute (CA 25810)
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 › Oncology › Drug Transport and Resistance Mechanisms
Keywords
cell surface receptors, major facilitator superfamily, organic anion transport, receptor specificity, envelope glycoprotein, aplastic anemia, hematopoietic lineage, cats
MeSH terms
Amino Acid Sequence, Anemia, Aplastic, Animals, Base Sequence, Carrier Proteins, Cats, Leukemia Virus, Feline, Cricetinae, Humans, Molecular Sequence Data, Receptors, Virus, Tissue Distribution, Gene Expression, CHO Cells, 3T3 Cells, Caenorhabditis elegans, Sequence Homology, Amino Acid, DNA, Complementary, Mice

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