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A Putative Cell Surface Receptor for Anemia-Inducing Feline Leukemia Virus Subgroup C Is a Member of a Transporter Superfamily
Open accessAbstract
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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“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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Metadata
- Authors
- Tailor, C. S., Willett, B. J., & Kabat, D.
- Affiliations
- Oregon Health & Science University (US)
- University of Glasgow (GB)
- ORCID
- Willett, Brian J.
- Venue
- Journal of Virology
- Publisher
- American Society for Microbiology
- Published
- 1999-08
- Volume
- 73
- Issue
- 8
- Pages
- 6500-6505
- ISSN
- 0022-538X (ISSN-L)
- 1098-5514
- PMC
- PMC112732
- 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
- green
- www.ncbi.nlm.nih.gov
- 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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