putative cell surface receptor for anemia-inducing feline leukemia virus subgroup C is a member of a transporter superfamily
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Published in | Journal of Virology Vol. 73; no. 8; pp. 6500 - 6505 |
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Format | Journal Article |
Language | English |
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American Society for Microbiology
01.08.1999
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ISSN | 0022-538X 1098-5514 |
DOI | 10.1128/jvi.73.8.6500-6505.1999 |
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AbstractList | 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. Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue JVI About JVI Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JVI RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0022-538X Online ISSN: 1098-5514 Copyright © 2014 by the American Society for Microbiology. For an alternate route to JVI .asm.org, visit: JVI 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.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. |
Author | Willett, B.J Kabat, D Tailor, C.S |
AuthorAffiliation | Department of Biochemistry and Molecular Biology, Oregon Health Sciences University, Portland, Oregon 97201-3098, 1 and Department of Veterinary Pathology, University of Glasgow, Glasgow G61 1QH, United Kingdom 2 |
AuthorAffiliation_xml | – name: Department of Biochemistry and Molecular Biology, Oregon Health Sciences University, Portland, Oregon 97201-3098, 1 and Department of Veterinary Pathology, University of Glasgow, Glasgow G61 1QH, United Kingdom 2 |
Author_xml | – sequence: 1 fullname: Tailor, C.S – sequence: 2 fullname: Willett, B.J – sequence: 3 fullname: Kabat, D |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/10400745$$D View this record in MEDLINE/PubMed |
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Notes | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 Corresponding author. Mailing address: Department of Biochemistry and Molecular Biology, Oregon Health Sciences University, 3181 SW Sam Jackson Park Rd., Mail Code L224, Portland, OR 97201-3098. Phone: (503) 494-2548. Fax: (503) 494-8393. E-mail: tailorc@ohsu.edu and kabat@ohsu.edu. |
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Mendeley... Domestic cats infected with the horizontally transmitted feline leukemia virus subgroup A (FeLV-A) often produce mutants (termed FeLV-C) that bind to a... |
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SubjectTerms | 3T3 Cells Amino Acid Sequence Anemia, Aplastic Anemia, Aplastic - virology Animals Base Sequence Caenorhabditis elegans Carrier Proteins Carrier Proteins - chemistry Carrier Proteins - classification Carrier Proteins - genetics Cats chemistry CHO Cells classification complementary DNA Cricetinae DNA, Complementary Feline leukemia virus genbank/af18637 Gene Expression genetics Humans Leukemia Virus, Feline Leukemia Virus, Feline - metabolism metabolism Mice Molecular Sequence Data nucleotide sequences receptors Receptors, Virus Receptors, Virus - chemistry Receptors, Virus - classification Receptors, Virus - genetics Sequence Homology, Amino Acid T-lymphocytes Tissue Distribution virology Virus-Cell Interactions |
Title | putative cell surface receptor for anemia-inducing feline leukemia virus subgroup C is a member of a transporter superfamily |
URI | http://jvi.asm.org/content/73/8/6500.abstract https://www.ncbi.nlm.nih.gov/pubmed/10400745 https://www.proquest.com/docview/17257197 https://www.proquest.com/docview/48664514 https://www.proquest.com/docview/69887716 https://pubmed.ncbi.nlm.nih.gov/PMC112732 |
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