Isolation of a Clone of Chinese Hamster Ovary Cells Deficient in Plant Lectin-Binding Sites
Open accessAbstract
Ricin, a galactose-binding lectin with potent cytotoxic activity, was used to select a clone of Chinese hamster ovary cells with altered plant lectin-binding properties. The clone (15B) is 80-fold less sensitive to the toxic action of ricin than the parent line. In the absence of ricin, it grows both in monolayer and suspension culture with a normal generation time. Plating efficiency, however, is significantly reduced. Relative to the parent cells, its binding of the Ricinus communis lectins, Phaseolus vulgaris erythroagglutinating phytohemagglutinin, Abrus precatorius phytohemagglutinin, and soybean phytohemagglutinin is less than 7%, while binding of lentil phytohemagglutinin, wheat-germ agglutinin, and mushroom phytohemagglutinin is 17%, 40%, and 109%, respectively. In contrast, its concanavalin A binding is increased by 70%. Consistent with these alterations, crude membrane preparations of the 15B cells were found to contain the same sugars as the parent-cell membranes but in different proportions. The 15B membranes have 28% less sialic acid, 38% less N -acetylglucosamine, 49% less galactose, the same amount of N -acetylgalactosamine, and 53% more mannose than the membranes of the parent cells.
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- Authors
- Gottlieb, C., Skinner, S. A. M., & Kornfeld, S.
- Affiliations
- Washington University in St. Louis (US)
- ORCID
- Kornfeld, Stuart
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1974-04
- Volume
- 71
- Issue
- 4
- Pages
- 1078-1082
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC388166
- OpenAlex
- W2011296435
- Cited by
- 117
- References
- 24
- Citations by year
- 2021: 1 · 2018: 2 · 2016: 2 · 2013: 3 · 2012: 2
- FWCI
- 5.11
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Life Sciences › Immunology and Microbiology › Immunology › Toxin Mechanisms and Immunotoxins
- Life Sciences › Immunology and Microbiology › Immunology › Galectins and Cancer Biology
- Keywords
- ricin, CHO cells, galactose-specific lectin, cell surface carbohydrates, membrane glycosylation, sialic acid, N-acetylglucosamine, galactose, mannose, concanavalin A binding, phytohemagglutinin
- MeSH terms
- Animals, Binding Sites, Binding Sites, Antibody, Cell Membrane, Clone Cells, Female, Cricetinae, Iodine Radioisotopes, Ovary, Ricin, Lectins
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