The Journal of Experimental Medicine
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© The Rockefeller University Press, 0022-1007/1996/12/2085/ $5.00
The Journal of Experimental Medicine, Volume 184, Number 6, December 1, 1996 2085-2090

Articles

Heterogeneity Among Ly-49C Natural Killer (NK) Cells: Characterization of Highly Related Receptors with Differing Functions and Expression Patterns

Jack Brennan*,{ddagger}, Suzanne Lemieux§, J. Douglas Freeman*, Dixie L. Mager*,{ddagger}, and Fumio Takei*,||

From the * Terry Fox Laboratory, British Columbia Cancer Agency; the {ddagger} Department of Medical Genetics, and the || Department of Pathology and Laboratory Medicine, the University of British Columbia, Vancouver, British Columbia; and the § Centre de Recherche en Immunologie, Institut Armand-Frappier, Université du Québec, Laval, Québec, Canada

Ly-49C is a member of the polymorphic family of murine NK cell inhibitory receptors. The 5E6 antibody that defines a subset of NK cells responsible for the rejection of parental H-2d bone marrow by F1 mice has been shown previously to react with Ly-49C. Here, the 5E6 antibody was found to detect two Ly-49C-related molecules in B6 mice. Two cDNA clones were isolated from B6 NK cells, one identical to previously reported Ly-49CB6 and the other a novel cDNA. The deduced amino acid sequence of the latter differs from that of Ly-49CBALB at only 4 residues, whereas the previously reported Ly-49CB6 differs at 22 residues. Flow cytometric analyses of COS cells transfected with the two cDNAs showed that the 5E6 antibody binds to both Ly-49 molecules, while another anti-Ly-49C antibody, 4LO3311, binds to the newly described Ly-49C but not the previously reported Ly-49CB6. Two-color flow cytometric analysis detected 5E6+4LO3311– as well as 5E6+4LO3311+ subsets of NK cells from B6, but not BALB/c, mice. The level of Ly-49C expression on B6 NK cells detected by the 4LO3311 antibody was substantially lower than that on BALB/c NK cells. Binding specificity of the novel Ly-49CB6 was indistinguishable from that of Ly-49CBALB, whereas no binding was detectable with previously reported Ly-49CB6. These results demonstrate that the newly described Ly-49CB6, not the previously reported Ly-49CB6, is the probable B6 allelic form of Ly49C. The previously reported Ly-49CB6 must be encoded by a separate gene and should be renamed Ly-49I. The implication of these results with respect to the role of Ly-49C in hybrid resistance is discussed.

Address correspondence to Fumio Takei, Terry Fox Laboratory, British Columbia Cancer Agency, 601 West 10th Avenue, Vancouver, British Columbia, V5Z 1L3 Canada.

This work was supported by a grant from the National Cancer Institute of Canada to F. Takei and D.L. Mager, with core support provided by the British Columbia Cancer Agency.

1 Abbreviation used in this paper: CRD, carbohydrate recognition domain.


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