Natural Resistance to Intracellular Infections: Nramp1 Encodes a Membrane Phosphoglycoprotein Absent in Macrophages from Susceptible (Nramp1D169) Mouse Strains

Journal of Immunology

Volumn 157, Issue 8, 1996, Pages 3559-3568

  Vidal, Silvia M ^a   Pinner, Elhanan ^b   Lepage, Pierre ^c   Gauthier, Susan ^b   Gros, Philippe ^b  

^a MONTREAL GENERAL HOSPITAL   (Canada)

^b MCGILL UNIVERSITY   (Canada)

^c HARVARD MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODY; CARRIER PROTEIN; CATION TRANSPORT PROTEIN; COMPLEMENTARY DNA; HYBRID PROTEIN; MEMBRANE PROTEIN; NATURAL RESISTANCE ASSOCIATED MACROPHAGE PROTEIN 1; NATURAL RESISTANCE-ASSOCIATED MACROPHAGE PROTEIN 1;

AMINO ACID SEQUENCE; ANIMAL; ARTICLE; GENETICS; GLYCOSYLATION; IMMUNIZATION; IMMUNOLOGY; INNATE IMMUNITY; LEISHMANIA; METABOLISM; MOLECULAR GENETICS; MOUSE; MOUSE STRAIN; MUTATION; MYCOBACTERIUM; NUCLEOTIDE SEQUENCE; ONCOGENE MYC; PERITONEUM MACROPHAGE; PHOSPHORYLATION; SACCHAROMYCES CEREVISIAE; SALMONELLA;

AMINO ACID SEQUENCE; ANIMALS; ANTIBODIES; BASE SEQUENCE; CARRIER PROTEINS; CATION TRANSPORT PROTEINS; DNA, COMPLEMENTARY; GENES, MYC; GLYCOSYLATION; IMMUNITY, NATURAL; IMMUNIZATION; LEISHMANIA; MACROPHAGES, PERITONEAL; MEMBRANE PROTEINS; MICE; MICE, INBRED STRAINS; MOLECULAR SEQUENCE DATA; MUTATION; MYCOBACTERIUM; PHOSPHORYLATION; RECOMBINANT FUSION PROTEINS; SACCHAROMYCES CEREVISIAE; SALMONELLA;

EID: 0030587961     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (51)

1. Gros, P., E. Skamene, and A. Forget. 1981. Genetic control of natural resistance to Mycobacterium bovis BCG. J. Immunol. 127:2417.
2. Skamene, E., P. Gros, A. Forget, P. A. L. Kongshavn, C. St.-Charles, and B. A. Taylor. 1982. Genetic regulation of resistance to intracellular pathogens. Nature 297:506.
3. Gros, P., E. Skamene, and A. Forget. 1983. Cellular mechanisms of genetically-controlled host resistance to Mycobacterium bovis (BCG). J. Immunol. 131:1966.
4. Lissner, C. R., R. N. Swanson, and A. D. O'Brien. 1983. Genetic control of the innate resistance of mice to Salmonella typhimurium: expression of the Ity gene in peritoneal and splenic macrophages isolated in vitro. J. Immunol. 131:3006.
5. Stach, J. L., P. Gros, A. Forget, and E. Skamene. 1984. Phenotypic expression of genetically controlled natural resistance to Mycobacterium bovis (BCG). J. Immunol. 132:888.
6. Crocker, P. R., J. M. Blackwell, and D. J. Bradley. 1984. Expression of the natural resistance gene Lsh in resident liver macrophages. Infect. Immun. 43: 1033.
7. Goto, Y., E. Buschman, and E. Skamene. 1989. Regulation of host resistance to Mycobacterium intracellulare in vivo and in vitro by the Bcg gene. Immunogenetics 30:218.
8. Radzioch, D., T. Hudson, M. Boule, L. Barrera, J. W. Urbance, L. Varesio, and E. Skamene. 1991. Genetic resistance/susceptibility to mycobacteria: phenotypic expression in bone marrow derived macrophage lines. J. Leukocyte Biol. 50:263.
9. Vidal, S. M., D. Malo, K. Vogan, E. Skamene, and P. Gros. 1993. Natural resistance to infection with intracellular parasites: identification of a candidate gene for Bcg. Cell 73:469.
10. Vidal, S., M. L. Tremblay, G. Govoni, S. Gauthier, G. Sebastiani, D. Malo, E. Skamene, M. Olivier, S. Jothy, and P. Gros. 1995b. The Ity/Lsh/Bcg locus: natural resistance to infection with intracellular parasites is abrogated by disruption of the Nramp1 gene. J. Exp. Med. 182:655.
11. Govoni, G., S. Vidai, M. Cellier, P. Lepage, D. Malo, and P. Gros. 1995. Structural organization and cell specific expression of the mouse Nramp1 gene. Genomics 27:9.
12. Cellier, M., G. Privé, A. Belouchi, T. Kwan, V. Rodrigues, W. Chia, and P. Gros. 1995. Nramp defines a family of membrane proteins. Proc. Natl. Acad. Sci. USA 92:10089.
13. Cellier, M., G. Govoni, S. Vidal, N. Groulx, J. Liu, F. Sanchez, E. Skamene, H. Schurr, and P. Gros. 1994. Human natural resistance-associated macrophage protein: cDNA cloning, chromosomal mapping, genomic organization, and tissue-specific expression. J. Exp Med. 180:1741.
14. Hu, J., N. Bumstead, E. Skamene, P. Gros, and D. Malo. 1996. Structural organization, sequence, and expression of the chicken NRAMP1 gene encoding the natural resistance-associated macrophage protein 1. DNA Cell Biol. 15:113.
15. Rodrigues, V., P. Y. Cheah, K. Ray, and W. Chia. 1995. Malvolio, the Drosophila homologue of mouse NRAMP-1 (Bcg), is expressed in macrophages and in the nervous system and is required for normal taste behavior. EMBO J. 14:3007.
16. West, A. H., D. J. Clark, J. Martin, W. Neupert, F.-U. Hartl, and A. L. Horwich. 1992. Two related genes encoding extremely hydrophobic proteins suppress a lethal mutation in the yeast mitochondrial processing enhancing protein. J. Biol. Chem. 267:24625.
17. Belouchi, A., M. Cellier, T. Kwan, H. S. Saini, G. Leroux, and P. Gros. 1995. The macrophage-specific membrane protein Nramp controlling natural resistance to infections in mice has homologues expressed in the root system of plants. Plant. Mol. Biol. 29:1181.
18. Cellier, M., A. Belouchi, and P. Gros. 1996 Resistance to intracellular infections: comparative genome analysis on NRAMP. Trends Genet. 12:201.
19. 2-terminal sequence of macrophage-expressed natural resistance-associated macrophage protein Nramp encodes a proline/serine-rich putative Src homology 3-binding domain. J. Exp. Med. 179:1115.
20. Gruenheid, S., M. Cellier, S. Vidal, and P. Gros. 1995. Identification and characterization of a second mouse Nramp gene. Genomics 25:514.
21. Vidal, S., A.-M. Belouchi, M. Cellier, B. Beatty, and P. Gros. 1995. a. Cloning and characterization of a second human NRAMP gene on chromosome 12q13. Mammalian Gen. 6:224.
22. Malo, D., K. Vogan, S. Vidal, J. Hu, M. Cellier, E. Schurr, A. Fuks, N. Bumstead, K. Morgan, and P. Gros. 1994. Haplotype mapping and sequence analysis of the mouse Nramp gene predicts susceptibility to infection with intracellular parasites. Genomics 23:51.
23. Smith, D. B., and K. S. Johnson. 1988, Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione 5-transferase. Gene 67:31.
24. Kaelin, W. G., Jr., D. C. Pallas, J. A. DeCaprio, F. J. Kaye, and D. M. Livingston. 1991. Identification of cellular proteins that can interact specifically with the T/E1A-binding region of the retinoblasloma gene product. Cell 64:521.
25. Evan, G. I., G. Lewis, G. Ramsay, and J. M. Bishop. 1985. Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product. Mol. Cell. Biol. 5:3610.
26. Vernet, T., D. Dingard, and D. Y. Thomas. 1987. A family of yeast expression vectors containing the phage f1 intergenic region. Gene 52:225.
27. Hinnebusch, A. G., and S. W. Liebman. 1991. The Molecular and Cellular Biology of the Yeast Saccharomyces. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, p. 627.
28. Ito, H., K. Fokuda, K. Murata, and A. Kimura. 1983. Transformation of intact yeast cells treated with alkali calions. J. Bacteriol. 153:163.
29. Sherman, F., G. R. Fink, and J. B. Hicks. 1982. Methods in Yeast Genetics. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY.
30. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680.
31. Denis, M., A. Forget, M. Pelletier, F. Gervais, and E. Skamene. 1990. Killing of Mycobacterium smegmatis by macrophages from genetically susceptible and resistant mice J. Leukocyte Biol. 47:25.
32. Kolodziej, P. A., and R. A. Young. 1991. Epitope tagging and protein surveillance. Methods Enzymol. 194:508.
33. Raymond, M., P. Gros, M. Whiteway, and D. Thomas. 1992. Functional complementation of the yeast ste-6 mutation by a mammalian multidrug resistance gene. Science 256:232.
34. Tarentino, A. L., T. H. Plummer, Jr., and F. Maley. 1974. The release of intact oligosaccharides from specific glycoproteins by endo-beta-N-acetylglucosaminidase H. J. Biol. Chem. 249:818.
35. Plummer, T. H., Jr., J. H. Elder, S. Alexander, A. W. Phelan, and A. L. Tarentino. 1984. Demonstration of peptide:N-glycosidase F activity in endo-beta-N-acetyl-glucosaminidase F preparations. J. Biol. Chem. 259:10700.
36. Bairoch, A. 1993. The PROSITE dictionary of sites and patterns in proteins: its current status. Nucleic Acids Res. 2:3097.
37. Hibbs, J. B., Z. Vavrin, and R. R. Taintor. 1987. Macrophage cytotoxicity: role of arginine deaminase and imino nitrogen oxidation to nitrite. Science 253:423.
38. Chandy, K. G., and G. A. Gutman. 1995. Ligand and voltage-gated ion channels. In Handbook of Receptors and Channels. R. A. North, ed. CRC Press, Boca Raton, FL, p. 1.
39. Huang, M. E., J. C. Chuat, and F. Galibert. 1994. A voltage-gated chloride channel in the yeast Saccharomyces cerevisiae. J. Mol. Biol. 242:595.
40. + channels and glutamate receptors. Proc. Natl. Acad. Sci. USA 92:4882.
41. Ruetz, S., M. Brault, C. Kast, C. Hamenway, J. Heitman, C. E. Grant, S. P. C. Cole, R. G. Deeley, and P. Gros. 1996. Functional expression of the multidrug resistance-associated protein in the yeast Saccharomyces cerevisiae. J. Biol. Chem. 271:4154.
42. Ruetz, S., and P. Gros. 1994. Phosphatidylcholine translocase: a physiological role of the mdr2 gene. Cell 77:1071.
43. Levitan, I. B. 1994. Modulation of ion channels by protein phosphorylation and dephosphorylation. Annu. Rev. Physiol. 56:193.
44. Howe, C. L., B. L. Granger, M. Hull, S. A. Green, C. A. Gabel, A. Helenius, and I. Mellman. 1988. Derived protein sequence, oligosaccharides, and membrane insertion of the 120-kDa lysosomal membrane glycoprotein (Igp120): identification of a highly conserved family of lysosomal membrane glycoproteins. Proc. Natl. Acad. Sci. USA 85:7577.
45. Fukuda, M. 1991. Lysosomal membrane glycoproteins: structure, biosynthesis and intracellular trafficking. J. Biol. Chem. 266:21327.
46. Kishi, F., and M. Nobumoto. 1995. Identification of natural resistance-associated macrophage protein in peripheral blood lymphocytes. Immunol. Lett. 47:93.
47. Fra, A., and R. Sitia. 1993. The endoplasmic reticulum as a site of protein degradation. Subcell. Biochem. 21:143.
48. Ward, C. L., O. Satoshi, and R. R. Kopito. 1995. Degradation of CFTR by the ubiquitin-proteasome pathway. Cell 83:121.
49. Jensen, T. J., M. A. Loo, S. Pind, D. B. Williams, A. L. Goldberg, and J. Riordan. 1995. Multiple proteolytic systems, including the proteasome, contribute to CFTR processing. Cell 83:129.
50. Desjardins, M. 1995. Biogenesis of phagolysosomes: the "kiss and run" hypothesis. Trends Cell. Biol. 5:183.
51. Liu, J., T. M. Fujiwara, N. T. Buu, F. O. Sanchez, M. Cellier, A.-J. Paradis, D. Frappier, E. Skamene, P. Gros, K. Morgan, and E. Schurr. 1995. Identification of polymorphisms and sequence variants in the human homologue of the mouse natural resistance-associated macrophage protein gene, a candidate gene for susceptibility to tuberculosis. Am. J. Hum. Genet. 56:845.