Nature 281, 396 - 398 (04 October 1979); doi:10.1038/281396a0

A normal cell protein cross-reactive to the major Abelson murine leukaemia virus gene product

Owen N. Witte, Naomi E. Rosenberg^* & David Baltimore

Department of Biology and Center for Cancer Research, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139 and ^*Cancer Research Center, Tufts University School of Medicine, Boston, Massachusetts 02111

Abelson murine leukaemia virus (A-MuLV) is a replication-defective retrovirus capable of rapid in vivo and in vitro transformation of bone marrow lymphoid target cells. A-MuLV was isolated from a steroid treated BALB/c mouse inoculated with the replication competent Moloney-MuLV (M-MuLV)¹⁻⁴. The A-MuLV genome (5.5 kilobases) retains regions of precise homology to M-MuLV at its 5' end (1,320 bases) and 3' end (730 bases). The centre of the A-MuLV genome (3,500 bases) is non-homologous to M-MuLV and presumably represents unique sequences derived from the mouse genome by a recombinational event⁵. The only known protein encoded by the A-MuLV genome is one of MW 120,000, called P120 (refs 6, 7). About one-quarter of this protein is encoded by the 5'-terminal M-MuL V-related sequences and the rest is encoded by the A-MuLV unique sequences. P120 has been found in all cell lines transformed by the strain of A-MuLV that originally derived from ANN-1 cells², including transformed non-producer cells. P120 can be translated in vitro using A-MuLV genomic RNA as messenger RNA. P120 is a phosphoprotein but there is no evidence for glycosylation^6,8,9. We have used an anti-A-MuLV syngeneic tumour regressor serum with defined specificities to search for cross-reacting normal cellular proteins. We have identified a protein of MW 150,000 (NCP150) in metabolically labelled thymus and other lymphoid organs. NCP150 by absorption and competition analysis is closely related to the unique region of the A-MuLV P120 protein.

References

1.	Abelson, H. T. & Rabstein, L. S. Cancer Res. 30, 2208−2212 (1970). | PubMed | ISI | ChemPort |
2.	Scher, C. D. & Siegler, R. Nature 253, 729−731 (1975). | Article | PubMed | ISI | ChemPort |
3.	Rosenberg, N., Baltimore, D. & Scher, C. D. Proc. natn. Acad. Sci. U.S.A. 72, 1932−1936 (1975). | ChemPort |
4.	Rosenberg, N. & Baltimore, D. J. exp. Med. 143, 1453−1463 (1976). | Article | PubMed | ISI | ChemPort |
5.	Shields, A. thesis, M.I.T., Cambridge, Mass. (1979).
6.	Witte, O. N., Rosenberg, N., Paskind, M., Shields, A. & Baltimore, D. Proc. natn. Acad. Sci. U.S.A. 75, 2488−2492 (1978). | ChemPort |
7.	Reynolds, F. H., Sacks, T. L., Deobagkar, D. H. & Stephenson, J. R. Proc. natn. Acad. Sci. U.S.A. 75, 3974−3978 (1978). | ChemPort |
8.	Reynolds, F. H., van de Ven, W. J. M. & Stephenson, J. R. J. Virol. 28, 665−670 (1978). | PubMed | ISI |
9.	Witte, O. N., Rosenberg, N. & Baltimore, D. J. Virol. (in the press).
10.	Witte, O. N. & Baltimore, D. J. Virol. 26, 750−761 (1978). | PubMed | ChemPort |
11.	Collett, M. S., Brugge, J. S. & Erikson, R. L. Cell 15, 1363−1369 (1978). | Article | PubMed | ChemPort |
12.	Oppermann, H., Levinson, A. D., Varmus, H. E., Levintow, L. & Bishop, J. M. Proc. natn. Acad. Sci. U.S.A. 76, 1804−1808 (1979). | ChemPort |
13.	Spector, D. H. et al. Cell 13, 371−379 (1978). | Article | PubMed | ISI | ChemPort |
14.	Risser, R., Stockert, E. & Old, L. J. Proc. natn. Acad. Sci. U.S.A. 75, 3918−3922 (1978). | ChemPort |