Three-dimensional structure and antigenicity of transmembrane-protein peptides of the human immunodeficiency virus type 1 (original) (raw)

Abstract

A point mutation (Ala-589 to Thr) in the transmembrane protein of the human immtmodeficlency vnus type 1 (HIV-I ) has been shown to decrease the sensitivity of the virus to the neutralizing effect of human HIV-1 specific antibodIes [( 1990) J Vlrol 64. 3240-32481. Here 17-residue peptides with the parental and mutant sequences were compared. the parental peptide bound antibodies of sera from HIV-l infected persons more frequently and with higher affinity than the mutant peptide. However. according to cu-cular dlchrolsm (CD). NMR spectroscopy and molecular modelling the peptides habe inchstingulshable backbone conformations under a variety of experimental condltlons. These techmquea showed for both peptldes that no ordered hehx was present m water solution. However, for both pepttdes in alcohol-water solutions approximately 60% a-hehx coulu be induced. The three-dimenslonal structures of these pcptides provide a basis for understandmg how this mutation in the transmembrane protein may affect the interactlon with both the outer envelope glycoprotein and with antlbodies.

Loading...

Loading Preview

Sorry, preview is currently unavailable. You can download the paper by clicking the button above.

References (26)

  1. Wilson. C.. Rettz Jr., MS., Aldrich. K . Klasse. P J.. Blomberg, J., Gallo. R.C. and Robert-Guroff, M. t 1990) J Vtrol. 64. 3240- 3248.
  2. Garnier. J., Osguthorpe. D.J. and Robson, B. (1978) J. Mol. B~ol. 120.97-120.
  3. Reitz Jr..
  4. M S.. Wtlson, C.. Naugle. C.. Gallo. R.C. and Robert- Guroff, M. (1988) Cell 54, 57-63.
  5. 41 [51 PI ]71 181 [91 PO1 IIll PA 1131 u41 u51 U61 [I71 [181 [I91 [W Pll [31] P31 Cianctolo. G.J., Bogerd. H. and Synderman. R. (1988) Immunol.
  6. Lett. 19, 7-14.
  7. Ruegg, C.K , Monell. C.R. and Strand, M. ( 1989) J. Vtrol. 63. 3257-3260.
  8. Qureshi, N.M., Coy, D.H., Carry, R.F. and Hendersson, L.A. (1990) AIDS 4. 5533558.
  9. Han. K.-H.. NIU. C.-H, Roller, P.P. and Ferretti. J.A. (1988) Biopolymers 27. 9233937.
  10. Dyson. H.J , Cross. K J., Houghten. R.A.. Wilson, I A.. Wrtght, P.E. and Lerner. R.A. (1985) Nature 318. 480483. Dyson. H.J.. Rance. M.. Houghten, R.A., Wrtght. P.E and Lerner, R.A. (1987) in: Biological Orpamzatton: Macromolecular Interactions at High Resolution (Burnett, R.M. and Vogel. H.S. Eds.) pp. 227-234. Academtc Press, New York.
  11. Oldstone. M.B.A., Ttshon, A., Lewickt, H.. Dyson. H J., Feher. V.A.. Assa-Munt.
  12. N. and Wnght, P.E (1991) J. Vtrol. 65, 17377 1734.
  13. Klasse, P.J.. Ptpkorn. R. and Blomberg. J. (1988) Proc. Nat] Acad. Sm. USA 85. 5225-5229.
  14. Kennedy, R.C.. Henkel. D.. Paolettt, D., Allan. J S.. Lee. T.H. and Essex. M. (1986) Science 231, 1556-1559.
  15. Klasse, P.J., Pipkorn, R. and Blomberg. J. (1991) Mol. Immunol. 28, 613-622.
  16. Provencher. SW and Glonecker, J. (1981) Biochemistry 20, 33-
  17. Bax, A. and Davts, D.G. (1985) J. Magn. Reson. 65. 3555360. Bothner-By, A A., Stephens. R.L . Lee. J.. Warren, C.D. and Jeanloz. R.W. (1984) J. Am. Chem. Sot. 106. 81 l-813
  18. Billeter. M.. Braun. W. and Wtithrich. K. (1982) J. Mol Biol. 155. 32 I-346
  19. Han. K.-H., Syi. J.-L, Brooks. B.R. and Ferretti, J A. (1990) Proc. Nat].
  20. Acad. Scl. USA 87, 2818-2822.
  21. Marqusee. S. and Baldwin. R.L. (1987) Proc. Nat). Acad. SCI. USA 84. 8898-8902.
  22. Pinter. A.. Honnen. W.J.. Tilley, S A.. Bona. C., Zaghouani. H.. Gorny. M.K. and Zolia-Pasner.
  23. S. (1989) J. Vtrol. 63.2675-2679.
  24. Perry. N.. Fox. G., Rowlands. D.. Brown, F.. Fry. E.. Acharya.
  25. R , Logan, D. and Stuart. D. (1990) Nature 347. 5699572. Kowalskl. M., Potz. J.. Bastrtpour, L.. Dorfman. T.. Goh. WC., Terwtlhger. E., Dayton, A. Rosen. C.. Haseltinr. W. and Sodroskt. J. (1987) Sctence 237. 1351 1355
  26. McKeatmg, J.A., McKnight, A. and Moore, J.P (1991) J. Virol. 65. 8522860.