Inhibition of XMRV and HIV-1 proteases by pepstatin A and acetyl-pepstatin

FEBS Journal

Volumn 279, Issue 17, 2012, Pages 3276-3286

  Matúz, Krisztina ^a   Mótyán, János ^a   Li, Mi ^b,c   Wlodawer, Alexander ^b   Tözsér, József ^a  

^a UNIVERSITY OF DEBRECEN   (Hungary)

^b NATIONAL CANCER INSTITUTE   (United States)

^c SAIC FREDERICK INC   (United States)

Author keywords

aspartic protease; crystal structure; enzyme inhibition; inhibitor binding; retrovirus

Indexed keywords

ACETYL PEPSTATIN; ASPARTIC PROTEINASE; HUMAN IMMUNODEFICIENCY VIRUS PROTEINASE; PEPSTATIN; UNCLASSIFIED DRUG; XENOTROPIC MULV RELATED VIRUS PROTEINASE;

ARTICLE; BINDING AFFINITY; COMPLEX FORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME BINDING; ENZYME INHIBITION; HUMAN IMMUNODEFICIENCY VIRUS 1; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN INTERACTION; XENOTROPIC MULV RELATED VIRUS;

AMINO ACID SEQUENCE; DIMERIZATION; HIV-1; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPSTATINS; PEPTIDE HYDROLASES; PROTEASE INHIBITORS; SEQUENCE HOMOLOGY, AMINO ACID; XENOTROPIC MURINE LEUKEMIA VIRUS-RELATED VIRUS;

HUMAN IMMUNODEFICIENCY VIRUS 1; XENOTROPIC MURINE LEUKEMIA VIRUS;

EID: 84865246590     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2012.08714.x     Document Type: Article

References (32)

1. Kohl NE, Emini EA, Schleif WA, Davis LJ, Heimbach JC, Dixon RA, Scolnick EM, &, Sigal IS, (1988) Active human immunodeficiency virus protease is required for viral infectivity. Proc Natl Acad Sci USA 85, 4686-4690.
2. Wlodawer A, &, Vondrasek J, (1998) Inhibitors of HIV-1 protease: a major success of structure-assisted drug design. Annu Rev Biophys Biomol Struct 27, 249-284.
3. Scourfield A, Waters L, &, Nelson M, (2011) Drug combinations for HIV: what's new? Expert Rev Anti Infect Ther 9, 1001-1011.
4. Poiesz BJ, Ruscetti FW, Reitz MS, Kalyanaraman VS, &, Gallo RC, (1981) Isolation of a new type C retrovirus (HTLV) in primary uncultured cells of a patient with Sézary T-cell leukaemia. Nature 294, 268-271.
5. Groom HC, &, Bishop KN, (2012) The tale of xenotropic murine leukemia virus-related virus. J Gen Virol 93, 915-924.
6. Paprotka T, Delviks-Frankenberry KA, Cingöz O, Martinez A, Kung HJ, Tepper CG, Hu WS, Fivash MJ Jr, Coffin JM, &, Pathak VK, (2011) Recombinant origin of the retrovirus XMRV. Science 333, 97-101.
7. Eizert H, Bander P, Bagossi P, Sperka T, Miklóssy G, Boross P, Weber IT, &, Tozsér J, (2008) Amino acid preferences of retroviral proteases for amino-terminal positions in a type 1 cleavage site. J Virol 82, 10111-10117.
8. Li M, Dimaio F, Zhou D, Gustchina A, Lubkowski J, Dauter Z, Baker D, &, Wlodawer A, (2011a) Crystal structure of XMRV protease differs from the structures of other retropepsins. Nat Struct Mol Biol 18, 227-229.
9. Seelmeier S, Schmidt H, Turk V, &, von der Helm K, (1988) Human immunodeficiency virus has an aspartic-type protease that can be inhibited by pepstatin A. Proc Natl Acad Sci USA 85, 6612-6616.
10. Giam CZ, &, Boros I, (1988) In vivo and in vitro autoprocessing of human immunodeficiency virus protease expressed in Escherichia coli. J Biol Chem 263, 14617-14620.
11. Hansen J, Billich S, Schulze T, Sukrow S, &, Moelling K, (1988) Partial purification and substrate analysis of bacterially expressed HIV protease by means of monoclonal antibody. EMBO J 7, 1785-1791.
12. Richards AD, Roberts R, Dunn BM, Graves MC, &, Kay J, (1989) Effective blocking of HIV-1 proteinase activity by characteristic inhibitors of aspartic proteinases. FEBS Lett 247, 113-117.
13. Fitzgerald PM, McKeever BM, Van Middlesworth JF, Springer JP, Heimbach JC, Leu CT, Herber WK, Dixon RA, &, Darke PL, (1990) Crystallographic analysis of a complex between human immunodeficiency virus type 1 protease and acetyl-pepstatin at 2.0-A resolution. J Biol Chem 265, 14209-14219.
14. Miller M, Schneider J, Sathyanarayana BK, Toth MV, Marshall GR, Clawson L, Selk L, Kent SB, &, Wlodawer A, (1989) Structure of complex of synthetic HIV-1 protease with a substrate-based inhibitor at 2.3 A resolution. Science 246, 1149-1152.
15. Li M, Gustchina A, Matúz K, Tözsér J, Namwong S, Goldfarb NE, Dunn BM, &, Wlodawer A, (2011) Structural and biochemical characterization of the inhibitor complexes of xenotropic murine leukemia virus-related virus protease. FEBS J 278, 4413-4424.
16. Kádas J, Boross P, Weber IT, Bagossi P, Matúz K, &, Tozsér J, (2008) C-terminal residues of mature human T-lymphotropic virus type 1 protease are critical for efficient dimerization and for catalytic activity. Biochem J 416, 357-364.
17. Menendez-Arias L, Gotte D, &, Oroszlan S, (1993) Moloney murine leukemia virus protease: bacterial expression and characterization of the purified enzyme. Virology 196, 557-563.
18. Bagossi P, Sperka T, Fehér A, Kádas J, Zahuczky G, Miklóssy G, Boross P, &, Tozsér J, (2005) Amino acid preferences for a critical substrate binding subsite of retroviral proteases in type 1 cleavage sites. J Virol 79, 4213-4218.
19. Menéndez-Arias L, Weber IT, Soss J, Harrison RW, Gotte D, &, Oroszlan S, (1994) Kinetic and modeling studies of subsites S4-S3′ of Moloney murine leukemia virus protease. J Biol Chem 269, 16795-16801.
20. Wondrak EM, &, Louis JM, (1996) Influence of flanking sequences on the dimer stability of human immunodeficiency virus type 1 protease. Biochemistry 35, 12957-12962.
21. Olivares I, Mulky A, Boross PI, Tozsér J, Kappes JC, López-Galíndez C, &, Menéndez-Arias LJ, (2007) HIV-1 protease dimer interface mutations that compensate for viral reverse transcriptase instability in infectious virions. J Mol Biol 372, 369-381.
22. Liu F, Boross PI, Wang YF, Tozsér J, Louis JM, Harrison RW, &, Weber IT, (2005) Kinetic, stability, and structural changes in high-resolution crystal structures of HIV-1 protease with drug-resistant mutations L24I, I50V, and G73S. J Mol Biol 354, 789-800.
23. Hoog SS, Towler EM, Zhao B, Doyle ML, Debouck C, &, Abdel-Meguid SS, (1996) Human immunodeficiency virus protease ligand specificity conferred by residues outside of the active site cavity. Biochemistry 35, 10279-10286.
24. Gillette WK, Esposito D, Taylor TE, Hopkins RF, Bagni RK, &, Hartley JL, (2010) Purify First: rapid expression and purification of proteins from XMRV. Protein Expr Purif 76, 238-247.
25. Mahalingam B, Louis JM, Hung J, Harrison RW, &, Weber IT, (2001) Structural implications of drug-resistant mutants of HIV-1 protease: high-resolution crystal structures of the mutant protease/substrate analogue complexes. Proteins 43, 455-464.
26. Fehér A, Boross P, Sperka T, Miklóssy G, Kádas J, Bagossi P, Oroszlan S, Weber IT, &, Tozsér J, (2006) Characterization of the murine leukemia virus protease and its comparison with the human immunodeficiency virus type 1 protease. J Gen Virol 87, 1321-1330.
27. Otwinowski Z, &, Minor W, (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276, 307-326.
28. McCoy AJ, Grosse-Kunstleve RW, Adams PD, Winn MD, Storoni LC, &, Read RJ, (2007) Phaser crystallographic software. J Appl Crystallogr 40, 658-674.
29. Murshudov GN, Skubak P, Lebedev AA, Pannu NS, Steiner RA, Nicholls RA, Winn MD, Long F, &, Vagin AA, (2011) REFMAC5 for the refinement of macromolecular crystal structures. Acta Crystallogr D Biol Crystallogr 67, 355-367.
30. Emsley P, &, Cowtan K, (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60, 2126-2132.
31. Brünger AT, (1992) The free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-474.
32. DeLano WL, (2002) The PyMOL Molecular Graphics System. DeLano Scientific, San Carlos, CA.