Post-translational modification of glutamine and lysine residues of HIV-1 aspartyl protease by transglutaminase increases its catalytic activity

Biochemical and Biophysical Research Communications

Volumn 393, Issue 3, 2010, Pages 546-550

  Lentini, Alessandro ^a   Tabolacci, Claudio ^a   Melino, Sonia ^a   Provenzano, Bruno ^a   Beninati, Simone ^a  

^a UNIVERSITY OF ROME TOR VERGATA   (Italy)

Author keywords

HIV 1 aspartyl protease; Polyamine; Protein cross linking; Transglutaminase; Virus

Indexed keywords

ASPARTIC PROTEINASE; BLOOD CLOTTING FACTOR 13A; CALCIUM; EPSILON(GAMMA GLUTAMYL)LYSINE; GLUTAMINE; HUMAN IMMUNODEFICIENCY VIRUS 1 ASPARTIC PROTEINASE; LYSINE; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; SPERMIDINE; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CROSS LINKING; DIMERIZATION; INCUBATION TIME; NONHUMAN; PRIORITY JOURNAL;

ANIMALS; ASPARTIC ACID PROTEASES; CATALYSIS; ENZYME ACTIVATION; FACTOR XIIIA; GLUTAMINE; GUINEA PIGS; HIV-1; HUMANS; LIVER; LYSINE; PROTEIN PROCESSING, POST-TRANSLATIONAL; SPERMIDINE; TRANSGLUTAMINASES;

CAVIA; HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 77949272188     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.02.060     Document Type: Article

References (32)

1. Kohl N.E., Emini E.A., Schleif W.A., Davis L.J., Heimbach J.C., Dixon R.A., Scolnick E.M., and Sigal I.S. Active human immunodeficiency virus protease is required for viral infectivity. Proc. Natl. Acad. Sci. USA 85 (1988) 4686-4690
2. Hoetelmans R.M., Meenhorst P.L., Mulder J.W., Burger D.M., Koks C.H., and Beijnen J.H. Clinical pharmacology of HIV protease inhibitors: focus on saquinavir, indinavir, andritonavir. Pharm. World Sci. 19 (1997) 159-175
3. Patick A.K., Boritzki T.J., and Bloom L.A. Activities of the human immunodeficiency virus type 1 (HIV-1) protease inhibitor nelfinavir mesylate in combination with reverse transcriptase and protease inhibitors against acute HIV-1 infection in vitro. Antimicrob. Agents Chemother. 41 (1997) 2159-2164
4. Kaushik-Basu N., Basu A., and Harris D. Peptide inhibition of HIV-1: current status and future potential. BioDrugs 22 (2008) 161-175
5. Sardana V.V., Schlabach A.J., Graham P., Bush B.L., Condra J.H., Culberson J.C., Gotlib L., Graham D.J., Kohl N.E., LaFemina R.L., et al. Human immunodeficiency virus type 1 protease inhibitors: evaluation of resistance engendered by amino acid substitutions in the enzyme's substrate binding site. Biochemistry 33 (1994) 2004-2010
6. Ermolieff J., Lin X., and Tang J. Kinetic properties of saquinavir-resistant mutants of human immunodeficiency virus type 1 protease and their implications in drug resistance in vivo. Biochemistry 36 (1997) 12364-12370
7. Mastrolorenzo A., Rusconi S., Scozzafava A., Barbaro G., and Supuran C.T. Inhibitors of HIV-1 protease: current state of the art 10 years after their introduction. From antiretroviral drugs to antifungal, antibacterial and antitumor agents based on aspartic protease inhibitors. Curr. Med. Chem. 14 (2007) 2734-2748
8. Brodt H.R., Kamps B.S., Gute P., Knupp B., Staszewski S., and Helm E.B. Changing incidence of AIDS-defining illnesses in the era of antiretroviral combination therapy. AIDS 11 (1997) 1731-1738
9. McKinnon J.E., Mellors J.W., and Swindells S. Simplification strategies to reduce antiretroviral drug exposure: progress and prospects. Antivir. Ther. 14 (2009) 1-12
10. Caflisch A., Schramm H.J., and Karplus M. Design of dimerization inhibitors of HIV-1 aspartic proteinase: a computer-based combinatorial approach. J. Computer-Aided Mol. Des. 14 (2000) 161-179
11. Todd M.J., Semo N., and Freire E. The structural stability of the HIV-1 protease. J. Mol. Biol. 283 (1998) 475-488
12. Xie D., Gulnik S., Gustchina E., Yu B., Shao W., Qoronfleh W., Nathan A., and Erickson J.W. Drug resistance mutations can effect dimer stability of HIV-1 protease at neutral pH. Protein Sci. 8 (1999) 1702-1707
13. Levy Y., and Caflisch A. The flexibility of monomeric and dimeric HIV-1 PR. J. Phys. Chem. B107 (2003) 3068-3079
14. Levy Y., Caflisch A., Onuchic J.N., and Wolynes P.G. The folding and dimerization of HIV-1 protease: evidence for a stable monomer from simulations. J. Mol. Biol. 340 (2004) 67-79
15. Folk J.E., and Finlayson J.S. The ε-(γ-glutamyl)lysine crosslink and the catalytic role of transglutaminases. Adv. Protein Chem. 31 (1977) 1-133
16. Folk J.E. Mechanism and basis for specificity of transglutaminase-catalyzed ε-(γ-glutamyl) lysine bond formation. Adv. Enzymol. 54 (1983) 1-56
17. Beninati S., and Mukherjee A.B. A novel transglutaminase-catalyzed posttranslational modification of HIV-1 aspartyl protease. Biochem. Biophys. Res. Commun. 187 (1992) 1211-1218
18. 4-bis(γ-glutamyl)putrescine. Methods Enzymol. 94 (1983) 451-457
19. Min B.S., Hattori M., Lee H.K., and Kim Y.H. Inhibitory constituents against HIV-1 protease from Agastache rugosa. Arch Pharm Res. 22 (1999) 75-77
20. Folk J.E., Park M.H., Chung S.I., Schrode J., Lester E.P., and Cooper H.L. Polyamines as physiological substrates for transglutaminases. J. Biol. Chem. 255 (1980) 3695-3700
21. Beninati S., Martinet N., and Folk J.E. High-performance liquid chromatographic method for the determination of ε-(γ-glutamyl)lysine and mono- and bis-γ-glutamyl derivatives of putrescine and spermidine. J. Chromatogr. 443 (1988) 329-335
22. Folk J.E. Transglutaminases. Ann. Rev. Biochem. 49 (1980) 517-531
23. Davies P.J.A., Chiocca E.A., Basilion J.P., Poddar S., and Stein J.P. Transglutaminases and their regulation: implications for polyamine metabolism. Adv. Exp. Med. Biol. 250 (1988) 391-401
24. Birckbichler P.J., Orr G.R., Carter H.A., and Patterson Jr. M.K. Catalytic formation of ε-(γ-glutamyl)lysine in guinea pig liver transglutaminase. Biochem. Biophys. Res. Commun. 78 (1977) 1-7
25. Lorand L., and Conrad S.M. Transglutaminases. Mol. Cell. Biochem. 58 (1984) 9-35
26. Beninati S., and Folk J.E. Covalent polyamine-protein conjugates: analysis and distribution. Adv. Exp. Med. Biol. 250 (1988) 411-422
27. Schneider J., and Kent S.B.H. Enzymatic activity of a synthetic 99 residue protein corresponding to the putative HIV-1 protease. Cell 54 (1988) 363-368
28. Ishima R., Ghirlando R., Tözsér J., Gronenborn A.M., Torchia D.A., and Louis J.M. Folded monomer of HIV-1 protease. J. Biol. Chem. 276 (2001) 49110-49116
29. Cordella-Miele E., Miele L., and Mukherjee A.B. A novel transglutaminase-mediated post-translational modification of phospholipase A2 dramatically increases its catalytic activity. J. Biol. Chem. 265 (1990) 17180-17188
30. Bergamini A., Capozzi M., Ghibelli L., Salanitro A., Milanese G., Wagner T., Beninati S., Pesce C.D., Amici C., and Rocchi G. Cystamine potently suppresses in vitro HIV replication in acutely and chronically infected human cells. J. Clin. Invest. 93 (1994) 2251-2257
31. Amendola A., Fesus L., Piacentini M., and Szondy Z. "Tissue" transglutaminase in AIDS. J. Immunol. Methods 265 (2002) 145-159
32. Nardacci R., Antinori A., Larocca L.M., Arena V., Amendola A., Perfettini J.L., Kroemer G., and Piacentini M. Characterization of cell death pathways in human immunodeficiency virus-associated encephalitis. Am. J. Pathol. 167 (2005) 695-704