HIV-1 Nef associates with p22-phox, a component of the NADPH oxidase protein complex

Cellular Immunology

Volumn 263, Issue 2, 2010, Pages 166-171

  Salmen, Siham ^a   Colmenares, Melisa ^a   Peterson, Darrel L ^b   Reyes, Elbert ^a   Rosales, Jose D ^a   Berrueta, Lisbeth ^a  

^a UNIVERSIDAD DE LOS ANDES   (Venezuela)

^b VIRGINIA COMMONWEALTH UNIVERSITY   (United States)

Author keywords

HIV; NADPH oxidase; Nef; Neutrophils; P22 phox; Superoxide

Indexed keywords

NEF PROTEIN; PROTEIN P22 PHOX; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; SUPEROXIDE; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; HUMAN; HUMAN CELL; HUMAN IMMUNODEFICIENCY VIRUS INFECTION; IMMUNOPATHOGENESIS; INNATE IMMUNITY; NEUTROPHIL; PHAGOCYTE; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION;

CLONING, MOLECULAR; FLOW CYTOMETRY; FLUORESCENT ANTIBODY TECHNIQUE; HIV-1; HUMANS; MULTIENZYME COMPLEXES; NADH, NADPH OXIDOREDUCTASES; NADPH OXIDASE; NEF GENE PRODUCTS, HUMAN IMMUNODEFICIENCY VIRUS;

HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 77953358778     PISSN: 00088749     EISSN: 10902163     Source Type: Journal    
DOI: 10.1016/j.cellimm.2010.03.012     Document Type: Article

References (32)

1. Babior B.M. NADPH oxidase. Curr. Opin. Immunol. 2004, 16:42-47.
2. de Mendez I., Homayounpour N., Leto T.L. Specificity of p47phox SH3 domain interactions in NADPH oxidase assembly and activation. Mol. Cell Biol. 1997, 17:2177-2185.
3. Nauseef W.M. Biological roles for the NOX family NADPH oxidases. J. Biol. Chem. 2008, 283:16961-16965.
4. Nisimoto Y., Motalebi S., Han C.H., Lambeth J.D. The p67(phox) activation domain regulates electron flow from NADPH to flavin in flavocytochrome b(558). J. Biol. Chem. 1999, 274:22999-23005.
5. Ago T., Nunoi H., Ito T., Sumimoto H. Mechanism for Phosphorylation-induced activation of the phagocyte NADPH Oxidase Protein p47phox. Triple replacement of serines 303, 304, and 328 with aspartates disrupts the sh3 domain-mediated intramolecular interaction in p47phox, thereby activating the oxidasethereby activating the oxidase. J. Biol. Chem. 1999, 274:33644-33653.
6. Dang P., Cross A., Babior B. Assembly of the neutrophil respiratory burst oxidase: a direct interaction between p67PHOX and cytochrome b558. Proc. Natl. Acad. Sci. 2001, 98:3001-3005.
7. Knaus U., Heyworth P., Evans T., Curnutte J., Bokoch G. Regulation of phagocyte oxygen radical production by the GTP-binding protein Rac2. Science 1991, 254:1512-1515.
8. Moskwa P., Dagher M.C., Paclet M.H., Morel F., Ligeti E. Participation of Rac GTPase activating proteins in the deactivation of the phagocytic NADPH oxidase. Biochemistry 2002, 41:10710-10716.
9. Kuritzkes D. Neutropenia, neutrophil dysfunction, and bacterial infection in patients with human immunodeficiency virus disease: the role of granulocyte colony-stimulating factor. Clin. Infect. Dis. 2000, 30:256-260.
10. Aboulafia D., Mitsuyasu R. Hematologic abnormalities in AIDS. Hematol. Oncol. Clin. North Am. 1991, 5:195-214.
11. Salmen S., Teran G., Borges L., Goncalves L., Albarran B., Urdaneta H., Montes H., Berrueta L. Increased Fas-mediated apoptosis in polymorphonuclear cells from HIV-infected patients. Clin. Exp. Immunol. 2004, 137:166-172.
12. Salmen S., Montes H., Soyano A., Hernández D., Berrueta L. Mechanisms of neutrophil death in human immunodeficiency virus-infected patients: role of reactive oxygen species, caspases and map kinase pathways. Clin. Exp. Immunol. 2007, 150:539-545.
13. Ellis M., Gupta S., Galant S., Hakim S., VandeVen C., Toy C., Cairo M.S. Impaired neutrophil function in patients with AIDS or AIDS-related complex: a comprehensive evaluation. J. Infect. Dis. 1988, 158:1268-1277.
14. Murphy P., Lane H., Fauci A., Gallin J. Impairment of neutrophil bactericidal capacity in patients with AIDS. J. Infect. Dis. 1988, 158:627-630.
15. Nielsen H., Kharazmi A., Faber V. Blood monocyte and neutrophil functions in the acquired immune deficiency syndrome. Scand. J. Immunol. 1986, 24:291-296.
16. Elbim C., Prevost M., Bouscarat F., Franzini E., Chollet-Martin S., Hakim J. Polymorphonuclear neutrophils from human immunodeficiency virus-infected patients show enhanced activation, diminished fMLP-induced l-selectin shedding, and an impaired oxidative burst after cytokine priming. Blood 1994, 84:2759-2766.
17. Elbim C., Pillet S., Prevost M., Preira A., Girard P., Rogine N., Matusani H., Hakim J., Israel N., Gougerot-Pocidalo M. Redox and activation status of monocytes from human immunodeficiency virus-infected patients: relationship with viral load. J. Virol. 1999, 73:4561-4566.
18. Okada H., Takei R., Tashiro M. HIV-1 Nef protein-induced apoptotic cytolysis of a broad spectrum of uninfected human blood cells independently of CD95(Fas). FEBS Lett. 1997, 414:603-606.
19. Quaranta M.G., Mattioli B., Giordani L., Viora M. The immunoregulatory effects of HIV-1 Nef on dendritic cells and the pathogenesis of AIDS. FASEB J. 2006, 20:2198-2208.
20. Hanna Z., Kay D.G., Rebai N., Guimond A., Jothy S., Jolicoeur P. Nef harbors a major determinant of pathogenicity for an AIDS-like disease induced by HIV-1 in transgenic mice. Cell 1998, 95:163-175.
21. Roeth J.F., Collins K.L. Human immunodeficiency virus type 1 Nef: adapting to intracellular trafficking pathways. Microbiol. Mol. Biol. Rev. 2006, 70:548-563.
22. Geyer M., Fackler O.T., Peterlin B.M. Structure-function relationships in HIV-1 Nef. EMBO Reports 2001, 2:580-585.
23. Foster J.L., Garcia J.V. HIV-1 Nef: at the crossroads. Retrovirology 2008, 5:1-13.
24. Olivetta E., Pietraforte D., Schiavoni I., Minetti M., Federico M., Sanchez M. HIV-1 Nef regulates the release of superoxide anions from human macrophages. Biochem. J. 2005, 390(Pt 2):591-602.
25. Vilhardt F., Plastre O., Sawada M., Suzuki K., Wiznerowicz M., Kiyokawa E., Trono D., Krause K.-H. The HIV-1 Nef protein and phagocyte NADPH oxidase activation. J. Biol. Chem. 2002, 277:42136-42143.
26. Liu S., Tobias R., McClure S., Styba G., Shi Q., Jackowski G. Removal of endotoxin from recombinant protein preparations. Clin. Biochem. 1997, 136:43-49.
27. Woodman R.C., Newburger P.E., Anklesaria P., Erickson R.W., Rae J., Cohen M.S., Curnutte J.T. A new X-linked variant of chronic granulomatous disease characterized by the existence of a normal clone of respiratory burst-competent phagocytic cells. Blood 1995, 85:231-241.
28. Creery D., Angel J.B., Aucoin S., Weiss W., Cameron W.D., Diaz-Mitoma F., Kumar A. Nef protein of human immunodeficiency virus and lipopolysaccharide induce expression of CD14 on human monocytes through differential utilization of interleukin-10. Clin. Diagn. Lab. Immunol. 2002, 9:1212-1221.
29. Okada H., Takei R., Tashiro M. Inhibition of HIV-1 Nef-induced apoptosis of uninfected human blood cells by serine/threonine protein kinase inhibitors, fasudil hydrochloride and M3. FEBS Lett. 1998, 422:363-367.
30. Kelley L.A., Sternberg M.J. Protein structure prediction on the web: a case study using the Phyre server. Nat. Protoc. 2009, 4:363-371.
31. Comeau S.R., Gatchell D.W., Vajda S., Camacho C.J. ClusPro: a fully automated algorithm for protein-protein docking. Nucleic Acids Res. 2004, 32:W96-99.
32. Olivetta E., Mallozzi C., Ruggieri V., Pietraforte D., Federico M., Sanchez M. HIV-1 Nef induces p47(phox) phosphorylation leading to a rapid superoxide anion release from the U937 human monoblastic cell line. J. Cell Biochem. 2009, 106:812-822.