Dimeric Rous sarcoma virus capsid protein structure relevant to immature gag assembly

Journal of Molecular Biology

Volumn 335, Issue 1, 2004, Pages 275-282

  Nandhagopal, Narayanasamy ^a   Simpson, Alan A ^a   Johnson, Marc C ^b   Francisco, Adam B ^b   Schatz, Gisela W ^b   Rossmann, Michael G ^a   Vogt, Volker M ^b  

^a PURDUE UNIVERSITY   (United States)

^b Department of Obstetrics Gynecology   (United States)

Author keywords

Amino terminal extension; Capsid protein; Dimer formation; Immature Gag particle; Rous sarcoma virus

Indexed keywords

AMINO ACID; CAPSID PROTEIN; DIMER; GAG PROTEIN; MONOMER;

AMINO ACID COMPOSITION; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CRYSTAL STRUCTURE; DIMERIZATION; GENE DELETION; PHENOTYPE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN ASSEMBLY; PROTEIN DOMAIN; PROTEIN PROCESSING; PROTEIN PURIFICATION; PROTEIN STRUCTURE; RETROVIRUS; ROUS SARCOMA ONCOVIRUS; VIRUS ASSEMBLY; VIRUS ENVELOPE; VIRUS PARTICLE; X RAY CRYSTALLOGRAPHY;

ROUS SARCOMA VIRUS; UNIDENTIFIED RETROVIRUS;

EID: 0345118106     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2003.10.034     Document Type: Article

References (33)

1. Kräusslich H.G., Welker R. Intercellular transport of retroviral capsid components. Curr. Top. Microbiol. Immunol. 214:1996;25-63.
2. Ganser B.K., Li S., Klishko V.Y., Finch J.T., Sundquist W.I. Assembly and analysis of conical models for the HIV-1 core. Science. 283:1999;80-83.
3. Kingston R.T., Olson N.H., Vogt V.M. The organization of the mature Rous sarcoma virus as studied by cryoelectron microscopy. J. Struct. Biol. 136:2001;67-80.
4. Li S., Hill C.P., Sundquist W.I., Finch J.T. Image reconstructions of helical assemblies of the HIV-1 CA protein. Nature. 407:2000;409-413.
5. Mayo K., Huseby D., McDermott J., Arvidson B., Finlay L., Barklis E. Retrovirus capsid protein assembly arrangements. J. Mol. Biol. 325:2003;225-237.
6. Ganser B.K., Cheng A., Sundquist W.I., Yeager M. Three-dimensional structure of the M-MuLV CA protein on a lipid monolayer: a general model for retroviral capsid assembly. EMBO J. 22:2003;2886-2892.
7. Wilk T., Gross I., Gowen B.E., Rutten T., de Haas F., Welker R., et al. Organization of immature human immunodeficiency virus type 1. J. Virol. 75:2001;759-771.
8. Nermut M.V., Hockley D.J., Bron P., Thomas D., Zhang W.-H., Jones I.M. Further evidence for hexagonal organization of HIV gag protein in prebudding assemblies and immature virus-like particles. J. Struct. Biol. 123:1998;143-149.
9. Campbell S., Vogt V.M. In vitro assembly of virus-like particles with Rous sarcoma virus Gag deletion mutants: identification of the p10 domain as a morphological determinant in the formation of spherical particles. J. Virol. 71:1997;4425-4435.
10. Joshi S.M., Vogt V.M. Role of the Rous sarcoma virus p10 domain in shape determination of Gag virus-like particles assembled in vitro and with Escherichia coli. J. Virol. 74:2000;10260-10268.
11. von Schwedler U.K., Stemmler T.L., Klishko V.Y., Li S., Albertine K.H., Davis D.R., Sundquist W.I. Proteolytic refolding of the HIV-1 capsid protein amino-terminus facilitates viral core assembly. EMBO J. 17:1998;1555-1568.
12. Gross I., Hohenberg H., Huckhagel C., Kräusslich H.G. N-terminal extension of human immunodeficiency virus capsid protein converts the in vitro assembly phenotype from tubular to spherical particles. J. Virol. 72:1998;4798-4810.
13. Momany C., Kovari L.C., Prongay A.J., Keller W., Gitti R.K., Lee B.M., et al. Crystal structure of dimeric HIV-1 capsid protein. Nature Struct. Biol. 3:1996;763-770.
14. Gamble T.R., Vajdos F.F., Yoo S., Worthylake D.K., Houseweart M., Sundquist W.I., Hill C.P. Crystal structure of human cyclophilin A bound to the amino-terminal domain of HIV-1 capsid. Cell. 87:1996;1285-1294.
15. Gamble T.R., Yoo S., Vajdos F.F., von Schwedler U.K., Worthylake D.K., Wang H., et al. Structure of the carboxyl-terminal dimerization domain of the HIV-1 capsid protein. Science. 278:1997;849-853.
16. Gitti R.K., Lee B.M., Walker J., Summers M.F., Yoo S., Sundquist W.I. Structure of the amino-terminal core domain of the HIV-1 capsid protein. Science. 273:1996;231-235.
17. Berthet-Colominas C., Monaco S., Novelli A., Sibaï G., Mallet F., Cusack S. Head-to-tail dimers and interdomain flexibility revealed by the crystal structure of HIV-1 capsid protein (p24) complexed with a monoclonal antibody Fab. EMBO J. 18:1999;1124-1136.
18. Tang C., Ndassa Y., Summers M.F. Structure of the N-terminal 283-residue fragment of the immature HIV-1 Gag protein. Nature Struct. Biol. 9:2002;537-543.
19. Kingston R.L., Fitzon-Ostendorp T., Eisenmesser E.Z., Schatz G.W., Vogt V.M., Post C.B., Rossmann M.G. Structure and self-association of the Rous sarcoma virus capsid protein. Structure. 8:2000;617-628.
20. Campos-Olivas R., Newman J.L., Summers M.F. Solution structure and dynamics of the Rous sarcoma virus capsid protein and comparison with capsid proteins of other retroviruses. J. Mol. Biol. 296:2000;633-649.
21. Jin Z., Jin L., Peterson D.L., Lawson C.L. Model for lentivirus capsid core assembly based on crystal dimers of EIAV p26. J. Mol. Biol. 286:1999;83-93.
22. Khorasanizadeh S., Campos-Olivas R., Summers M.F. Solution structure of the capsid protein from the human T-cell leukemia virus type-I. J. Mol. Biol. 291:1999;491-505.
23. von Schwedler U.K., Stray K.M., Garrus J.E., Sundquist W.I. Functional surfaces of the human immunodeficiency virus type 1 capsid protein. J. Virol. 77:2003;5439-5450.
24. Worthylake D.K., Wang H., Yoo S., Sundquist W.I., Hill C.P. Structures of the HIV-1 capsid protein dimerization domain at 2.6 Å resolution. Acta Crystallog. sect. D. 55:1999;85-92.
25. Lanman J., Lam T.T., Barnes S., Sakalian M., Marshall A.G., Prevelige P.E. Jr. Identification of novel interactions in HIV-1 capsid protein assembly by high resolution mass spectrometry. J. Mol. Biol. 325:2003;759-772.
26. Nermut M.V., Bron P., Thomas D., Rumlova M., Ruml T., Hunter E. Molecular organization of Mason-Pfizer monkey virus capsids assembled from Gag polyprotein in Escherichia coli. J. Virol. 76:2002;4321-4330.
27. Brünger A.T., Adams P.D., Clore G.M., DeLano W.L., Gros P., Grosse-Kunstleve R.W., et al. Crystallography and NMR system: a new software suite for macromolecular structure determination. Acta Crystallog. sect. D. 54:1998;905-921.
28. Ma Y.M., Vogt V.M. Rous sarcoma virus Gag protein-oligonucleotide interaction suggests a critical role for protein dimer formation in assembly. J. Virol. 76:2002;5452-5462.
29. Ma Y.M., Vogt V.M. Nucleic acid binding-induced Gag dimerization in the assembly of Rous sarcoma virus particles in vitro. J. Virol. 2004;. In the press.
30. Johnson M.C., Scobie H.M., Ma Y.M., Vogt V.M. Nucleic acid-independent retrovirus assembly can be driven by dimerization. J. Virol. 76:2002;1177-1185.
31. Gross I., Hohenberg H., Wilk T., Wiegers K., Grättinger M., Müller B., et al. A conformational switch controlling HIV-1 morphogenesis. EMBO J. 19:2000;103-113.
32. Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:1997;307-326.
33. Navaza J. AMoRe: an automated package for molecular replacement. Acta Crystallog. sect. A. 50:1994;157-163.