Abstract
AbstractGag protein oligomerization, an essential step during virus assembly, results in budding of spherical virus particles. This process is critically dependent on the spacer p2, located between the capsid and the nucleocapsid proteins. P2 contributes also, in association with NCp7, to specific recognition of the HIV‐1 packaging signal resulting in viral genome encapsidation. There is no structural information about the 20 last amino acids of the C‐terminal part of capsid (CA[CTD]) and p2, in the molecular mechanism of Gag assembly. In this study the structure of a peptide encompassing the 14 residues of p2 with the upstream 21 residues and the downstream 13 residues was determined by 1H NMR in 30% trifluoroethanol (TFE). The main structural motif is a well‐defined amphipathic α‐helix including p2, the seven last residues of the CA(CTD), and the two first residues of NCp7. Peptides containing the p2 domain have a strong tendency to aggregate in solution, as shown by gel filtration analyses in pure H2O. To take into account the aggregation phenomena, models of dimer and trimer formed through hydrophobic or hydrophilic interfaces were constructed by molecular dynamic simulations. Gel shift experiments demonstrate that the presence of at least p2 and the 13 first residues of NCp7 is required for RNA binding. A computer‐generated model of the Gag polyprotein segment (282–434)Gag interacting with the packaging element SL3 is proposed, illustrating the importance of p2 and NCp7 in genomic encapsidation.
References
63
Referenced
74
10.1128/JVI.72.3.2072-2078.1998
/ J. Virol. / A putative α‐helical structure which overlaps the capsid‐P2 boundary in the human immunode‐ficiency virus type 1 Gag precursor is crucial for viral particle assembly by Accola M.A. (1998)10.1074/jbc.273.13.7177
10.1093/emboj/18.5.1124
10.1021/bi00185a041
10.1128/JVI.71.6.4425-4435.1997
{'key': 'e_1_2_7_7_1', 'first-page': '539', 'volume-title': 'Biophysical chemistry, part II: Techniques for the study of biological structure and function', 'author': 'Cantor C.R.', 'year': '1980'}
/ Biophysical chemistry, part II: Techniques for the study of biological structure and function by Cantor C.R. (1980)10.1128/JVI.77.12.7058-7066.2003
10.1128/jvi.69.4.2101-2109.1995
/ J. Virol. / RNA secondary structure and binding sites for gag gene products in the 5′packaging signal of human immunodeficiency virus type 1 by Clever J. (1995)10.1006/viro.1998.9374
10.1126/science.279.5349.384
10.1016/S0006-291X(05)81166-0
10.1073/pnas.89.14.6472
10.1006/immu.1994.1014
10.1016/0022-2836(88)90447-0
10.1016/S0006-3495(01)75725-6
10.1126/science.278.5339.849
10.1006/viro.1998.9237
10.1021/bi00411a020
10.1021/ja00231a044
10.1093/emboj/19.1.103
10.1093/protein/7.3.309
10.1128/jvi.66.4.1856-1865.1992
10.1016/S0079-6565(99)00003-5
10.1128/JVI.72.7.5877-5885.1998
/ J. Virol. / Nonreciprocal packaging of human immunodeficiency virus type 1 and type 2 RNA: A possible role for the P2 domain of Gag in RNA encapsidation by Kaye J.F. (1998)10.1016/S0969-2126(00)00148-9
10.1128/jvi.69.6.3407-3419.1995
/ J. Virol. / The spacer peptide between human immunodeficiency virus capsid and nucleocapsid proteins is essential for ordered assembly and viral infectivity by Krausslich H.G. (1995)10.1128/JVI.72.1.564-577.1998
/ J. Virol. / Genetic determinants of Rous sarcoma virus particle size by Krishna N.K. (1998)10.1016/0006-291X(80)90695-6
10.1083/jcb.200303200
10.1038/35030177
10.1073/pnas.2234683100
10.1128/JVI.76.22.11729-11737.2002
10.1128/JVI.76.11.5452-5462.2002
10.1016/S0022-2836(02)01176-2
10.1006/jmbi.2000.4030
10.1007/BF00227466
10.1038/nsb0996-763
10.1128/JVI.72.9.7659-7663.1998
/ J. Virol. / Detection of a trimeric human immunodeficiency virus type 1 Gag intermediate is dependent on sequences in the matrix protein, p17 by Morikawa Y. (1998)10.1128/JVI.74.1.16-23.2000
10.1021/ja00034a071
10.1021/bi00438a050
10.1128/JVI.76.9.4321-4330.2002
10.1110/ps.04614804
10.1016/S0021-9258(18)98720-X
10.1007/BF02192855
10.1016/0006-291X(83)91225-1
10.1038/378743a0
10.1074/jbc.M405632200
10.1016/S0300-9084(97)83501-8
10.1016/S0006-3495(98)77804-X
10.1006/viro.1993.1210
10.1128/jvi.67.7.4264-4273.1993
10.1128/JVI.72.10.7950-7959.1998
/ J. Virol. / Analysis of minimal human immunodeficiency virus type 1 gag coding sequences capable of virus‐like particle assembly and release by Wang C.T. (1998)10.1111/j.1432-1033.1997.00523.x
10.1128/JVI.72.4.2846-2854.1998
10.1128/JVI.75.2.759-771.2001
10.1016/0022-2836(91)90214-Q
10.1107/S0907444998007689
10.1051/epn/19861701011
10.1023/A:1008382624724
10.1128/JVI.75.6.2753-2764.2001
10.1128/JVI.72.3.1782-1789.1998
10.1016/S0006-3495(00)76600-8
Dates
Type | When |
---|---|
Created | 20 years, 7 months ago (Jan. 18, 2005, 11:27 p.m.) |
Deposited | 1 year, 10 months ago (Oct. 12, 2023, 8:30 p.m.) |
Indexed | 11 months, 3 weeks ago (Sept. 6, 2024, 1:43 p.m.) |
Issued | 20 years, 7 months ago (Feb. 1, 2005) |
Published | 20 years, 7 months ago (Feb. 1, 2005) |
Published Online | 16 years, 8 months ago (Jan. 1, 2009) |
Published Print | 20 years, 7 months ago (Feb. 1, 2005) |
@article{Morellet_2005, title={Helical structure determined by NMR of the HIV‐1 (345–392)Gag sequence, surrounding p2: Implications for particle assembly and RNA packaging}, volume={14}, ISSN={1469-896X}, url={http://dx.doi.org/10.1110/ps.041087605}, DOI={10.1110/ps.041087605}, number={2}, journal={Protein Science}, publisher={Wiley}, author={Morellet, Nelly and Druillennec, Sabine and Lenoir, Christine and Bouaziz, Serge and Roques, Bernard P.}, year={2005}, month=feb, pages={375–386} }