Characterization of the amino-terminal domain of Mx2/MxB-dependent interaction with the HIV-1 capsid

doi:10.1007/s13238-014-0113-5

Protein Cell

2014, Vol. 5

Issue (12) : 954-957 https://doi.org/10.1007/s13238-014-0113-5

LETTER

Characterization of the amino-terminal domain of Mx2/MxB-dependent interaction with the HIV-1 capsid

Jia Kong^1,²,Bo Xu^1,²,Wei Wei^2,^3,⁴,Xin Wang^1,²,Wei Xie^1,^2,^*(

),Xiao-Fang Yu^1,^2,^3,^4,^*(

)

1. School of Life Science, Tianjin University, Tianjin 300072, China
2. Collaborative Innovation Center of Chemical Science and Engineering, Tianjin 300072, China
3. Department of Molecular Microbiology and Immunology, Johns Hopkins Bloomberg School of Public Health, Baltimore, MD 21205, USA
4. Institute of Virology and AIDS Research, First Hospital of Jilin University, Changchun 130061, China

Download: PDF(609 KB)
Export: BibTeX | EndNote | Reference Manager | ProCite | RefWorks

Corresponding Author(s): Wei Xie

Issue Date: 30 December 2014

Cite this article:

Jia Kong,Bo Xu,Wei Wei, et al. Characterization of the amino-terminal domain of Mx2/MxB-dependent interaction with the HIV-1 capsid[J]. Protein Cell, 2014, 5(12): 954-957.

URL:

https://academic.hep.com.cn/pac/EN/10.1007/s13238-014-0113-5
https://academic.hep.com.cn/pac/EN/Y2014/V5/I12/954

1	Busnadiego I, Kane M, Rihn SJ, Preugschas HF, Hughes J, Blanco-Melo D, Strouvelle VP, Zang TM, Willett BJ, Boutell C (2014) Host and Viral Determinants of Mx2 Antiretroviral Activity. J Virol88: 7738-7752 https://doi.org/10.1128/JVI.00214-14
2	Chappie JS, Acharya S, Leonard M, Schmid SL, Dyda F (2010) G domain dimerization controls dynamin’s assembly-stimulated GTPase activity. Nature465: 435-440 https://doi.org/10.1038/nature09032
3	Fricke T, White T, Schulte B, de Souza Aranha Vieira D, Dharan A, Campbell E, Brandariz-Nunez A, Diaz-Griffero F (2014) Mx2 binds to the HIV-1 core and prevents the uncoating process of HIV-1. Retrovirology11: 68 https://doi.org/10.1186/s12977-014-0068-x
4	Gao S, von der Malsburg A, Paeschke S, Behlke J, Haller O, Kochs G, Daumke O (2010) Structural basis of oligomerization in the stalk region of dynamin-like MxA. Nature465: 502-506 https://doi.org/10.1038/nature08972
5	Gao S, von der Malsburg A, Dick A, Faelber K, Schr?der, Gunnar F, Haller O, Kochs G, Daumke O (2011) Structure of myxovirus resistance protein A reveals intra-and intermolecular domain interactions required for the antiviral function. Immunity35: 514-525 https://doi.org/10.1016/j.immuni.2011.07.012
6	Goujon C, Moncorge O, Bauby H, Doyle T, Ward C, Schaller T, Hue S, Barclay W, Schulz R, Malim M (2013) Human MX2 is an interferon-induced post-entry inhibitor of HIV-1 infection. Nature502: 559-562 https://doi.org/10.1038/nature12542
7	Haller O, Gao S, von der Malsburg A, Daumke O, Kochs G (2010) Dynamin-like MxA GTPase: structural insights into oligomerization and implications for antiviral activity. J Biol Chem285: 28419-28424 https://doi.org/10.1074/jbc.R110.145839
8	Hung M, Niedziela-Majka A, Jin D, Wong M, Leavitt S, Brendza KM, Liu X, Sakowicz R (2013) Large-scale functional purification of recombinant HIV-1 capsid. PLoS One8: e58035 https://doi.org/10.1371/journal.pone.0058035
9	Kane M, Yadav S, Bitzegeio J, Kutluay S, Zang T, Wilson S, Schoggins J, Rice C, Yamashita M, Hatziioannou T (2013) MX2 is an interferon-induced inhibitor of HIV-1 infection. Nature502: 563-566 https://doi.org/10.1038/nature12653
10	Lindenmann J (1962) Resistance of mice to mouse-adapted influenza A virus. Virology16: 203-204 https://doi.org/10.1016/0042-6822(62)90297-0
11	Liu Z, Pan Q, Ding S, Qian J, Xu F, Zhou J, Cen S, Guo F, Liang C (2013) The interferon-inducible Mx2 protein inhibits HIV-1 infection. Cell Host Microbe14: 398-410 https://doi.org/10.1016/j.chom.2013.08.015
12	Melen K, Keskinen P, Ronni T, Sareneva T, Lounatmaa K, Julkunen I (1996) Human Mx2 protein, an interferon-alpha-inducible GTPase, contains a nuclear targeting signal and is localized in the heterochromatin region beneath the nuclear envelope. J Biol Chem271: 23478-23486 https://doi.org/10.1074/jbc.271.38.23478
13	Pornillos O, Ganser-Pornillos BK, Yeager M (2011) Atomic-level modelling of the HIV capsid. Nature469: 424-427 https://doi.org/10.1038/nature09640
14	Stremlau M, Perron M, Lee M, Li Y, Song B, Javanbakht H, Diaz-Griffero F, Anderson D, Sundquist W, Sodroski J (2006) Specific recognition and accelerated uncoating of retroviral capsids by the TRIM5alpha restriction factor. Proc Natl Acad Sci USA103: 5514-5519 https://doi.org/10.1073/pnas.0509996103
15	Yang H, Ji X, Zhao G, Ning J, Zhao Q, Aiken C, Gronenborn AM, Zhang P, Xiong Y (2012) Structural insight into HIV-1 capsid recognition by rhesus TRIM5α. Proc Natl Acad Sci USA109: 18372-18377 https://doi.org/10.1073/pnas.1210903109

[1]

Supplementary Material

Download

Viewed

Full text

Abstract

Cited

Shared

Discussed