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This article is part of the supplement: 15th International Conference on Human Retroviruses: HTLV and Related Viruses

Open Access Meeting abstract

Structure of the xenotropic murine leukaemia virus-related virus matrix protein

Michal Doležal12, Iva Pichová1, Tomáš Ruml2, Richard Hrabal3 and Michaela Rumlová1*

Author Affiliations

1 Institute of Organic Chemistry and Biochemistry, IOCB Research Centre and Gilead Sciences, Academy of Sciences of the Czech Republic, Prague, 166 10, Czech Republic

2 Department of Biochemistry and Microbiology, Institute of Chemical Technology Prague, Prague, 166 28, Czech Republic

3 Laboratory of NMR spectroscopy, Institute of Chemical Technology Prague, Prague, 166 28, Czech Republic

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Retrovirology 2011, 8(Suppl 1):A227  doi:10.1186/1742-4690-8-S1-A227

The electronic version of this article is the complete one and can be found online at: http://www.retrovirology.com/content/8/S1/A227


Published:6 June 2011

© 2011 Doležal et al; licensee BioMed Central Ltd.

This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Meeting abstract

We present the preparation of the xenotropic murine leukaemia virus-related virus matrix protein (XMRV-MA) and its structure determined by NMR spectroscopy.

The DNA fragment encoding XMRV-MA was obtained from prostate tumour cell cDNA (Rv1 cell line) by PCR and inserted into a pET-22b plasmid. Non-myristoylated, uniformly 13C- and 15N-labeled XMRV-MA, fused with histidine tag, was produced in E. coli BL21 (DE3) cells. The protein was purified by immobilized metal affinity chromatography (NiNTA-agarose) and size-exclusion chromatography (Sephadex 75), and then concentrated to 5 mg/ml.

All NMR data were collected at 298 K on a 600 MHz Bruker Avance III spectrometer equipped with a cryogenic triple-resonance probe and analyzed with CcpNmr Analysis. Back-bone and side-chain resonances were assigned using standard NMR experiments and structural constraints were obtained from 13C- and 15N-edited NOESY experiments. Structures were calculated with ARIA.

Although the protein sequence of the XMRV-MA is very similar to that of the murine leukaemia virus matrix protein (MLV-MA), it varies in several amino acid residues. We compared the structures of the XMRV-MA and MLV-MA and found that those changes are localized in a few domains, mostly on the surface of the protein.