Nonmyristoylated Matrix Protein from the Mason–Pfizer Monkey Virus Forms Oligomers

Vlach, Jiří; Srb, Pavel; Prchal, Jan; Grocký, Marián; Lang, Jan; Ruml, Tomáš; Hrabal, Richard

doi:10.1016/j.jmb.2009.05.063

Cited by 11 publications

(36 citation statements)

References 56 publications

(58 reference statements)

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“…Recently, we have suggested that the increased propensity of M-PMV MA to form specific oligomers helps to stabilize the outer layer of the virions 9. Our current results support such conclusion and show that the virus has developed an efficient mechanism of the formation of oligomers.…”

Section: Discussionsupporting

confidence: 87%

“…16 This procedure yielded τ M values significantly longer than the values predicted by HydroNMR (Table 2). This result is, however, in agreement with the specific WT MA oligomerization manifested as a monomer–dimer–trimer equilibrium in which approximately a half of monomeric units is engaged in oligomers at 1.1 mM concentration 9. In order to keep the number of motional parameters as low as possible, we describe the oligomerization by a simpler monomer–dimer model in this work.…”

Section: Resultssupporting

confidence: 78%

“…Global correlation time τ M of 8.6 ns was found for WT MA using the known K D of 0.76 mM9. In the case of R55F MA, the calculation was carried out for several K D values and the lowest χ 2 between the fitted and experimental data was found for K D of 1.5 mM, yielding τ M of 7.9 ns.…”

Section: Resultsmentioning

confidence: 96%

“…9, 19 All NMR experiments were measured on Bruker DRX 500 Avance NMR spectrometer (basic frequency 500.13 MHz for 1 H) at 25 °C. Spectral widths were set to 7 kHz for 1 H and 1.52 kHz for 15 N, with 2048 and 200 complex points respectively.…”

Section: Methodsmentioning

confidence: 99%

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Oligomerization of a Retroviral Matrix Protein Is Facilitated by Backbone Flexibility on Nanosecond Time Scale

et al. 2011

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Oligomerization capacity of the retroviral matrix protein is an important feature that affects assembly of immature virions and their interaction with cellular membrane. A combination of NMR relaxation measurements and advanced analysis of molecular dynamics simulation trajectory provided an unprecedentedly detailed insight into internal mobility of matrix proteins of the Mason-Pfizer monkey virus. Strong evidences have been obtained that the oligomerization capacity of the wild type matrix protein is closely related to the enhanced dynamics of several parts of its backbone on ns timescale. Increased flexibility has been observed for two regions: the loop between α-helices α2 and α3 and the C-terminal half of α-helix α3 which accommodate amino acid residues that form the oligomerization interface. On the other hand, matrix mutant R55F that has changed structure and does not exhibit any specific oligomerization in solution was found considerably more rigid. Our results document that conformational selection mechanism together with induced fit and favorable structural pre-organization play an important role in the control of the oligomerization process. Supporting informationThe RMSD versus starting structure of both WT and R55F MA molecules during MD simulation trajectory is shown in Fig. S1. Figure S2 shows examples of correlation functions and S 2 (w) for time window length ranging from 0 to 100 ns. The experimental NMR relaxation data are provided for WT MA (Tab. S1) and R55F MA (Tab. S2). The complete sets of the resulting experimentbased motional parameters are shown for two types of the fitting procedures: with monomer-dimer equilibrium included (Tables S3 and S4) and without considering the monomer-dimer equilibrium presence (Tables S5 and S6). Also the full sets of dihedral angle distribution from MD trajectories of WT MA for monomer, dimer and trimer are shown (Fig. S3 -S5). This material is available free of charge at

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Section: Discussionsupporting

confidence: 87%

Section: Resultssupporting

confidence: 78%

Section: Resultsmentioning

confidence: 96%

Section: Methodsmentioning

confidence: 99%

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Oligomerization of a Retroviral Matrix Protein Is Facilitated by Backbone Flexibility on Nanosecond Time Scale

et al. 2011

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“…Recently, we have reported that in contrast to the HIV-1 MA, the non-myristoylated M-PMV MA protein readily forms trimers upon increasing its concentration in solution[15]. The increased oligomerization capacity of M-PMV MA is probably related to the necessity to stabilize Gag within the capsid shell[15].…”

Section: Introductionmentioning

confidence: 99%

Expression and purification of myristoylated matrix protein of Mason-Pfizer monkey virus for NMR and MS measurements

Prchal

Junková

Strmiskova

et al. 2011

Protein Expression and Purification

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Matrix proteins play multiple roles both in early and late stages of the viral replication cycle. Their N-terminal myristoylation is important for interaction with the host cell membrane during virus budding. We used Escherichia coli, carrying N-myristoyltransferase gene, for the expression of the myristoylated His-tagged matrix protein of Mason-Pfizer monkey virus. An efficient, single-step purification procedure eliminating all contaminating proteins including, importantly, the non-myristoylated matrix protein was designed. The comparison of NMR spectra of matrix protein with its myristoylated form revealed substantial structural changes induced by this fatty acid modification.

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Molecular aspects of the interaction between Mason—Pfizer monkey virus matrix protein and artificial phospholipid membrane

et al. 2016

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The Mason-Pfizer monkey virus is a type D retrovirus, which assembles its immature particles in the cytoplasm prior to their transport to the host cell membrane. The association with the membrane is mediated by the N-terminally myristoylated matrix protein. To reveal the role of particular residues which are involved in the capsid-membrane interaction, covalent labelling of arginine, lysine and tyrosine residues of the Mason-Pfizer monkey virus matrix protein bound to artificial liposomes containing 95% of phosphatidylcholine and 5% phosphatidylinositol-(4,5)-bisphosphate (PI(4,5)P ) was performed. The experimental results were interpreted by multiscale molecular dynamics simulations. The application of these two complementary approaches helped us to reveal that matrix protein specifically recognizes the PI(4,5)P molecule by the residues K20, K25, K27, K74, and Y28, while the residues K92 and K93 stabilizes the matrix protein orientation on the membrane by the interaction with another PI(4,5)P molecule. Residues K33, K39, K54, Y66, Y67, and K87 appear to be involved in the matrix protein oligomerization. All arginine residues remained accessible during the interaction with liposomes which indicates that they neither contribute to the interaction with membrane nor are involved in protein oligomerization. Proteins 2016; 84:1717-1727. © 2016 Wiley Periodicals, Inc.

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Nonmyristoylated Matrix Protein from the Mason–Pfizer Monkey Virus Forms Oligomers

Cited by 11 publications

References 56 publications

Oligomerization of a Retroviral Matrix Protein Is Facilitated by Backbone Flexibility on Nanosecond Time Scale

Oligomerization of a Retroviral Matrix Protein Is Facilitated by Backbone Flexibility on Nanosecond Time Scale

Expression and purification of myristoylated matrix protein of Mason-Pfizer monkey virus for NMR and MS measurements

Molecular aspects of the interaction between Mason—Pfizer monkey virus matrix protein and artificial phospholipid membrane

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