Budding is the final step of the late phase of retroviral life cycle. It begins with the interaction of Gag precursor with plasma membrane (PM) through its N-terminal domain, the matrix protein (MA). However, single genera of Retroviridae family differ in the way how they interact with PM. While in case of Lentiviruses (e.g., human immunodeficiency virus) the structural polyprotein precursor Gag interacts with cellular membrane prior to the assembly, Betaretroviruses [Mason-Pfizer monkey virus (M-PMV)] first assemble their virus-like particles (VLPs) in the pericentriolar region of the infected cell and therefore, already assembled particles interact with the membrane. Although both these types of retroviruses use similar mechanism of the interaction of Gag with the membrane, the difference in the site of assembly leads to some differences in the mechanism of the interaction. Here we describe the interaction of M-PMV MA with PM with emphasis on the structural aspects of the interaction with single phospholipids.

Department of Biochemistry and Microbiology Institute of Chemical Technology Prague Czech Republic

Laboratory of NMR Spectroscopy Institute of Chemical Technology Prague Czech Republic

Laboratory of NMR Spectroscopy Institute of Chemical Technology Prague Czech Republic ; Department of Biochemistry and Microbiology Institute of Chemical Technology Prague Czech Republic

Zobrazit více v PubMed

Bryant M., Ratner L. (1990). Myristoylation-dependent replication and assembly of human immunodeficiency virus-1. Proc. Natl. Acad. Sci. U.S.A. 87 523–52710.1073/pnas.87.2.523 PubMed DOI PMC

Chen K., Bachtair I., Piszczek G., Bouamr F., Carter C., Tjandra N. (2008). Solution NMR characterizations of oligomerization and dynamics of equine infectious anemia virus matrix protein and its interaction with PIP2. Biochemistry 47 1928–193710.1021/bi701984h PubMed DOI PMC

Chopra H. C., Mason M. M. (1970). A new virus in a spontaneous mammary tumor of a rhesus monkey. Cancer Res. 30 2081–2086 PubMed

Chukkapalli V., Hogue I. B., Boyko V., Hu W. S., Ono A. (2008). Interaction between the human immunodeficiency virus type 1 Gag matrix domain and phosphatidylinositol-(4,5)-bisphosphate is essential for efficient Gag membrane binding. J. Virol. 82 2405–241710.1128/JVI.01614-07 PubMed DOI PMC

Freed E. O. (1998). HIV-1 Gag proteins: diverse functions in the virus life cycle. Virology 251 1–1510.1006/viro.1998.9398 PubMed DOI

Hamard-Peron E., Juillard F., Saad J. S., Roy C., Roingeard P., Summers M. F., et al. (2010). Targeting of murine leukemia virus Gag to the plasma membrane is mediated by PI(4,5)P-2/PS and a polybasic region in the matrix. J. Virol. 84 503–51510.1128/JVI.01134-09 PubMed DOI PMC

Hunter E. (1994). Macromolecular interactions in the issembly of hiv and other retroviruses. Semin. Virol. 5 71–8310.1006/smvy.1994.1008 DOI

Montiel N. A. (2010). An updated review of simian Betaretrovirus (SRV) in macaque hosts. J. Med. Primatol. 39 303–31410.1111/j.1600-0684.2010.00412.x PubMed DOI

Peitzsch R. M., Mclaughlin S. (1993). Binding of acylated peptides and fatty-fcids to phospholipid-vesicles - pertinence to myristoylated proteins. Biochemistry 32 10436–1044310.1021/bi00090a020 PubMed DOI

Prchal J., Srb P., Hunter E., Ruml T., Hrabal R. (2012). The structure of myristoylated Mason-Pfizer monkey virus matrix protein and the role of phosphatidylinositol-(4,5)-bisphosphate in its membrane binding. J. Mol. Biol. 423 427–43810.1016/j.jmb.2012.07.021 PubMed DOI PMC

Rhee S. S., Hunter E. (1991). Amino acid substitutions within the matrix protein of type D retroviruses affect assembly, transport and membrane association of a capsid. EMBO J. 10 535–546 PubMed PMC

Roth M. G. (2004). Phosphoinositides in constitutive membrane traffic. Physiol. Rev. 84 699–73010.1152/physrev.00033.2003 PubMed DOI

Saad J. S., Ablan S. D., Ghanam R. H., Kim A., Andrews K., Nagashima K., et al. (2008). Structure of the myristylated human immunodeficiency virus type 2 matrix protein and the role of phosphatidylinositol-(4,5)-bisphosphate in membrane targeting. J. Mol. Biol. 382 434–44710.1016/j.jmb.2008.07.027 PubMed DOI PMC

Saad J. S., Miller J., Tai J., Kim A., Ghanam R. H., Summers M. F. (2006). Structural basis for targeting hiv-1 Gag proteins to the plasma membrane for virus assembly. Proc. Natl. Acad. Sci. U.S.A. 103 11364–1136910.1073/pnas.0602818103 PubMed DOI PMC

Stansell E., Apkarian R., Haubova S., Diehl W. E., Tytler E. M., Hunter E. (2007). Basic residues in the Mason-Pfizer monkey virus gag matrix domain regulate intracellular trafficking and capsid-membrane interactions. J. Virol. 81 8977–898810.1128/JVI.00657-07 PubMed DOI PMC

Stansell E., Tytler E., Walter M. R., Hunter E. (2004). An early stage of Mason-Pfizer monkey virus budding is regulated by the hydrophobicity of the gag matrix domain core. J. Virol. 78 5023–503110.1128/JVI.78.10.5023-5031.2004 PubMed DOI PMC

Sugiki T., Takeuchi K., Yamaji T., Takano T., Tokunaga Y., Kumagai K., et al. (2012). Structural basis for the golgi association by the pleckstrin homology domain of the ceramide trafficking protein (CERT). J. Biol. Chem. 287 33706–3371810.1074/jbc.M112.367730 PubMed DOI PMC

Tang C., Loeliger E., Luncsford P., Kinde I., Beckett D., Summers M. F. (2004). Entropic switch regulates myristate exposure in the HIV-1 matrix protein. Proc. Natl. Acad. Sci. U.S.A. 101 517–52210.1073/pnas.0305665101 PubMed DOI PMC

Vlach J., Lipov J., Rumlova M., Veverka V., Lang J., Srb P., et al. (2008). D-retrovirus morphogenetic switch driven by the targeting signal accessibility to Tctex-1 of dynein. Proc. Natl. Acad. Sci. U.S.A. 105 10565–1057010.1073/pnas.0801765105 PubMed DOI PMC

Vlach J., Saad J. S. (2013). Trio engagement via plasma membrane phospholipids and the myristoyl moiety governs HIV-1 matrix binding to bilayers. Proc. Natl. Acad. Sci. U.S.A. 110 3525–353010.1073/pnas.1216655110 PubMed DOI PMC

Zhou W., Parent L. J., Wills J. W., Resh M. D. (1994). Identification of a membrane-binding domain within the amino-terminal region of human immunodeficiency virus type 1 Gag protein which interacts with acidic phospholipids. J. Virol. 68 2556-2569 PubMed PMC

Zhou W., Resh M. D. (1996). Differential membrane binding of the human immunodeficiency virus type 1 matrix protein. J. Virol. 70 8540–8548 PubMed PMC