Ein, Gag, DLS, Structure, Interface, Biological dimerBackground The Feline Immunodeficiency Virus > 자유게시판

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Ein, Gag, DLS, Structure, Interface, Biological dimerBackground The Feline Immunodeficiency Virus (FIV) is an enveloped virus from the family Retroviridae, genus lentivirus, which also contains the human immunodeficiency virus (HIV), equine infectious anemia virus (EIAV) and simian immunodeficiency virus (SIV). FIV infection induces an* Correspondence: christophe.guillon@ibcp.fr Laboratoire de Biocristallographie et Biologie Structurale des Cibles Th apeutiques, IBCP-BMSSI, UMR 5086 CNRS Universit?de Lyon, SFR BioSciences Gerland-Lyon Sud, 7 Passage du Vercors, 69367 Lyon, Cedex 07, Franceimmunodeficiency syndrome in infected domestic cats or wild felids, which resembles HIV-induced AIDS. Therefore, this syndrome has been dubbed feline AIDS. FIV is an important veterinary issue as it infects up to 30 of domestic cats in some parts of the world with apparently no evolution of host resistance [1,2]. Moreover, FIV has been described as a useful model for the development PubMed ID:https://www.ncbi.nlm.nih.gov/pubmed/23410069 of AIDS vaccines, antiretroviral drugs, and non-pathogenic gene therapy vectors [3,4]. However, compared to primate lentiviruses, many fundamental aspects of FIV biology are not well understood, and no?2013 Serri e 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.Serri e et al. Retrovirology 2013, 10:64 http://www.retrovirology.com/content/10/1/Page 2 ofstructural data are available except for two of the viral enzymes, the dUTP-pyrophosphatase [5], and the protease [6,7]. Matrix protein (MA), p15 in FIV Fmoc-D-Asp-OtBu or EIAV and p17 in HIV or SIV, is the N-terminal subunit of the retroviral Gag polyprotein. This Gag polyprotein is involved in the architecture of the viral particle, which is common to HIV and FIV and is essential for infectivity of the virus [8-10]. The MA subunit of Gag is also PubMed ID:https://www.ncbi.nlm.nih.gov/pubmed/13867361 involved in recruiting the viral envelope glycoproteins onto virions [8-10]. In FIV, HIV or SIV, the N-terminal domain of Gag undergoes a co-translational covalent modification of the MA N-terminus with a myristoyl group [11-15]. tert-Butyl (7-bromoheptyl)carbamate This myristoylation, together with a highly basic patch of amino acid residues located at the N-terminus of the MA, directs the Gag polyprotein to the plasma membrane (PM), mediating the association between Gag and the inner leaflet of the PM lipid bilayer, 4-Dichloro-5-methylpyridine Benzaldehyde where Gag forms a hexagonal network [16]. The N-terminal end of Gag for some retroviruses, including EIAV, is not myristoylated, and some N-terminal ends bear a different chemical modification [17,18]. Interestingly, FIV appears to be an exception among nonprimate lentiviruses because of its capacity to be myristoylated [19]. After the budding of virus particles from host cells, the Gag polyprotein is cleaved by the viral protease into its different subunits during maturation [20]. In the mature particle, the capsid and the nucleocapsid subunits of the Gag polyprotein make a compact RNA-containing conically shaped capsid inside the virion, in contrast to the MA protein, which remains at the inner surface of the virus membrane. In the HIV model, the N-terminal myristoyl group of MA can adopt sequestered and exposed conformations [21] consistent with a myristoyl switch mechanism for regulating membrane binding [22-25]. The formation of MA trimers in HIV can trigger.