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Gene Review:

gag - gag protein

Friend murine leukemia virus

Barklis, E. et al., Abe, A. et al., McDermott, J. et al., Parent, L.J. et al., Mayo, K. et al., et al.

Johnson, Spidel, Ako-Adjei, Wills, Vogt,

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Disease relevance of gag

In the absence of envelope gene expression, retrovirus packaging cell lines expressing Moloney murine leukemia virus (MLV) gag and pol genes produce large amounts of noninfectious virus-like particles that contain reverse transcriptase, processed Gag protein, and viral RNA (gag-pol RNA particles) [1].
In human cells infected by HIV type 1 (HIV-1), the viral Gag protein directs the assembly of nascent viral particles at the plasma membrane [2].
These defective mutant viruses showed no apparent alteration to Gag protein processing or reduction in the yield of virions after transient transfection, but the mutants failed to form circular viral DNAs in acutely infected cells [3].
Central to both Gag protein arrangements is the capsid (CA) protein, a domain of PrGag, which is cleaved from the precursor to yield a mature Gag protein composed of an N-terminal domain (NTD), a flexible linker region, and a C-terminal domain (CTD) [4].
Here, we report that the matrix (MA) protein contains regions that in conjunction with myristylation are important for Gag protein stability and the assembly of murine leukemia viruses [5].

High impact information on gag

Using PC + DHGN monolayers, we examined membrane-bound arrays of an N-terminal His-tagged Moloney murine leukemia virus (M-MuLV) capsid (CA) protein, His-MoCA, and in vivo studies suggest that in vitro-derived His-MoCA arrays reflect some of the Gag protein interactions which occur in assembling virus particles [6].
Retroviral late domains (L domains) are short amino acid sequences in the Gag protein that facilitate the process of budding [7].
The presence of myristic acid at the N terminus of the Myr1E Gag protein does not explain its replication defect, because other myristylated derivatives of RSV Gag are fully infectious (e.g., Myr2 [C. R. Erdie and J. W. Wills, J. Virol. 64:5204-5208, 1990]) [8].
To analyze contacts made by Moloney murine leukemia virus (M-MuLV) capsid (CA) proteins in immature and mature virus particles, we have employed a cysteine-specific crosslinking approach that permits the identification of retroviral Gag protein interactions at particular residues [9].

References

In vitro cell-free conversion of noninfectious Moloney retrovirus particles to an infectious form by the addition of the vesicular stomatitis virus surrogate envelope G protein. Abe, A., Chen, S.T., Miyanohara, A., Friedmann, T. J. Virol. (1998) [Pubmed]
Efficient assembly of an HIV-1/MLV Gag-chimeric virus in murine cells. Chen, B.K., Rousso, I., Shim, S., Kim, P.S. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
Phosphorylated serine residues and an arginine-rich domain of the moloney murine leukemia virus p12 protein are required for early events of viral infection. Yueh, A., Goff, S.P. J. Virol. (2003) [Pubmed]
Retrovirus capsid protein assembly arrangements. Mayo, K., Huseby, D., McDermott, J., Arvidson, B., Finlay, L., Barklis, E. J. Mol. Biol. (2003) [Pubmed]
Matrix protein of Akv murine leukemia virus: genetic mapping of regions essential for particle formation. Jørgensen, E.C., Pedersen, F.S., Jørgensen, P. J. Virol. (1992) [Pubmed]
Structural analysis of membrane-bound retrovirus capsid proteins. Barklis, E., McDermott, J., Wilkens, S., Schabtach, E., Schmid, M.F., Fuller, S., Karanjia, S., Love, Z., Jones, R., Rui, Y., Zhao, X., Thompson, D. EMBO J. (1997) [Pubmed]
The C-terminal half of TSG101 blocks Rous sarcoma virus budding and sequesters Gag into unique nonendosomal structures. Johnson, M.C., Spidel, J.L., Ako-Adjei, D., Wills, J.W., Vogt, V.M. J. Virol. (2005) [Pubmed]
RNA dimerization defect in a Rous sarcoma virus matrix mutant. Parent, L.J., Cairns, T.M., Albert, J.A., Wilson, C.B., Wills, J.W., Craven, R.C. J. Virol. (2000) [Pubmed]
Crosslink analysis of N-terminal, C-terminal, and N/B determining regions of the Moloney murine leukemia virus capsid protein. McDermott, J., Karanjia, S., Love, Z., Barklis, E. Virology (2000) [Pubmed]

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