HIV-1 and MLV Gag proteins are sufficient to recruit APOBEC3G into virus-like particles

@article{citeulike:2789377, abstract = {The cytidine deaminase hAPOBEC3G is an antiviral human factor that counteracts the replication of HIV-1 in absence of the Vif protein. hAPOBEC3G is packaged into virus particles and lethally hypermutates HIV-1. In this work, we examine the mechanisms governing hAPOBEC3G packaging. By GST pull-down and co-immunoprecipitation assays, we show that hAPOBEC3G binds to HIV-1 Pr55 Gag and its NC domain and to the RT and IN domains contained in Pr160 Gag-Pol. We demonstrate that the expression of HIV-1 Gag is sufficient to induce the packaging of hAPOBEC3G into Gag particles. Gag-Pol polypeptides containing RT and IN domains, as well as HIV-1 genomic RNA, seem not to be necessary for hAPOBEC3G packaging. Lastly, we show that hAPOBEC3G and its murine ortholog are packaged into HIV-1 and MLV Gag particles. We conclude that the Gag polypeptides from distant retroviruses have conserved domains allowing the packaging of the host antiviral factor APOBEC3G.}, author = {Douaisi, Marc and Dussart, Sylvie and Courcoul, Marianne and Bessou, Gilles and Vigne, Robert and Decroly, Etienne }, citeulike-article-id = {2789377}, doi = {10.1016/j.bbrc.2004.07.005}, journal = {Biochemical and Biophysical Research Communications}, keywords = {apobec, assembly}, month = {August}, number = {3}, pages = {566--573}, posted-at = {2008-05-12 13:36:31}, priority = {2}, title = {HIV-1 and MLV Gag proteins are sufficient to recruit APOBEC3G into virus-like particles}, url = {http://dx.doi.org/10.1016/j.bbrc.2004.07.005}, volume = {321}, year = {2004} }

TY - JOUR ID - citeulike:2789377 L3 - citeulike-article-id:2789377 TI - HIV-1 and MLV Gag proteins are sufficient to recruit APOBEC3G into virus-like particles JF - Biochemical and Biophysical Research Communications VL - 321 IS - 3 SP - 566 EP - 573 N2 - The cytidine deaminase hAPOBEC3G is an antiviral human factor that counteracts the replication of HIV-1 in absence of the Vif protein. hAPOBEC3G is packaged into virus particles and lethally hypermutates HIV-1. In this work, we examine the mechanisms governing hAPOBEC3G packaging. By GST pull-down and co-immunoprecipitation assays, we show that hAPOBEC3G binds to HIV-1 Pr55 Gag and its NC domain and to the RT and IN domains contained in Pr160 Gag-Pol. We demonstrate that the expression of HIV-1 Gag is sufficient to induce the packaging of hAPOBEC3G into Gag particles. Gag-Pol polypeptides containing RT and IN domains, as well as HIV-1 genomic RNA, seem not to be necessary for hAPOBEC3G packaging. Lastly, we show that hAPOBEC3G and its murine ortholog are packaged into HIV-1 and MLV Gag particles. We conclude that the Gag polypeptides from distant retroviruses have conserved domains allowing the packaging of the host antiviral factor APOBEC3G. KW - apobec KW - assembly AU - Douaisi, Marc AU - Dussart, Sylvie AU - Courcoul, Marianne AU - Bessou, Gilles AU - Vigne, Robert AU - Decroly, Etienne PY - 2004/08/27/ UR - http://dx.doi.org/10.1016/j.bbrc.2004.07.005 ER -