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10 p, 2.5 MB Gag-protease coevolution analyses define novel structural surfaces in the HIV-1 matrix and capsid involved in resistance to Protease Inhibitors / Codoñer, Francisco M. (Universidad Católica de Valencia) ; Peña, Ruth (Institut Germans Trias i Pujol. Institut de Recerca de la Sida IrsiCaixa) ; Blanch-Lombarte, Oscar (Institut Germans Trias i Pujol. Institut de Recerca de la Sida IrsiCaixa) ; Jiménez-Moyano, Esther (Institut Germans Trias i Pujol. Institut de Recerca de la Sida IrsiCaixa) ; Pino, Maria (Institut Germans Trias i Pujol. Institut de Recerca de la Sida IrsiCaixa) ; Vollbrecht, Thomas (University of California San Diego) ; Clotet Sala, Bonaventura (Institut Germans Trias i Pujol. Institut de Recerca de la Sida IrsiCaixa) ; Martinez-Picado, Javier (Institut Germans Trias i Pujol. Institut de Recerca de la Sida IrsiCaixa) ; Draenert, Rika (Ludwig-Maximilians-Universität München) ; Prado, Julia G (Institut Germans Trias i Pujol. Institut de Recerca de la Sida IrsiCaixa) ; Universitat Autònoma de Barcelona. Departament de Medicina
Despite the major role of Gag in establishing resistance of HIV-1 to protease inhibitors (PIs), very limited data are available on the total contribution of Gag residues to resistance to PIs. To identify in detail Gag residues and structural interfaces associated with the development of HIV-1 resistance to PIs, we traced viral evolution under the pressure of PIs using Gag-protease single genome sequencing and coevolution analysis of protein sequences in 4 patients treated with PIs over a 9-year period. [...]
2017 - 10.1038/s41598-017-03260-4
Scientific reports, Vol. 7 (june 2017)  

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