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. 2016 Sep 19;8(9):256. doi: 10.3390/v8090256

Figure 1.

Figure 1

Rous sarcoma virus (RSV) RNA, and RSV and human immunodeficiency virus type 1 (HIV-1) protein constructs used in this work. (A) Predicted secondary structures of RSV MΨ (top) and RSV 167 (bottom) derived from nucleotides (nt) 156–315 and 1249–1409 of the RSV Prague C genome, respectively. Four mutant MΨ constructs are indicated by the boxed nt and arrows: UGCG to GAGA, GG to CC, A197G, and a triple mutation AGC to UCA. Additional nt at the 5′ and 3′ ends of each RNA that are not present in the RSV genome are shown in gray; (B) RSV and HIV-1 Gag constructs used in this work, with full-length wild-type Gag shown at the top of each set for comparison. Matrix (MA), capsid (CA) and nucleocapsid (NC), as well as various spacer peptides (SP, SP1, and SP2), the HIV-1 p6 domain, and the RSV p2, p10, and protease domain (PR) comprise these constructs. In the case of the two chimeric constructs, H132R and R155H, the residues at the junctions are explicitly shown. H132R contains the 132-residue HIV-1 MA in place of RSV MA in the context of RSV Gag, and R155H contains the 155-residue RSV MA in place of HIV-1 MA in the context of HIV-1 Gag.