ABSTRACT. We investigated the association between the polymorphisms GSTP1 rs1695 and XRCC1 rs1799782 and rs25487 and the clinical outcome of patients with non-small cell lung cancer (NSCLC) receiving cisplatin-based chemotherapy. Genotyping of GSTP1 rs1695 and XRCC1 rs1799782, and rs25487 was conducted by polymerase chain reaction-restriction fragment length polymorphism analysis. By conditional logistic regression analysis, patients carrying the GG genotype of GSTP1 rs1695 and the AA genotype of XRCC1 rs25487 were found to be more highly associated with response to chemotherapy than were those carrying the AA genotype; the ORs (95%CIs) were 0.13 (0.04-0.37) and 3.37 (1.44-8.53), respectively. Presence of the GG genotype of GSTP1 rs1695 and the GA and AA genotypes of XRCC1 rs25487 was associated with overall survival of (2015) NSCLC, and the hazards ratios (95%CI) were 4. 35 (1.40-17.92), 0.53 (0.31-0.91), and 0.39 (0.18-0.83), respectively. The results of our study suggest that the GSTP1 rs1695 and XRCC1 rs25487 polymorphisms might affect the clinical outcome of patients with advanced NSCLC receiving cisplatin-based chemotherapy.
Summary. -Th e successful foamy viruses (FVs) infection includes at least two essential events, attachment to the cell surface and fusion of the viral envelope with the cell membrane. For the FVs, membrane fusion between virus and cell is mediated by envelope glycoprotein (Env) transmembrane (TM) subunit gp47. Compared with other retroviruses, FV TM subunit shares a similar but not identical structural characteristic. Th is paper focuses on in sillico analyses of all 15 available FV TM subunits gp47 based on their amino acid sequences. Th e hydrophobicity analysis revealed that the 15 FVs gp47 had two prominent hydrophobic regions, the N-terminal fusion peptide (FP) and the C-terminal region, which included a membrane-spanning domain (MSD) and a membrane proximal ectodomain region (MPER). In most FVs gp47, two heptad repeats, the coiled coils characterized by repetition of 7-amino acid-motif, were found to be correspondently located downstream of FP (named "N-HR") and the upstream of MPER (named "C-HR"). Furthermore, the solvent accessibility and secondary structure were predicted for all FVs gp47. Th ese observations suggested that FVs gp47 possessed several fusion domains, which were necessary in the process of lipid membrane fusion between FVs and the target cells.Keywords: foamy virus; envelope glycoprotein; transmembrane subunit gp47; hydrophobicity analysis; fusion domain * Corresponding authors. E-mail: lizhi@snnu.edu.cn; phone: +86-29-85310581. Abbreviations: BFV = bovine foamy virus; BSV = bovine syncytial virus; C-HR = C-terminal heptad repeat; EFV = equine foamy virus; Env = envelope glycoprotein; ERRS = endoplasmic reticulum retrieval signal; FFV = feline foamy virus; FP = fusion peptide; FSV = feline syncytial virus; FV(s) = foamy virus(es); HBV = hepatitis B virus; HIV = human immunodefi ciency virus; HR = heptad repeat; MMTV = mouse mammary tumor virus; MPER = Membrane proximal ectodomain region; MSD = membrane-spanning domain; N-HR = N-terminal heptad repeat; PFV = prototype foamy virus; SFV agm = african green monkey simian foamy virus; SFV cpz = chimpanzee foamy virus; SFV gor = gorilla foamy virus; SFV mac = macaque foamy virus; SFV mar = marmoset foamy virus; SFV spm = spider monkey foamy virus; SFV sqm = squirrel monkey foamy virus; SIV = simian immunodefi ciency virus; SloEFV = sloth endogenous foamy virus; SU = central surface domain; TM = transmembrane domain the subfamily Spumaretrovirinae of the family Retroviridae (Dirk and Axel, 2011). Till now, 15 FVs have been reported, which were derived from 6 non-primate and 9 primate hosts, including cat, horse, cattle, non-human primates and human. As indicated by their names, FVs possess highly fusogenic activity, which induces infected cells in vitro to form foamlike multinucleated cells. FVs can establish lifelong persistent infections in their hosts in the absence of any pathogenicity (Linial, 2000). As with other retroviruses, the FV envelope protein (Env) harbors essential features that allow viral adsorption, uptake and fusogenic release...
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