No abstract

During 2009–2010, a survey was conducted in gardens and commercial fig orchards throughout Iran to determine the prevalence of Fig leaf mottle‐associated virus 1 (FLMaV‐1), Fig leaf mottle‐associated virus 2 (FLMaV‐2), Fig mild mottle‐associated virus (FMMaV), Fig latent virus 1 (FLV‐1) and Fig mosaic virus (FMV). Reverse transcription‐polymerase chain reaction and dot immunobinding assay (DIBA) were conducted on 104 fig samples collected from seven provinces. FLV‐1, FLMaV‐1 and FMV were found in 14.5, 11.5 and 8.6% of the samples, respectively, but FLMaV‐2 and FMMaV were absent. The overall average of infection reached 18.3%, with a peak of 42.9% in Semnan Province, followed by Golestan (40%), Tehran (32.3%), Lorestan (28.6%) and Mazandaran (25%) provinces. No infection was found in Fars and Gilan provinces. Fig samples from Varamin and Khorramabad districts showed high levels of mixed infections, 35.7 and 28.6%, respectively. The presence of FMV and FLV‐1 in the sap of symptomatic fig leaves was also ascertained by DIBA. Sequence analysis of amplified DNA from the partial RNA‐dependent RNA polymerase gene of two FMV isolates from Iran showed a low level of nucleotide variability (5%). The Iranian isolates shared a common phylogeny with other Mediterranean FMV isolates and in particular with those originating from Turkey already reported in GenBank. This is the first report on the presence of FLMaV‐1 and FLV‐1 in Iran and offers a preliminary insight into the unsatisfactory health status of fig in this country.

No abstract

Since the current treatments have not resulted in the desired outcomes for melanoma patients, there is a need to identify more effective medications. Together with other snake venom proteins, cytotoxin-II has shown promising results in tumoral cells. In this study, recombinant cytotoxin-II (rCTII) was expressed in SHuffle® T7 Express cells, while the epitope mapping of rCTII was performed to reveal the antibody-binding regions of rCTII. The MTT (3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide) assay was used to assess the viability of SK-MEL-3 and HFF-2 cells after treating these cells with rCTII. The qRT-PCR was performed to evaluate the expression levels of matrix metallopeptidase 3 (MMP-3), SMAD2, SMAD3, caspase-8, caspase-9, and miR-214 in order to reveal the rCTII-induced signaling pathways in melanoma. Our results have shown that two regions of amino acids, 6–16 and 19–44, as predicted epitopes of this toxin, are essential for understanding the toxicity of rCTII. Treating the melanoma cells with rCTII substantially inhibited the transforming growth factor-beta (TGF-β)–SMAD signaling pathway and down-regulated the expression of MMP-3 and miR-214 as well. This cytotoxin also restored apoptosis mainly via the intrinsic pathway. The down-regulation of MMP-3 and miR-214 might be associated with the anti-metastatic property of rCTII in melanoma. The inhibitory effect of rCTII on the TGF-β signaling pathway might be associated with increased apoptosis and decreased cancer cell proliferation. It is interesting to see that the IC50 value of rCTII has been lower in the melanoma cells than non-tumoral cells, which may indicate its potential effects as a drug. In conclusion, rCTII, as a novel medication, might serve as a potent and efficient anticancer drug in melanoma.

No abstract

The ability of mass spectrometry for discrimination between protein and peptide masses which are unique to specific pathogens provides an accurate and fast method for the detection of different types of pathogens, especially viruses. Capsid proteins are specific to each virus and can be used as a biomarker for detection of this pathogen. On the other hand, single-chain variable fragment (scFv) antibodies have been recently used to enhance the accuracy of immunoassay techniques. So conjugation of mass spectrometry and scFv antibody provides a very accurate and fast method for the detection of viruses. In this report, for the first time, we have immobilized scFv antibody of fig mosaic virus (FMV) on the magnetic nanoparticles (MNPs) to extract the virus capsid protein from complex biological media and subsequently identified this protein through both its intact molecular mass and peptide mass fingerprint (PMF) by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS).