The transfer of genetic information between unrelated species is referred to as horizontal gene transfer. Previous studies have demonstrated that both retroviral and non-retroviral sequences have been integrated into eukaryotic genomes. Recently, we identified many non-retroviral sequences in plant genomes. In this study, we investigated the evolutionary origin and gene transfer of domains present in endornaviruses which are double-stranded RNA viruses. Using the available sequences for endornaviruses, we found that Bell pepper endornavirus-like sequences homologous to the glycosyltransferase 28 domain are present in plants, fungi, and bacteria. The phylogenetic analysis revealed the glycosyltransferase 28 domain of Bell pepper endornavirus may have originated from bacteria. In addition, two domains of Oryza sativa endornavirus, a glycosyltransferase sugar-binding domain and a capsular polysaccharide synthesis protein, also exhibited high similarity to those of bacteria. We found evidence that at least four independent horizontal gene transfer events for the glycosyltransferase 28 domain have occurred among plants, fungi, and bacteria. The glycosyltransferase sugar-binding domains of two proteobacteria may have been horizontally transferred to the genome of Thalassiosira pseudonana. Our study is the first to show that three glycome-related viral genes in the genus Endornavirus have been acquired from marine bacteria by horizontal gene transfer.
A keratinolytic proteinase (KPase) which is regarded as an important factor in the pathogenesis of dermatophytosis was isolated and purified from Microsporum (M.) canis culture filtrates. Enzyme-linked immunosorbent assay (ELISA) was used to determine the occurrence of circulating antibodies to this enzyme in sera samples from guinea pigs with superficial fungal infections caused by M. canis. Of sera samples from guinea pigs infected with M. canis, 75% were reactive within 10 weeks, however, those ELISA values were relatively low compared with those from guinea pigs immunized with KPase. The presence of circulating antibodies was first detected 2 weeks post inoculation with M. canis, corresponding to the period when the lesions were most severe. The titers of the ELISA antibodies reached a peak at 4 weeks; at that time the lesions had disappeared completely.
The infectious full-length cDNA clones of Cucumber green mottle mosaic virus (CGMMV) isolates KW and KOM, which were isolated from watermelon and oriental melon, respectively, were constructed under the control of the cauliflower mosaic virus 35S promoter. We successfully inoculated Nicotiana benthamiana with the cloned CGMMV isolates KW and KOM by Agrobacterium-mediated infiltration. Virulence and symptomatic characteristics of the cloned CGMMV isolates KW and KOM were tested on several indicator plants. No obvious differences between two cloned isolates in disease development were observed on the tested indicator plants. We also determined full genome sequences of the cloned CGMMV isolates KW and KOM. Sequence comparison revealed that only four amino acids (at positions 228, 699, 1212, and 1238 of the replicase protein region) differ between the cloned isolates KW and KOM. A previous study reported that the isolate KOM could not infect Chenopodium amaranticolor, but the cloned KOM induced chlorotic spots on the inoculated leaves. When compared with the previously reported sequence of the original KOM isolate, the cloned KOM contained one amino acid mutation (Ala to Thr) at position 228 of the replicase protein, suggesting that this mutation might be responsible for induction of chlorotic spots on the inoculated leaves of C. amaranticolor.
Introduction: N-hydroxy-7-(2-naphthylthio) heptanomide (HNHA) is a novel HDAC inhibitor that shows better pharmacological properties than known HDAC inhibitors. We investigated a therapeutic role and its mechanisms of HNHA in renal cell carcinoma. Methods: Renal cell carcinoma cell lines, Caki-1, A-498, 786-O and UMRC-3 cells were used for in vitro study. Crystal violet assay was used to assess cell growth. Apoptosis was evaluated by TUNEL assay and confirmed by expression of cleaved caspase-3 and caspase-7. Cytochrome c release was evaluated by mitochondria staining. For in vivo study, Caki-1 and A-498 cells were injected (1.0 x 107/mouse) into the dorsal sub-membrane of 6-week-old BALB/C nude mice. Two different drugs were injected at Lethal Dose 50: HNHA, 206 µg/mL and SAHA, 138 µg/mL. Result: HNHA suppressed tumor proliferation in all panels of renal cell carcinoma cells. TUNEL assay and Western blots showed that remarkable apoptosis was induced by HNHA in Caki-1 and A-498 cells. HNHA induced apoptotic cell death by caspase activation and Bcl 2 suppression in renal cell carcinoma in vitro and in vivo. HNHA also caused cytochrome c release from mitochondria through Bax and Bak expression. A primary caspase activation was initiated by cytochrome c release from mitochondria, which is able to induce biochemical reactions, caspase activation and subsequent cell death. Conclusion: HNHA induces more potent apoptotic cell death in renal cell carcinoma in vitro and in vivo than the previous HDAC inhibitors. HNHA-induced apoptosis is mediated by cytochrome c release from mitochondria through induction of Bax and Bak expression in renal cell carcinoma. Citation Format: Kyung Seok Han, Ki Cheong Park, Jeong Yong Jeon, Sang Yong Kim, Dami Song, Woong Kyu Han, Sung Joon Hong. A novel HDAC inhibitor, N-hydroxy-7-(2-naphthylthio) heptanomide (HNHA), induces apoptotic cell death through mitochondrial cytochrome c release in renal cell carcinoma. [abstract]. In: Proceedings of the 105th Annual Meeting of the American Association for Cancer Research; 2014 Apr 5-9; San Diego, CA. Philadelphia (PA): AACR; Cancer Res 2014;74(19 Suppl):Abstract nr 5520. doi:10.1158/1538-7445.AM2014-5520
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.
customersupport@researchsolutions.com
10624 S. Eastern Ave., Ste. A-614
Henderson, NV 89052, USA
This site is protected by reCAPTCHA and the Google Privacy Policy and Terms of Service apply.
Copyright © 2025 scite LLC. All rights reserved.
Made with 💙 for researchers
Part of the Research Solutions Family.