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This study investigated the optimum temperature and holding solutions for the storage of cut flowers of Arenaria juncea M. Bieb. to facilitate their introduction as a new ornamental plant. We examined the effects of different holding solutions on the water uptake, vase life, and fresh weight of five branches of A. juncea. After harvest, cut branches were stored at 4, 15, 20, and 25°C. To study the effect of the holding solutions, the cut branches were treated with a combination of sucrose (1% and 3%), 8-hydroxyqunoline sulfate (8-HQS: 10, 50, and 100 mg·L-1), and commercial preservative solutions Chrysal and Floralife. At a storage temperature of 4°C, the vase life was 29 days, which was significantly longer compared to room temperature, where the vase life was 7.8 days. Thus, a lower temperature was more effective at extending the vase life. A combination of 1% sucrose and 100 mg·L-1 8-HQS prolonged the vase life by approximately two weeks compared to the control. The effect of both Chrysal and Floralife was similar to the effect of the holding solutions composed of sucrose and 8-HQS. Moreover, rapid reduction of water uptake and fresh weight resulted in a shorter vase life.

Petunia plants are used for urban landscaping in many parts of the world, including South Korea. In this study, we aimed to investigate the occurrence of petunia vein clearing virus (PVCV) infection in petunia plants in Seoul, South Korea. PVCV was detected from 23 of 79 petunia samples collected from Seoul. We obtained the complete genome sequences of the Korean isolates in this study (called PVCV-Kr, Kr2, and Kr3), which were compared with the genome sequence of the USA isolate of the virus (PVCV-USA). The genomic DNA of the three PVCV isolates was found to comprise 7210-7267 nucleotides (nts), which is 4-15 nts longer than the PVCV-USA genome. The genomes of the Kr and Kr2 isolates encode a large polyprotein of 252 kDa (2180 amino acids (aa)). The genome of the Kr3 isolate encodes a large polyprotein of 255 kDa (2203 aa). The polyprotein has six protein domains: a movement protein (MP; 72 aa), a coiled-coil domain (CC; 33 aa), an RNA-binding domain (RB; 18 aa), a protease (PR; 21 aa), a reverse transcriptase (RT; 196 aa), and an RNase H (RH; 121 aa). The large polyprotein and six domains of the three isolates showed 93.9-100.0% sequence homology with those of PVCV-USA. Furthermore, the polymerase polyprotein gene (PR, RT, and RH) of the four PVCV isolates containing the USA isolate grouped with those of Rice tungro bacilliform virus and Soybean chlorotic mottle virus, which belong to the same family (Caulimoviridae). Our findings suggested that the Korean isolates represent a new isolate of PVCV. To our knowledge, this is the first report of PVCV detection in South Korea.