The nuclear lamina is a proteinaceous structure located underneath the inner nuclear membrane (INM), where it associates with the peripheral chromatin. It contains lamins and lamin-associated proteins, including many integral proteins of the INM, chromatin modifying proteins, transcriptional repressors and structural proteins. A fraction of lamins is also present in the nucleoplasm, where it forms stable complexes and is associated with specific nucleoplasmic proteins. The lamins and their associated proteins are required for most nuclear activities, mitosis and for linking the nucleoplasm to all major cytoskeletal networks in the cytoplasm. Mutations in nuclear lamins and their associated proteins cause about 20 different diseases that are collectively called laminopathies’. This review concentrates mainly on lamins, their structure and their roles in DNA replication, chromatin organization, adult stem cell differentiation, aging, tumorogenesis and the lamin mutations leading to laminopathic diseases.

Carp interstitial nephritis and gill necrosis virus (CNGV) is an unclassified large DNA virus that morphologically resembles members of the Herpesviridae but contains a large (ca. ϳ280-kbp) linear double-stranded DNA. This virus has also been named koi herpesvirus, koi herpes-like virus, and cyprinid herpesvirus 3. CNGV is the cause of a lethal disease that afflicts common carp and koi. By using immunohistochemistry, molecular analysis, and electron microscopy we previously demonstrated that this virus is present mainly in the intestine and kidney of infected fish. Based on these observations, we postulated that viruses and/or viral components may appear in droppings of infected carp. Here we report that (i) by using PCR we demonstrated that fish droppings contain viral DNA, (ii) fish droppings contain viral antigens which are useful for CNGV diagnosis, and (iii) fish droppings contain active virus which can infect cultured common carp brain cells and induce the disease in naïve fish following inoculation. Thus, our findings show that CNGV can be identified by using droppings without taking biopsies or killing fish and that infectious CNGV is present in the stools of sick fish. The possibility that fish droppings preserve viable CNGV during the nonpermissive seasons is discussed.

The nuclear lamina is a proteinaceous structure located underneath the inner nuclear membrane (INM) J. Cell. Mol. Med. Vol 13, No 6, 2009 pp. 1059-1085 © Jerusalem, Jerusalem 91904, Israel. Tel.: 972-2-6585995 Fax: 972-2-5637848 E-mail: gru@vms.huji.ac.il The lamin molecule (Fig. 1A)

Cyprinid herpesvirus 3 (CyHV-3), previously designated carp interstitial nephritis and gill necrosis virus or koi herpesvirus, is the cause of a worldwide mortal disease of koi and carp. Morphologically, the virus resembles herpesviruses, yet it bears a genome of 277 to 295 kbp, which is divergent from most of the genomic sequences available in GenBank. The disease afflicts fish in the transient seasons, when the water temperature is 18 to 28°C, conditions which permit virus propagation in cultured cells. Here we report that infectious virus is preserved in cultured cells maintained for 30 days at 30°C. CyHV-3-infected vacuolated cells with deformed morphology converted to normal, and plaques disappeared following shifting up of the temperature and reappeared after transfer to the permissive temperature. Viral propagation and viral gene transcription were turned off by shifting cells to the nonpermissive temperature. Upon return of the cells to the permissive temperature, transcription of viral genes was reactivated in a sequence distinguished from that occurring in naïve cells following infection. Our results show that CyHV-3 persists in cultured cells maintained at the nonpermissive temperature and suggest that viruses could persist for long periods in the fish body, enabling a new burst of infection upon a shift to a permissive temperature.Cyprinus carpio is a widely cultivated eurythermal fish which accounts for much of the world's aquaculture production. In recent years, this fish has been afflicted by a disease causing mass mortalities in fisheries worldwide (6,12,23). The sickness is seasonal, afflicting fish when the water temperature is 18 to 28°C. The agent causing the disease is a large double-stranded DNA virus designated carp interstitial nephritis and gill necrosis virus, koi herpesvirus, or cyprinid herpesvirus 3 (CyHV-3) (9, 25, 31). Morphologically, CyHV-3 resembles herpesviruses (9, 10) and shows sequence homology to two other aquatic herpesvirus-like viruses, CyHV-1 and CyHV-2, afflicting Cyprinus carpio and Carassius auratus, respectively (31). On the other hand, CyHV-3 expresses proteins resembling those of Poxviridae members and other large DNA viruses (10, 11). It is not yet known whether CyHV-3 undergoes latent infection. This question is not only important for the characterization of this unique virus but also has economic implications, since it is unclear how and where the virus is preserved between the seasons and by what means the transfer of the virus from virus-free to contaminated regions can be avoided.CyHV-3 DNA was identified in infected fish maintained for 64 days postinfection (dpi) at the nonpermissive temperature range, but infectious virus was not found in these fish (4, 5). Recently, it was reported that infected fish maintained for ϳ200 days at 12°C released infectious virus upon shift of the water temperature to a permissive temperature, i.e., 22°C (28). These reports strongly suggest that CyHV-3 persists in fish maintained at low temperatures for an extended period. In ...

Adhesive materials extracted from the brown alga Fucus serratus are composed of phenolic polymer, alginate, and CaCl2. The phenolic polymer undergoes an oxidation reaction in the presence of bromoperoxidase, KI, and H2O2. The nanostructure of the adhesive was investigated using small angle X-ray scattering, light scattering, and cryo- transmission electron microscopy experiments. These have shown that the phenolic polymer undergoes self-assembly and forms flexible chain-like objects. Oxidation or adding alginate does not alter this structure. However, once calcium ions are added, a rigid network is formed. Presumably, this network is responsible for the cohesive strength of the glue.