Electronogramma, showing mature vaccinia virus particles (shown with dark arrows) in the cytoplasm of human carcinoma cell. Vaccinia virus replication in tumor cells leads to their unavoidable death. Light arrow shows the mitochondria.
Electronogramma, showing mature vaccinia virus particles (shown with dark arrows) in the cytoplasm of human carcinoma cell. Vaccinia virus replication in tumor cells leads to their unavoidable death. Light arrow shows the mitochondria.
Dinocampus coccinellae paralysis virus (DcPV) is an RNA virus found in insects, specifically belonging to the picorna-like virus family Iflaviridae. Discovered in 2015, this virus infects the parasitic braconid wasp Dinocampus coccinellae without causing any noticeable symptoms. It has been suggested that DcPV is linked to the paralysis induced by the wasp in its host, the spotted lady beetle Coleomegilla maculata, which becomes a "zombie bodyguard" for the wasp's pupa.
Dinocampus coccinellae paralysis virus (DcPV) is an RNA virus found in insects, specifically belonging to the picorna-like virus family Iflaviridae. Discovered in 2015, this virus infects the parasitic braconid wasp Dinocampus coccinellae without causing any noticeable symptoms. It has been suggested that DcPV is linked to the paralysis induced by the wasp in its host, the spotted lady beetle Coleomegilla maculata, which becomes a "zombie bodyguard" for the wasp's pupa.
Wikimedia Commons, Chelsea Bonnain, Mya Breitbart and Kristen N. Buck.
08 Apr 2024
Structure of a typical bacteriophage belonging to the Myoviridae family. The expanded inset shows a model of the gp37 tail fiber protein of phage T4 (PDB ID code 2XGF), visualized in Chimera (Pettersen et al., 2004), and VMD (Humphrey et al., 1996). Seven iron ions (red spheres) are coordinated octahedrally by histidine residues, forming a trimer as shown in the top image, while the bottom image shows a gp37 monomer.
Structure of a typical bacteriophage belonging to the Myoviridae family. The expanded inset shows a model of the gp37 tail fiber protein of phage T4 (PDB ID code 2XGF), visualized in Chimera (Pettersen et al., 2004), and VMD (Humphrey et al., 1996). Seven iron ions (red spheres) are coordinated octahedrally by histidine residues, forming a trimer as shown in the top image, while the bottom image shows a gp37 monomer.
Wikimedia Commons, Chelsea Bonnain, Mya Breitbart and Kristen N. Buck.
Metal-polymer nanocomposites can be easily prepared by thermolysis of noble metal thiolates (i.e., organosulfur compounds with the following chemical formula: Me(RS)x, where Me is the noble metal and x its oxidation number, RS- is the thiolate ligand) dissolved in a molten polymer matrix (e.g., amorphous polystyrene, PS). In this in situ synthesis process, the metal nanoparticles are generated in form of cluster compounds, that is, nano-sized core/shell structures, where the core is a metallic single-crystal and the shell is a thiolate monolayer (e.g., Aun(SR)m, where n is the metal cluster nuclearity and m the number of thiolate molecules in the shell). After this precipitation step, the particles with the same size spontaneously tend to form small aggregates in the fluid polymeric medium. The aggregation process takes place by interdigitation of the normal alkane thiolate chains contained in the cluster shell. Generally, the obtained aggregates have a small size, are planar and made of close packed nanoparticles (2D-superlattices). This special types of aggregates with a regular topology are quite commonly observed in the microscopical analysis made by electron microscopy (TEM) of a metal-polymer nanocomposite produced by thermolysis of a metal thiolate precursor. When the nanoparticles have a surface plasmon resonance (SPR) (e.g., silver and gold cluster compounds), the presence of these small regular aggregates in the material determines a number of technologically useful functional properties like, for example, the plasmonic thermochromism [1].
Metal-polymer nanocomposites can be easily prepared by thermolysis of noble metal thiolates (i.e., organosulfur compounds with the following chemical formula: Me(RS)x, where Me is the noble metal and x its oxidation number, RS- is the thiolate ligand) dissolved in a molten polymer matrix (e.g., amorphous polystyrene, PS). In this in situ synthesis process, the metal nanoparticles are generated in form of cluster compounds, that is, nano-sized core/shell structures, where the core is a metallic single-crystal and the shell is a thiolate monolayer (e.g., Aun(SR)m, where n is the metal cluster nuclearity and m the number of thiolate molecules in the shell). After this precipitation step, the particles with the same size spontaneously tend to form small aggregates in the fluid polymeric medium. The aggregation process takes place by interdigitation of the normal alkane thiolate chains contained in the cluster shell. Generally, the obtained aggregates have a small size, are planar and made of close packed nanoparticles (2D-superlattices). This special types of aggregates with a regular topology are quite commonly observed in the microscopical analysis made by electron microscopy (TEM) of a metal-polymer nanocomposite produced by thermolysis of a metal thiolate precursor. When the nanoparticles have a surface plasmon resonance (SPR) (e.g., silver and gold cluster compounds), the presence of these small regular aggregates in the material determines a number of technologically useful functional properties like, for example, the plasmonic thermochromism [1].
Envelopped extracellular baculovirus virions can be found in two forms: OV (occluded virus) and BV (budded virus). The nucleocapsid is about 21 nm x 260 nm.
Envelopped extracellular baculovirus virions can be found in two forms: OV (occluded virus) and BV (budded virus). The nucleocapsid is about 21 nm x 260 nm.
Nanoparticles of ductile metals can be easily cold-sintered by pressing to lead nano-crystalline metals. Nano-crystalline materials have a number of anomalous physical and mechanical properties (e.g., high electrical resistivity, low thermal conductivity, high thermal expansion coefficient) [1]. For example, monodispersed spherical bismuth nanoparticles, produced by thermal decomposition of pure bismuth thiolate (i.e., Bi(SC12H25)3), have been cold-sintered by hydraulic press to produce a nanostructured material with unique thermoelectric properties [2].
Nanoparticles of ductile metals can be easily cold-sintered by pressing to lead nano-crystalline metals. Nano-crystalline materials have a number of anomalous physical and mechanical properties (e.g., high electrical resistivity, low thermal conductivity, high thermal expansion coefficient) [1]. For example, monodispersed spherical bismuth nanoparticles, produced by thermal decomposition of pure bismuth thiolate (i.e., Bi(SC12H25)3), have been cold-sintered by hydraulic press to produce a nanostructured material with unique thermoelectric properties [2].
Rose rosette disease (RRD) was initially detected during the 1940s within the Rocky Mountains. Among the hosts known for this disease, only Rosa species and hybrids have been identified. The common wild host for RRD is the Multiflora rose (Rosa multiflora), and the disease has since proliferated across extensive regions of the United States, affecting Multiflora and other wild rose varieties.
Rose rosette disease (RRD) was initially detected during the 1940s within the Rocky Mountains. Among the hosts known for this disease, only Rosa species and hybrids have been identified. The common wild host for RRD is the Multiflora rose (Rosa multiflora), and the disease has since proliferated across extensive regions of the United States, affecting Multiflora and other wild rose varieties.
This negatively-stained transmission electron micrograph (TEM) revealed the presence of numerous herpes simplex virions, located both inside the nucleus, and extracellularly in this tissue sample. As members of the Herpesviridae virus family, there are two strains of the herpes simplex virus, HSV-1, which is responsible for cold sores, and HSV-2, which is responsible for genital herpes. At the core of its icosahedral proteinaceous capsid, the HSV contains a double-stranded DNA linear genome.
This negatively-stained transmission electron micrograph (TEM) revealed the presence of numerous herpes simplex virions, located both inside the nucleus, and extracellularly in this tissue sample. As members of the Herpesviridae virus family, there are two strains of the herpes simplex virus, HSV-1, which is responsible for cold sores, and HSV-2, which is responsible for genital herpes. At the core of its icosahedral proteinaceous capsid, the HSV contains a double-stranded DNA linear genome.
This negatively-stained transmission electron micrograph (TEM) revealed the presence of numerous herpes simplex virions, members of the Herpesviridae virus family. There are two strains of the herpes simplex virus, HSV-1, which is responsible for cold sores, and HSV-2, which is responsible for genital herpes. At the core of its icosahedral proteinaceous capsid, the HSV contains a double-stranded DNA linear genome.
This negatively-stained transmission electron micrograph (TEM) revealed the presence of numerous herpes simplex virions, members of the Herpesviridae virus family. There are two strains of the herpes simplex virus, HSV-1, which is responsible for cold sores, and HSV-2, which is responsible for genital herpes. At the core of its icosahedral proteinaceous capsid, the HSV contains a double-stranded DNA linear genome.
Wikimedia Commons, Jacqueline Z.-M. Chan, Andrew D. Millard, Nicholas H. Mann, Hendrik Schäfer
10 Apr 2024
Transmission electron microscope (TEM) micrograph of phage RPP1 (Schitoviridae, formerly in Podoviridae) negatively stained with uranylacetate. Based on its morphology this phage was classified as kind of podoviruses.
Transmission electron microscope (TEM) micrograph of phage RPP1 (Schitoviridae, formerly in Podoviridae) negatively stained with uranylacetate. Based on its morphology this phage was classified as kind of podoviruses.
Wikimedia Commons, Jacqueline Z.-M. Chan, Andrew D. Millard, Nicholas H. Mann, Hendrik Schäfer
Venn diagram indicating the global proximity in gene content of CeV, its two closest relatives, PgV and AaV, and one member of each genus of the family Mimiviridae (Cafeteriavirus genus, CroV; Mimivirus genus, Mimi). The numbers in parentheses correspond to the raw number of encoded proteins without a homolog in the four other viruses. The numbers without parentheses indicate how many distinct clusters they constitute. The analysis was driven using OrthoMCL software, with a 10−5 E-value threshold and 1.5-mcl inflation parameter. [1]
Venn diagram indicating the global proximity in gene content of CeV, its two closest relatives, PgV and AaV, and one member of each genus of the family Mimiviridae (Cafeteriavirus genus, CroV; Mimivirus genus, Mimi). The numbers in parentheses correspond to the raw number of encoded proteins without a homolog in the four other viruses. The numbers without parentheses indicate how many distinct clusters they constitute. The analysis was driven using OrthoMCL software, with a 10−5 E-value threshold and 1.5-mcl inflation parameter. [1]
Wikimedia Commons, Jancovich J.K., Qin Q., Zhang QY., Chinchar V.G; Gray M., Chinchar V.
14 Mar 2024
Schematic diagram of Ranavirus replication. Virions enter cells by one of two possible routes and initial events in virus replication (early viral transcription and the synthesis of unit length genomes) take place within the nucleus. Viral genomes are subsequently transported into the cytoplasm where they are methylated and serve as templates for concatemer formation. Viral assembly sites contain viral DNA and a number of virus-encoded proteins and serve as the loci of virion formation. Newly synthesized virions are found free within the cytoplasm or within paracrystalline arrays, and, a minority, at least in vitro, bud from the plasma membrane and in the process acquire an envelope.[1]
Schematic diagram of Ranavirus replication. Virions enter cells by one of two possible routes and initial events in virus replication (early viral transcription and the synthesis of unit length genomes) take place within the nucleus. Viral genomes are subsequently transported into the cytoplasm where they are methylated and serve as templates for concatemer formation. Viral assembly sites contain viral DNA and a number of virus-encoded proteins and serve as the loci of virion formation. Newly synthesized virions are found free within the cytoplasm or within paracrystalline arrays, and, a minority, at least in vitro, bud from the plasma membrane and in the process acquire an envelope.[1]
Wikimedia Commons, Jancovich J.K., Qin Q., Zhang QY., Chinchar V.G; Gray M., Chinchar V.