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01 Mar 2024
Annotated schematic drawing of a Enterobacteria phage T7 virion (cross section and side view).
Annotated schematic drawing of a Enterobacteria phage T7 virion (cross section and side view).
01 Mar 2024
24 Jan 2024
Colorized scanning electron micrograph of Ebola virus particles (green) in extracellular space between infected African green monkey kidney cells. 
Colorized scanning electron micrograph of Ebola virus particles (green) in extracellular space between infected African green monkey kidney cells. 
24 Jan 2024
01 Feb 2024
Segmented linear dsRNA genome. Contains 10 to 12 segments coding for 10 to 14 proteins. Segments size range from 0.2 to 3.0 kb. Genome total size range from 18.2 to 30.5 kb.
Segmented linear dsRNA genome. Contains 10 to 12 segments coding for 10 to 14 proteins. Segments size range from 0.2 to 3.0 kb. Genome total size range from 18.2 to 30.5 kb.
01 Feb 2024
08 Feb 2024
Schematic drawing of immature and mature virion of gammaretrivirus in cross section. Enveloped, spherical to pleomorphic in shape, 80-100 nm in diameter.
Schematic drawing of immature and mature virion of gammaretrivirus in cross section. Enveloped, spherical to pleomorphic in shape, 80-100 nm in diameter.
08 Feb 2024
01 Apr 2024
Schematic diagrams of a vesicular stomatitis virus (VSV) virion. A VSV particle is composed of a cellular lipid bilayer, viral RNA genome, and five viral proteins: nucleo- (N), phospho- (P), matrix (M), glyco- (G), and large (L) proteins. The virus particle contains a ribonucleoprotein (RNP) composed of N–RNA and RNA-dependent RNA polymerase (RdRp) complexes. [1]
Schematic diagrams of a vesicular stomatitis virus (VSV) virion. A VSV particle is composed of a cellular lipid bilayer, viral RNA genome, and five viral proteins: nucleo- (N), phospho- (P), matrix (M), glyco- (G), and large (L) proteins. The virus particle contains a ribonucleoprotein (RNP) composed of N–RNA and RNA-dependent RNA polymerase (RdRp) complexes. [1]
01 Apr 2024
11 Apr 2024
This transmission electron micrograph (TEM) revealed the presence of numbers of Nodamura virus virions. At its core, the Nodamura virus possesses a positive-sense, single-stranded RNA virus ((+) ssRNA) genome. Its outer protein coat, or capsid, is icosahedral (T=3) in shape, which means that its composed of 32 equilateral, triangular facets.
This transmission electron micrograph (TEM) revealed the presence of numbers of Nodamura virus virions. At its core, the Nodamura virus possesses a positive-sense, single-stranded RNA virus ((+) ssRNA) genome. Its outer protein coat, or capsid, is icosahedral (T=3) in shape, which means that its composed of 32 equilateral, triangular facets.
11 Apr 2024
22 Feb 2024
Transmission electron micrograph of two plant rhabdovirus particles. 
Transmission electron micrograph of two plant rhabdovirus particles. 
22 Feb 2024
25 Jan 2024
Enveloped, brick-shaped or ovoid virion, 220-450 nm long and 140-260 nm wide. The surface membrane displays surface tubules or surface filaments. Two distinct infectious virus particles exists: the intracellular mature virus (IMV) and the extracellular enveloped virus (EEV).
Enveloped, brick-shaped or ovoid virion, 220-450 nm long and 140-260 nm wide. The surface membrane displays surface tubules or surface filaments. Two distinct infectious virus particles exists: the intracellular mature virus (IMV) and the extracellular enveloped virus (EEV).
25 Jan 2024
18 Feb 2024
Foliar chlorosis and mosaic of papaya (Carica papaya) caused by papaya ringspot virus (PRSV).
Foliar chlorosis and mosaic of papaya (Carica papaya) caused by papaya ringspot virus (PRSV).
18 Feb 2024
01 Mar 2024
Schematic drawings of a tailed phage virion (Escherichia virus T4, cross sections and side view). 
Schematic drawings of a tailed phage virion (Escherichia virus T4, cross sections and side view). 
01 Mar 2024
07 Feb 2024
Schematic drawing of a Bacillus phage Phi29 virion (cross section and side view). Non-enveloped, head-tail structure. The prolate capsid is about 45 x 54 nm, with a T=3, Q=5 symmetry. The tail is non-contractile and has a collar with 12 appendages attached to the neck region that are important for host cell recognition and entry. The 55 capsid (head) fibers are not always present and may have been lost in some lab strains. They may enhance the attachment of the virions onto the host cell wall.
Schematic drawing of a Bacillus phage Phi29 virion (cross section and side view). Non-enveloped, head-tail structure. The prolate capsid is about 45 x 54 nm, with a T=3, Q=5 symmetry. The tail is non-contractile and has a collar with 12 appendages attached to the neck region that are important for host cell recognition and entry. The 55 capsid (head) fibers are not always present and may have been lost in some lab strains. They may enhance the attachment of the virions onto the host cell wall.
07 Feb 2024
05 Jul 2024
Under the electron microscope, a macrophage dominates the scene, actively engulfing rod-shaped tuberculosis bacteria with its arm-like projections. The bacteria, characterized by their rough surfaces, are trapped by the macrophage's flexible membrane. This high-resolution image vividly illustrates the dynamic interplay between immune cells and pathogens, highlighting the crucial role of macrophages in defending against infections like tuberculosis.
Under the electron microscope, a macrophage dominates the scene, actively engulfing rod-shaped tuberculosis bacteria with its arm-like projections. The bacteria, characterized by their rough surfaces, are trapped by the macrophage's flexible membrane. This high-resolution image vividly illustrates the dynamic interplay between immune cells and pathogens, highlighting the crucial role of macrophages in defending against infections like tuberculosis.
05 Jul 2024
01 Feb 2024
(A) Diagram of a bi-antennary N-linked glycan. The terminal sialic acid residues are displayed with an α-2,3 linkage, as well as an α-2,6 linkage, to illustrate the “linear” and “bent” presentations. (B) Illustration of IAV cell entry. (i) IAVs initiate cell entry by using the HA receptor-binding domain (located in the HA1 region) to associate with sialylated glycoconjugates on a host “receptor.” Binding to the “receptor” triggers endocytosis. (ii) The virus then traffics to the endosome where the lower pH facilitates a conformational change in HA, exposing the fusion peptide (located in the HA2 region) for insertion into the endosomal membrane. (iii) The HA pre-hairpin conformation begins to collapse, forming a six-helix bundle that promotes hemifusion of the viral envelop with the endosomal membrane. At some point, the M2 channel opens to release the viral ribonucleoproteins (vRNPs) from M1 by acidifying the viral interior. (iv) HA further collapses into a trimer of hairpins to promote the formation of the fusion pore, which (v) releases the vRNPs into the cytosol. (vi) The exposed nuclear localization signals (NLS) on the vRNPs are recognized by the adaptor protein importin-α, leading to the recruitment of importin-β that (vii) facilitates the transport through the nuclear pore complex (NPC) and into the nucleus. [1]
(A) Diagram of a bi-antennary N-linked glycan. The terminal sialic acid residues are displayed with an α-2,3 linkage, as well as an α-2,6 linkage, to illustrate the “linear” and “bent” presentations. (B) Illustration of IAV cell entry. (i) IAVs initiate cell entry by using the HA receptor-binding domain (located in the HA1 region) to associate with sialylated glycoconjugates on a host “receptor.” Binding to the “receptor” triggers endocytosis. (ii) The virus then traffics to the endosome where the lower pH facilitates a conformational change in HA, exposing the fusion peptide (located in the HA2 region) for insertion into the endosomal membrane. (iii) The HA pre-hairpin conformation begins to collapse, forming a six-helix bundle that promotes hemifusion of the viral envelop with the endosomal membrane. At some point, the M2 channel opens to release the viral ribonucleoproteins (vRNPs) from M1 by acidifying the viral interior. (iv) HA further collapses into a trimer of hairpins to promote the formation of the fusion pore, which (v) releases the vRNPs into the cytosol. (vi) The exposed nuclear localization signals (NLS) on the vRNPs are recognized by the adaptor protein importin-α, leading to the recruitment of importin-β that (vii) facilitates the transport through the nuclear pore complex (NPC) and into the nucleus. [1]
01 Feb 2024
22 Feb 2024
Electron micrograph of herpes virus. 
Electron micrograph of herpes virus. 
22 Feb 2024
23 Feb 2024
Electron Micrographs of Sulfolobus islandicus rod-shaped viruses SIRV5 (left) and SIRV8 (right) stained with 2% uranyl acetate. Scale bar 100 nm [1].
Electron Micrographs of Sulfolobus islandicus rod-shaped viruses SIRV5 (left) and SIRV8 (right) stained with 2% uranyl acetate. Scale bar 100 nm [1].
23 Feb 2024
02 Feb 2024
Adenovirus-mediated gene therapy refers to a treatment approach that utilizes adenoviruses as vectors to deliver therapeutic genes into target cells or tissues. Adenoviruses, which are common viruses that cause respiratory and other infections in humans, have been modified to carry therapeutic genes instead of causing illness. These modified adenoviruses are used to deliver the therapeutic genes into the patient's cells, where they can correct genetic defects, enhance immune responses, or target specific diseases. This method holds promise for treating a variety of genetic disorders, cancers, and other diseases by introducing therapeutic genes into the body to replace or supplement defective or missing genes.
Adenovirus-mediated gene therapy refers to a treatment approach that utilizes adenoviruses as vectors to deliver therapeutic genes into target cells or tissues. Adenoviruses, which are common viruses that cause respiratory and other infections in humans, have been modified to carry therapeutic genes instead of causing illness. These modified adenoviruses are used to deliver the therapeutic genes into the patient's cells, where they can correct genetic defects, enhance immune responses, or target specific diseases. This method holds promise for treating a variety of genetic disorders, cancers, and other diseases by introducing therapeutic genes into the body to replace or supplement defective or missing genes.
02 Feb 2024
07 Feb 2024
Non-enveloped, head-tail structure. The capsid is about 90 nm in diameter, with a T=13 icosahedral symmetry. It is composed of 11 pentamers at the vertices and 120 hexamers on the faces. The tail is about 160 nm in length and 9 nm in width, with a subterminal disk and 3 long kinked fibers (120 nm). There is also a conical tip with a single straight central fiber (50 nm).[1]
Non-enveloped, head-tail structure. The capsid is about 90 nm in diameter, with a T=13 icosahedral symmetry. It is composed of 11 pentamers at the vertices and 120 hexamers on the faces. The tail is about 160 nm in length and 9 nm in width, with a subterminal disk and 3 long kinked fibers (120 nm). There is also a conical tip with a single straight central fiber (50 nm).[1]
07 Feb 2024
09 Feb 2024
(A) Schematic of the eight viral RNA (vRNA) gene segments that comprise the influenza A and B genomes. The 5′ and 3′ untranslated regions (UTRs), which contain the viral promoters, are represented with a line, and the box corresponds to the coding region within each vRNA. (B) Diagram of the viral mRNAs that are transcribed from the IAV (left) and IBV (right) vRNA templates. Boxes indicate the viral gene product encoded by each mRNA and the dashed lines show the alternative splicing of the IAV M and NS transcripts, as well as the IBV NS transcript. Red circles represent the 5′ M7pppG cap, black lines denote the 10–13 nucleotide, host-derived primers that are obtained by the cap-snatching mechanism of the viral polymerase. A(n) corresponds to the 3′ poly-A tail produced by reiterative stuttering of the viral polymerase. The smaller mRNAs (empty boxes) represent transcripts that encode nonessential accessory proteins found in many strains, whereas those that are less prevalent (PB2-S1, M42, and NS3) are not illustrated (6–11). (C) Diagram of an influenza A or B virus. The viral membrane proteins HA, NA, and M2 are shown, along with the eight viral ribonucleoproteins (vRNPs), and the matrix protein M1 that supports the viral envelope. To highlight the vRNP components, the illustration beneath the virus is not to scale. A single vRNA gene segment is shown wrapped around multiple nucleoprotein (NP) copies with the conserved promoter regions in the 5′ and 3′ UTRs forming a helical hairpin, which is bound by a single heterotrimeric viral RNA-dependent RNA polymerase (PB1, PB2, and PA). (D) Top view of an influenza virus cross-section showing the vRNP “1 + 7” configuration. vRNPs are depicted with black circles as it is not known if the positioning of a particular vRNP is conserved or interchangeable [1]. 
(A) Schematic of the eight viral RNA (vRNA) gene segments that comprise the influenza A and B genomes. The 5′ and 3′ untranslated regions (UTRs), which contain the viral promoters, are represented with a line, and the box corresponds to the coding region within each vRNA. (B) Diagram of the viral mRNAs that are transcribed from the IAV (left) and IBV (right) vRNA templates. Boxes indicate the viral gene product encoded by each mRNA and the dashed lines show the alternative splicing of the IAV M and NS transcripts, as well as the IBV NS transcript. Red circles represent the 5′ M7pppG cap, black lines denote the 10–13 nucleotide, host-derived primers that are obtained by the cap-snatching mechanism of the viral polymerase. A(n) corresponds to the 3′ poly-A tail produced by reiterative stuttering of the viral polymerase. The smaller mRNAs (empty boxes) represent transcripts that encode nonessential accessory proteins found in many strains, whereas those that are less prevalent (PB2-S1, M42, and NS3) are not illustrated (6–11). (C) Diagram of an influenza A or B virus. The viral membrane proteins HA, NA, and M2 are shown, along with the eight viral ribonucleoproteins (vRNPs), and the matrix protein M1 that supports the viral envelope. To highlight the vRNP components, the illustration beneath the virus is not to scale. A single vRNA gene segment is shown wrapped around multiple nucleoprotein (NP) copies with the conserved promoter regions in the 5′ and 3′ UTRs forming a helical hairpin, which is bound by a single heterotrimeric viral RNA-dependent RNA polymerase (PB1, PB2, and PA). (D) Top view of an influenza virus cross-section showing the vRNP “1 + 7” configuration. vRNPs are depicted with black circles as it is not known if the positioning of a particular vRNP is conserved or interchangeable [1]. 
09 Feb 2024
18 Feb 2024
Faint mosaic pattern caused by Prunus Necrotic Ringspot Virus (PNRSV), on "Graham Thomas" ('Ausmas'). Researchers maintain this infected plant at FSC to show the symptoms for teaching purposes. It is the only infected plant in our gardens.
Faint mosaic pattern caused by Prunus Necrotic Ringspot Virus (PNRSV), on "Graham Thomas" ('Ausmas'). Researchers maintain this infected plant at FSC to show the symptoms for teaching purposes. It is the only infected plant in our gardens.
18 Feb 2024
02 Apr 2024
This negative-stained transmission electron micrograph (TEM) depicts the ultrastructural details of an influenza virus particle, or virion. A member of the taxonomic family Orthomyxoviridae, the influenza virus is a single-stranded RNA organism. The flu is a contagious respiratory illness caused by influenza viruses. It can cause mild to severe illness, and at times can lead to death. The best way to prevent this illness is by getting a flu vaccination each fall.
This negative-stained transmission electron micrograph (TEM) depicts the ultrastructural details of an influenza virus particle, or virion. A member of the taxonomic family Orthomyxoviridae, the influenza virus is a single-stranded RNA organism. The flu is a contagious respiratory illness caused by influenza viruses. It can cause mild to severe illness, and at times can lead to death. The best way to prevent this illness is by getting a flu vaccination each fall.
02 Apr 2024
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