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ichv 1 strain auburn 1  (ATCC)


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    ATCC ichv 1 strain auburn 1
    (A) Terminase based phylogeny of the Alloherpesviridae and related viruses. Amino acid sequence data for selected viruses representing the phylogenetic spread of herpesviruses were used along with that of the bacteriophage T4. The names of virus genera and families are in red and blue font, respectively. The nomenclature in black font consists of the underlying GenBank nucleotide accession number followed by the virus name, which is either a systematic one for classified members of the Alloherpesviridae , or a common one for unclassified viruses grouping in the Alloherpesviridae , and viruses in other families. The names of unclassified viruses are marked with asterisks. The scale shows the number of substitutions per position. (B,C) Micrographs of <t>purified</t> <t>IcHV-1</t> capsids (B) and virions (C), scale bar = 100nm. (D,E) Icosahedral reconstructions of IcHV-1 capsid (D) and virion (E). Radial-depth cued isosurface representations are shown, viewed along a two-fold symmetry axis. The colour key indicates the radial distance in nm from the particle centre. The penton, hexons, and triplexes in the asymmetric unit are colour-coded and indicated in (D). Two copies of the inner-tegument protein pORF65 are indicated by purple/pink arrows in (E). In the virion reconstruction, density was found in the distal hexon channels, occluding the opening. Cross-sections through the reconstruction showed weak, blurred density radiating from this feature (inset, E).
    Ichv 1 Strain Auburn 1, supplied by ATCC, used in various techniques. Bioz Stars score: 94/100, based on 49 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 94 stars, based on 49 article reviews
    ichv 1 strain auburn 1 - by Bioz Stars, 2026-03
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    Images

    1) Product Images from "Cryo-EM of a Divergent Herpesvirus Reveals Structural Conservation and Novelty Including a Portal-Vertex Tegument Protein with Multiple Macrodomain-like Folds"

    Article Title: Cryo-EM of a Divergent Herpesvirus Reveals Structural Conservation and Novelty Including a Portal-Vertex Tegument Protein with Multiple Macrodomain-like Folds

    Journal: bioRxiv

    doi: 10.64898/2026.02.13.705735

    (A) Terminase based phylogeny of the Alloherpesviridae and related viruses. Amino acid sequence data for selected viruses representing the phylogenetic spread of herpesviruses were used along with that of the bacteriophage T4. The names of virus genera and families are in red and blue font, respectively. The nomenclature in black font consists of the underlying GenBank nucleotide accession number followed by the virus name, which is either a systematic one for classified members of the Alloherpesviridae , or a common one for unclassified viruses grouping in the Alloherpesviridae , and viruses in other families. The names of unclassified viruses are marked with asterisks. The scale shows the number of substitutions per position. (B,C) Micrographs of purified IcHV-1 capsids (B) and virions (C), scale bar = 100nm. (D,E) Icosahedral reconstructions of IcHV-1 capsid (D) and virion (E). Radial-depth cued isosurface representations are shown, viewed along a two-fold symmetry axis. The colour key indicates the radial distance in nm from the particle centre. The penton, hexons, and triplexes in the asymmetric unit are colour-coded and indicated in (D). Two copies of the inner-tegument protein pORF65 are indicated by purple/pink arrows in (E). In the virion reconstruction, density was found in the distal hexon channels, occluding the opening. Cross-sections through the reconstruction showed weak, blurred density radiating from this feature (inset, E).
    Figure Legend Snippet: (A) Terminase based phylogeny of the Alloherpesviridae and related viruses. Amino acid sequence data for selected viruses representing the phylogenetic spread of herpesviruses were used along with that of the bacteriophage T4. The names of virus genera and families are in red and blue font, respectively. The nomenclature in black font consists of the underlying GenBank nucleotide accession number followed by the virus name, which is either a systematic one for classified members of the Alloherpesviridae , or a common one for unclassified viruses grouping in the Alloherpesviridae , and viruses in other families. The names of unclassified viruses are marked with asterisks. The scale shows the number of substitutions per position. (B,C) Micrographs of purified IcHV-1 capsids (B) and virions (C), scale bar = 100nm. (D,E) Icosahedral reconstructions of IcHV-1 capsid (D) and virion (E). Radial-depth cued isosurface representations are shown, viewed along a two-fold symmetry axis. The colour key indicates the radial distance in nm from the particle centre. The penton, hexons, and triplexes in the asymmetric unit are colour-coded and indicated in (D). Two copies of the inner-tegument protein pORF65 are indicated by purple/pink arrows in (E). In the virion reconstruction, density was found in the distal hexon channels, occluding the opening. Cross-sections through the reconstruction showed weak, blurred density radiating from this feature (inset, E).

    Techniques Used: Sequencing, Virus, Purification

    Solvent-excluded surface (SES) representations of the asymmetric units of the IcHV-1 capsid (A) and virion (B). The asymmetric units contain 16 copies of the major capsid protein pORF39, (blue): six (P1-P6) make up a complete P-hexon, six (C1-C6) make up a complete C-hexon, and three (E1-E3) contribute to half of an E-hexon. One copy is present and contributed to the penton. The asymmetric unit comprises six triplexes each composed of one copy of pORF53 (purple), and two copies of pORF27 (white). In the virion, two copies of the inner-tegument protein pORF65 are positioned on the Tb and Tc triplexes. Additionally, three copies of pORF42 occlude the distal tips of the hexon-channels. (C) Schematic representation of the virion asymmetric unit coloured as in (A)–(B). (D) A ribbon diagram of the penton pORF39 is shown, color-coded to highlight the domain structure previously defined for orthoherpesvirus MCPs. The IcHV-1 MCP features an extended C-terminal region (red), which folds toward the helix–hairpin domain to form a helical bundle. This region and adopts different conformations in penton versus hexon environments (compare E and F). (E) A ribbon diagram of the penton MCP is shown in rainbow colour-scheme from N-terminus (blue) to C-terminus (red). (F) A ribbon diagram of the hexon MCP is shown in the same rainbow colour-scheme. A second, neighbouring copy is shown in both ribbon and transparent sovent-excluded surface (blue), to highlight the domain insertion of the C-terminal domain in this form of the IcHV-1 capsomere. (G) A ribbon diagram of pORF53 is shown in rainbow colour-scheme, with the associated two copies of pORF27 shown as SES (white). (H) Two copies of pORF27 are shown as ribbon diagrams, one in rainbow colour-scheme and one in white. The associated copy of pORF53 is displayed as a purple SES. (I) SES representation of a P-hexon (blue/gold) and adjacent Tc triplex (purple/white). pORF65 is shown as a ribbon diagram in rainbow colour-scheme.
    Figure Legend Snippet: Solvent-excluded surface (SES) representations of the asymmetric units of the IcHV-1 capsid (A) and virion (B). The asymmetric units contain 16 copies of the major capsid protein pORF39, (blue): six (P1-P6) make up a complete P-hexon, six (C1-C6) make up a complete C-hexon, and three (E1-E3) contribute to half of an E-hexon. One copy is present and contributed to the penton. The asymmetric unit comprises six triplexes each composed of one copy of pORF53 (purple), and two copies of pORF27 (white). In the virion, two copies of the inner-tegument protein pORF65 are positioned on the Tb and Tc triplexes. Additionally, three copies of pORF42 occlude the distal tips of the hexon-channels. (C) Schematic representation of the virion asymmetric unit coloured as in (A)–(B). (D) A ribbon diagram of the penton pORF39 is shown, color-coded to highlight the domain structure previously defined for orthoherpesvirus MCPs. The IcHV-1 MCP features an extended C-terminal region (red), which folds toward the helix–hairpin domain to form a helical bundle. This region and adopts different conformations in penton versus hexon environments (compare E and F). (E) A ribbon diagram of the penton MCP is shown in rainbow colour-scheme from N-terminus (blue) to C-terminus (red). (F) A ribbon diagram of the hexon MCP is shown in the same rainbow colour-scheme. A second, neighbouring copy is shown in both ribbon and transparent sovent-excluded surface (blue), to highlight the domain insertion of the C-terminal domain in this form of the IcHV-1 capsomere. (G) A ribbon diagram of pORF53 is shown in rainbow colour-scheme, with the associated two copies of pORF27 shown as SES (white). (H) Two copies of pORF27 are shown as ribbon diagrams, one in rainbow colour-scheme and one in white. The associated copy of pORF53 is displayed as a purple SES. (I) SES representation of a P-hexon (blue/gold) and adjacent Tc triplex (purple/white). pORF65 is shown as a ribbon diagram in rainbow colour-scheme.

    Techniques Used: Solvent

    (A–C) Ribbon diagram representations of the portal complexes of the IcHV-1 capsid (A), virion (B), and that of HSV-1 (C), each shown in rainbow colouring. The IcHV-1 portal consists of 12 copies of pORF37, likewise the HSV-1 portal complex comprises 12 copies of pUL6. All structures exhibit C12 symmetry. (D, E) Corresponding cryo-EM density maps of the IcHV-1 capsid (D) and virion (E), portals, resolved to 4.3 Å and 4.6 Å respectively. In the capsid map, an additional density is observed on the outer face of the wing domain (purple), assigned by ModelAngelo as the N-terminus of pORF37. Due to discontinuity in the density, we were unable to determine whether this short α-helix originates from the same monomer or is contributed by a neighbouring subunit. (F, G) Structural comparison of HSV-1 pUL6 (F) and IcHV-1 Orf37 (G). Each monomer is shown as a ribbon diagram coloured to highlight the domain structure (left) and rainbow representation (right). (H) Two adjacent virion portal pORF37 monomers are shown as ribbon diagrams (yellow and blue) within the reconstructed volume (transparent surface), to highlight two instances of β-augmentation. Yellow and blue boxes indicate unique monomer–monomer interaction regions. (I) Enlarged view of the yellow-boxed region, showing β-strand augmentation in which a three-stranded β-sheet is assembled by two neighbouring protomers to form the clip region. (J, K) View of the top of the wing domain in the capsid (J) and virion (K) portal, highlighting a rearrangement between the two forms whereby the N-terminal β-strand which contributes to a four-stranded β-sheet in one monomer (black arrows) inserts instead into the same β-sheet in the neighbouring protomer, forming an inter-subunit β-sheet extension. This rearrangement likely accounts for the loss of the N-terminal helical density at the base of the wing domain in the virion portal.
    Figure Legend Snippet: (A–C) Ribbon diagram representations of the portal complexes of the IcHV-1 capsid (A), virion (B), and that of HSV-1 (C), each shown in rainbow colouring. The IcHV-1 portal consists of 12 copies of pORF37, likewise the HSV-1 portal complex comprises 12 copies of pUL6. All structures exhibit C12 symmetry. (D, E) Corresponding cryo-EM density maps of the IcHV-1 capsid (D) and virion (E), portals, resolved to 4.3 Å and 4.6 Å respectively. In the capsid map, an additional density is observed on the outer face of the wing domain (purple), assigned by ModelAngelo as the N-terminus of pORF37. Due to discontinuity in the density, we were unable to determine whether this short α-helix originates from the same monomer or is contributed by a neighbouring subunit. (F, G) Structural comparison of HSV-1 pUL6 (F) and IcHV-1 Orf37 (G). Each monomer is shown as a ribbon diagram coloured to highlight the domain structure (left) and rainbow representation (right). (H) Two adjacent virion portal pORF37 monomers are shown as ribbon diagrams (yellow and blue) within the reconstructed volume (transparent surface), to highlight two instances of β-augmentation. Yellow and blue boxes indicate unique monomer–monomer interaction regions. (I) Enlarged view of the yellow-boxed region, showing β-strand augmentation in which a three-stranded β-sheet is assembled by two neighbouring protomers to form the clip region. (J, K) View of the top of the wing domain in the capsid (J) and virion (K) portal, highlighting a rearrangement between the two forms whereby the N-terminal β-strand which contributes to a four-stranded β-sheet in one monomer (black arrows) inserts instead into the same β-sheet in the neighbouring protomer, forming an inter-subunit β-sheet extension. This rearrangement likely accounts for the loss of the N-terminal helical density at the base of the wing domain in the virion portal.

    Techniques Used: Cryo-EM Sample Prep, Comparison



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    (A) Terminase based phylogeny of the Alloherpesviridae and related viruses. Amino acid sequence data for selected viruses representing the phylogenetic spread of herpesviruses were used along with that of the bacteriophage T4. The names of virus genera and families are in red and blue font, respectively. The nomenclature in black font consists of the underlying GenBank nucleotide accession number followed by the virus name, which is either a systematic one for classified members of the Alloherpesviridae , or a common one for unclassified viruses grouping in the Alloherpesviridae , and viruses in other families. The names of unclassified viruses are marked with asterisks. The scale shows the number of substitutions per position. (B,C) Micrographs of purified IcHV-1 capsids (B) and virions (C), scale bar = 100nm. (D,E) Icosahedral reconstructions of IcHV-1 capsid (D) and virion (E). Radial-depth cued isosurface representations are shown, viewed along a two-fold symmetry axis. The colour key indicates the radial distance in nm from the particle centre. The penton, hexons, and triplexes in the asymmetric unit are colour-coded and indicated in (D). Two copies of the inner-tegument protein pORF65 are indicated by purple/pink arrows in (E). In the virion reconstruction, density was found in the distal hexon channels, occluding the opening. Cross-sections through the reconstruction showed weak, blurred density radiating from this feature (inset, E).

    Journal: bioRxiv

    Article Title: Cryo-EM of a Divergent Herpesvirus Reveals Structural Conservation and Novelty Including a Portal-Vertex Tegument Protein with Multiple Macrodomain-like Folds

    doi: 10.64898/2026.02.13.705735

    Figure Lengend Snippet: (A) Terminase based phylogeny of the Alloherpesviridae and related viruses. Amino acid sequence data for selected viruses representing the phylogenetic spread of herpesviruses were used along with that of the bacteriophage T4. The names of virus genera and families are in red and blue font, respectively. The nomenclature in black font consists of the underlying GenBank nucleotide accession number followed by the virus name, which is either a systematic one for classified members of the Alloherpesviridae , or a common one for unclassified viruses grouping in the Alloherpesviridae , and viruses in other families. The names of unclassified viruses are marked with asterisks. The scale shows the number of substitutions per position. (B,C) Micrographs of purified IcHV-1 capsids (B) and virions (C), scale bar = 100nm. (D,E) Icosahedral reconstructions of IcHV-1 capsid (D) and virion (E). Radial-depth cued isosurface representations are shown, viewed along a two-fold symmetry axis. The colour key indicates the radial distance in nm from the particle centre. The penton, hexons, and triplexes in the asymmetric unit are colour-coded and indicated in (D). Two copies of the inner-tegument protein pORF65 are indicated by purple/pink arrows in (E). In the virion reconstruction, density was found in the distal hexon channels, occluding the opening. Cross-sections through the reconstruction showed weak, blurred density radiating from this feature (inset, E).

    Article Snippet: IcHV-1 strain Auburn 1 (ATCC VR-665) was propagated in brown bullhead (BB) cells (ATCC CCL-59) in 30 T-175 flasks.

    Techniques: Sequencing, Virus, Purification

    Solvent-excluded surface (SES) representations of the asymmetric units of the IcHV-1 capsid (A) and virion (B). The asymmetric units contain 16 copies of the major capsid protein pORF39, (blue): six (P1-P6) make up a complete P-hexon, six (C1-C6) make up a complete C-hexon, and three (E1-E3) contribute to half of an E-hexon. One copy is present and contributed to the penton. The asymmetric unit comprises six triplexes each composed of one copy of pORF53 (purple), and two copies of pORF27 (white). In the virion, two copies of the inner-tegument protein pORF65 are positioned on the Tb and Tc triplexes. Additionally, three copies of pORF42 occlude the distal tips of the hexon-channels. (C) Schematic representation of the virion asymmetric unit coloured as in (A)–(B). (D) A ribbon diagram of the penton pORF39 is shown, color-coded to highlight the domain structure previously defined for orthoherpesvirus MCPs. The IcHV-1 MCP features an extended C-terminal region (red), which folds toward the helix–hairpin domain to form a helical bundle. This region and adopts different conformations in penton versus hexon environments (compare E and F). (E) A ribbon diagram of the penton MCP is shown in rainbow colour-scheme from N-terminus (blue) to C-terminus (red). (F) A ribbon diagram of the hexon MCP is shown in the same rainbow colour-scheme. A second, neighbouring copy is shown in both ribbon and transparent sovent-excluded surface (blue), to highlight the domain insertion of the C-terminal domain in this form of the IcHV-1 capsomere. (G) A ribbon diagram of pORF53 is shown in rainbow colour-scheme, with the associated two copies of pORF27 shown as SES (white). (H) Two copies of pORF27 are shown as ribbon diagrams, one in rainbow colour-scheme and one in white. The associated copy of pORF53 is displayed as a purple SES. (I) SES representation of a P-hexon (blue/gold) and adjacent Tc triplex (purple/white). pORF65 is shown as a ribbon diagram in rainbow colour-scheme.

    Journal: bioRxiv

    Article Title: Cryo-EM of a Divergent Herpesvirus Reveals Structural Conservation and Novelty Including a Portal-Vertex Tegument Protein with Multiple Macrodomain-like Folds

    doi: 10.64898/2026.02.13.705735

    Figure Lengend Snippet: Solvent-excluded surface (SES) representations of the asymmetric units of the IcHV-1 capsid (A) and virion (B). The asymmetric units contain 16 copies of the major capsid protein pORF39, (blue): six (P1-P6) make up a complete P-hexon, six (C1-C6) make up a complete C-hexon, and three (E1-E3) contribute to half of an E-hexon. One copy is present and contributed to the penton. The asymmetric unit comprises six triplexes each composed of one copy of pORF53 (purple), and two copies of pORF27 (white). In the virion, two copies of the inner-tegument protein pORF65 are positioned on the Tb and Tc triplexes. Additionally, three copies of pORF42 occlude the distal tips of the hexon-channels. (C) Schematic representation of the virion asymmetric unit coloured as in (A)–(B). (D) A ribbon diagram of the penton pORF39 is shown, color-coded to highlight the domain structure previously defined for orthoherpesvirus MCPs. The IcHV-1 MCP features an extended C-terminal region (red), which folds toward the helix–hairpin domain to form a helical bundle. This region and adopts different conformations in penton versus hexon environments (compare E and F). (E) A ribbon diagram of the penton MCP is shown in rainbow colour-scheme from N-terminus (blue) to C-terminus (red). (F) A ribbon diagram of the hexon MCP is shown in the same rainbow colour-scheme. A second, neighbouring copy is shown in both ribbon and transparent sovent-excluded surface (blue), to highlight the domain insertion of the C-terminal domain in this form of the IcHV-1 capsomere. (G) A ribbon diagram of pORF53 is shown in rainbow colour-scheme, with the associated two copies of pORF27 shown as SES (white). (H) Two copies of pORF27 are shown as ribbon diagrams, one in rainbow colour-scheme and one in white. The associated copy of pORF53 is displayed as a purple SES. (I) SES representation of a P-hexon (blue/gold) and adjacent Tc triplex (purple/white). pORF65 is shown as a ribbon diagram in rainbow colour-scheme.

    Article Snippet: IcHV-1 strain Auburn 1 (ATCC VR-665) was propagated in brown bullhead (BB) cells (ATCC CCL-59) in 30 T-175 flasks.

    Techniques: Solvent

    (A–C) Ribbon diagram representations of the portal complexes of the IcHV-1 capsid (A), virion (B), and that of HSV-1 (C), each shown in rainbow colouring. The IcHV-1 portal consists of 12 copies of pORF37, likewise the HSV-1 portal complex comprises 12 copies of pUL6. All structures exhibit C12 symmetry. (D, E) Corresponding cryo-EM density maps of the IcHV-1 capsid (D) and virion (E), portals, resolved to 4.3 Å and 4.6 Å respectively. In the capsid map, an additional density is observed on the outer face of the wing domain (purple), assigned by ModelAngelo as the N-terminus of pORF37. Due to discontinuity in the density, we were unable to determine whether this short α-helix originates from the same monomer or is contributed by a neighbouring subunit. (F, G) Structural comparison of HSV-1 pUL6 (F) and IcHV-1 Orf37 (G). Each monomer is shown as a ribbon diagram coloured to highlight the domain structure (left) and rainbow representation (right). (H) Two adjacent virion portal pORF37 monomers are shown as ribbon diagrams (yellow and blue) within the reconstructed volume (transparent surface), to highlight two instances of β-augmentation. Yellow and blue boxes indicate unique monomer–monomer interaction regions. (I) Enlarged view of the yellow-boxed region, showing β-strand augmentation in which a three-stranded β-sheet is assembled by two neighbouring protomers to form the clip region. (J, K) View of the top of the wing domain in the capsid (J) and virion (K) portal, highlighting a rearrangement between the two forms whereby the N-terminal β-strand which contributes to a four-stranded β-sheet in one monomer (black arrows) inserts instead into the same β-sheet in the neighbouring protomer, forming an inter-subunit β-sheet extension. This rearrangement likely accounts for the loss of the N-terminal helical density at the base of the wing domain in the virion portal.

    Journal: bioRxiv

    Article Title: Cryo-EM of a Divergent Herpesvirus Reveals Structural Conservation and Novelty Including a Portal-Vertex Tegument Protein with Multiple Macrodomain-like Folds

    doi: 10.64898/2026.02.13.705735

    Figure Lengend Snippet: (A–C) Ribbon diagram representations of the portal complexes of the IcHV-1 capsid (A), virion (B), and that of HSV-1 (C), each shown in rainbow colouring. The IcHV-1 portal consists of 12 copies of pORF37, likewise the HSV-1 portal complex comprises 12 copies of pUL6. All structures exhibit C12 symmetry. (D, E) Corresponding cryo-EM density maps of the IcHV-1 capsid (D) and virion (E), portals, resolved to 4.3 Å and 4.6 Å respectively. In the capsid map, an additional density is observed on the outer face of the wing domain (purple), assigned by ModelAngelo as the N-terminus of pORF37. Due to discontinuity in the density, we were unable to determine whether this short α-helix originates from the same monomer or is contributed by a neighbouring subunit. (F, G) Structural comparison of HSV-1 pUL6 (F) and IcHV-1 Orf37 (G). Each monomer is shown as a ribbon diagram coloured to highlight the domain structure (left) and rainbow representation (right). (H) Two adjacent virion portal pORF37 monomers are shown as ribbon diagrams (yellow and blue) within the reconstructed volume (transparent surface), to highlight two instances of β-augmentation. Yellow and blue boxes indicate unique monomer–monomer interaction regions. (I) Enlarged view of the yellow-boxed region, showing β-strand augmentation in which a three-stranded β-sheet is assembled by two neighbouring protomers to form the clip region. (J, K) View of the top of the wing domain in the capsid (J) and virion (K) portal, highlighting a rearrangement between the two forms whereby the N-terminal β-strand which contributes to a four-stranded β-sheet in one monomer (black arrows) inserts instead into the same β-sheet in the neighbouring protomer, forming an inter-subunit β-sheet extension. This rearrangement likely accounts for the loss of the N-terminal helical density at the base of the wing domain in the virion portal.

    Article Snippet: IcHV-1 strain Auburn 1 (ATCC VR-665) was propagated in brown bullhead (BB) cells (ATCC CCL-59) in 30 T-175 flasks.

    Techniques: Cryo-EM Sample Prep, Comparison