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  1. Article: A novel stabilization mechanism accommodating genome length variation in evolutionarily related viral capsids.

    Podgorski, Jennifer M / Podgorski, Joshua / Abad, Lawrence / Jacobs-Sera, Deborah / Freeman, Krista G / Brown, Colin / Hatfull, Graham / Luque, Antoni / White, Simon J

    bioRxiv : the preprint server for biology

    2023  

    Abstract: Tailed bacteriophages are one of the most numerous and diverse group of viruses. They store their genome at quasi-crystalline densities in capsids built from multiple copies of proteins adopting the HK97-fold. The high density of the genome exerts an ... ...

    Abstract Tailed bacteriophages are one of the most numerous and diverse group of viruses. They store their genome at quasi-crystalline densities in capsids built from multiple copies of proteins adopting the HK97-fold. The high density of the genome exerts an internal pressure, requiring a maturation process that reinforces their capsids. However, it is unclear how capsid stabilization strategies have adapted to accommodate the evolution of larger genomes in this virus group. Here we characterized a novel capsid reinforcement mechanism in two evolutionary-related actinobacteriophages that modifies the length of a stabilization protein to accommodate a larger genome while maintaining the same capsid size. We used cryo-EM to reveal that capsids contained split hexamers of HK97-fold proteins with a stabilization protein in the chasm. The observation of split hexamers in mature capsids was unprecedented, so we rationalized this result mathematically, discovering that icosahedral capsids can be formed by all split or skewed hexamers as long as their T-number is not a multiple of three. Our results suggest that analogous stabilization mechanisms can be present in other icosahedral capsids, and they provide a strategy for engineering capsids accommodating larger DNA cargoes as gene delivery systems.
    Language English
    Publishing date 2023-11-03
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2023.11.03.565530
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: A structural dendrogram of the actinobacteriophage major capsid proteins provides important structural insights into the evolution of capsid stability.

    Podgorski, Jennifer M / Freeman, Krista / Gosselin, Sophia / Huet, Alexis / Conway, James F / Bird, Mary / Grecco, John / Patel, Shreya / Jacobs-Sera, Deborah / Hatfull, Graham / Gogarten, Johann Peter / Ravantti, Janne / White, Simon J

    Structure (London, England : 1993)

    2023  Volume 31, Issue 3, Page(s) 282–294.e5

    Abstract: Many double-stranded DNA viruses, including tailed bacteriophages (phages) and herpesviruses, use the HK97-fold in their major capsid protein to make the capsomers of the icosahedral viral capsid. After the genome packaging at near-crystalline densities, ...

    Abstract Many double-stranded DNA viruses, including tailed bacteriophages (phages) and herpesviruses, use the HK97-fold in their major capsid protein to make the capsomers of the icosahedral viral capsid. After the genome packaging at near-crystalline densities, the capsid is subjected to a major expansion and stabilization step that allows it to withstand environmental stresses and internal high pressure. Several different mechanisms for stabilizing the capsid have been structurally characterized, but how these mechanisms have evolved is still not understood. Using cryo-EM structure determination of 10 capsids, structural comparisons, phylogenetic analyses, and Alphafold predictions, we have constructed a detailed structural dendrogram describing the evolution of capsid structural stability within the actinobacteriophages. We show that the actinobacteriophage major capsid proteins can be classified into 15 groups based upon their HK97-fold.
    MeSH term(s) Capsid Proteins/chemistry ; Capsid/chemistry ; Phylogeny ; Bacteriophages/metabolism ; Virus Assembly ; Cryoelectron Microscopy
    Chemical Substances Capsid Proteins
    Language English
    Publishing date 2023-01-16
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 1213087-4
    ISSN 1878-4186 ; 0969-2126
    ISSN (online) 1878-4186
    ISSN 0969-2126
    DOI 10.1016/j.str.2022.12.012
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Virion glycosylation influences mycobacteriophage immune recognition.

    Freeman, Krista G / Robotham, Anna C / Parks, Olivia B / Abad, Lawrence / Jacobs-Sera, Deborah / Lauer, Michael J / Podgorski, Jennifer M / Zhang, Yu / Williams, John V / White, Simon J / Kelly, John F / Hatfull, Graham F / Pope, Welkin H

    Cell host & microbe

    2023  Volume 31, Issue 7, Page(s) 1216–1231.e6

    Abstract: Glycosylation of eukaryotic virus particles is common and influences their uptake, trafficking, and immune recognition. In contrast, glycosylation of bacteriophage particles has not been reported; phage virions typically do not enter the cytoplasm upon ... ...

    Abstract Glycosylation of eukaryotic virus particles is common and influences their uptake, trafficking, and immune recognition. In contrast, glycosylation of bacteriophage particles has not been reported; phage virions typically do not enter the cytoplasm upon infection, and they do not generally inhabit eukaryotic systems. We show here that several genomically distinct phages of Mycobacteria are modified with glycans attached to the C terminus of capsid and tail tube protein subunits. These O-linked glycans influence antibody production and recognition, shielding viral particles from antibody binding and reducing production of neutralizing antibodies. Glycosylation is mediated by phage-encoded glycosyltransferases, and genomic analysis suggests that they are relatively common among mycobacteriophages. Putative glycosyltransferases are also encoded by some Gordonia and Streptomyces phages, but there is little evidence of glycosylation among the broader phage population. The immune response to glycosylated phage virions in mice suggests that glycosylation may be an advantageous property for phage therapy of Mycobacterium infections.
    MeSH term(s) Animals ; Mice ; Mycobacteriophages/genetics ; Mycobacteriophages/metabolism ; Glycosylation ; Bacteriophages/genetics ; Virion/genetics ; Glycosyltransferases/metabolism ; Polysaccharides/metabolism
    Chemical Substances Glycosyltransferases (EC 2.4.-) ; Polysaccharides
    Language English
    Publishing date 2023-06-16
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2278004-X
    ISSN 1934-6069 ; 1931-3128
    ISSN (online) 1934-6069
    ISSN 1931-3128
    DOI 10.1016/j.chom.2023.05.028
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 6578: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
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