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The structures of bacteriophages K1E and K1-5 explain processive degradation of polysaccharide capsules and evolution of new host specificities.

The structures of bacteriophages K1E and K1-5 explain processive degradation of polysaccharide capsules and evolution of new host specificities. Research Abstract Details 

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  • The structures of bacteriophages K1E and K1-5 explain processive degradation of polysaccharide capsules and evolution of new host specificities. Abstract Text:

    petr g leimanPetr G Leiman,anthony j battistiAnthony J Battisti,valorie d bowmanValorie D Bowman,katharina stummeyerKatharina Stummeyer,martina Martina ,rita gerardy-schahnRita Gerardy-Schahn,dean schollDean Scholl,ian j molineuxIan J Molineux,

    External polysaccharides of many pathogenic bacteria form capsules protecting the bacteria from the animal immune system and phage infection. However, some bacteriophages can digest these capsules using glycosidases displayed on the phage particle. We have utilized cryo-electron microscopy to determine the structures of phages K1E and K1-5 and thereby establish the mechanism by which these phages attain and switch their host specificity. Using a specific glycosidase, both phages penetrate the capsule and infect the neuroinvasive human pathogen Escherichia coli K1. In addition to the K1-specific glycosidase, each K1-5 particle carries a second enzyme that allows it to infect E. coli K5, whose capsule is chemically different from that of K1. The enzymes are organized into a multiprotein complex attached via an adapter protein to the virus portal vertex, through which the DNA is ejected during infection. The structure of the complex suggests a mechanism for the apparent processivity of degradation that occurs as the phage drills through the polysaccharide capsule. The enzymes recognize the adapter protein by a conserved N-terminal sequence, providing a mechanism for phages to acquire different enzymes and thus to evolve new host specificities.

    The structures of bacteriophages K1E and K1-5 explain processive degradation of polysaccharide capsules and evolution of new host specificities. Publishing Authors By Initials

    pg leimanPG Leiman,aj battistiAJ Battisti,vd bowmanVD Bowman,k stummeyerK Stummeyer,m M ,r gerardy-schahnR Gerardy-Schahn,d schollD Scholl,ij molineuxIJ Molineux,

    For similar viruses: virion research abstracts see: viruses: virion research

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    The structures of bacteriophages K1E and K1-5 explain processive degradation of polysaccharide capsules and evolution of new host specificities. Journal Published:

    PUBLICATION TYPE: Research Support, U.S. Gov't,

    Journal: Journal of molecular biology

    VOLUME: 371

    Page Numbers: 836-49

    Journal Abbreviation: J. Mol. Biol.

    ISSN: 0022-2836

    DAY: 2

    MONTH: 06

    YEAR: 2007

    The structures of bacteriophages K1E and K1-5 explain processive degradation of polysaccharide capsules and evolution of new host specificities. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 2985088

    The structures of bacteriophages K1E and K1-5 explain processive degradation of polysaccharide capsules and evolution of new host specificities. Keywords Mesh Terms:

    KEYWORDS: Virion

    MESH TERMS: chemistry

    Chemical & Substance for Abstract: The structures of bacteriophages K1E and K1-5 explain processive degradation of polysaccharide capsules and evolution of new host specificities. Information

    Substance Name: Viral Proteins

    Registry Number: 0

    Grant and Affiliation Information for The structures of bacteriophages K1E and K1-5 explain processive degradation of polysaccharide capsules and evolution of new host specificities.

    AFFILIATION: Department of Biological Sciences, Purdue University, 915 W. State Street, West Lafayette, IN 47907-2054, USA. leiman@purdue.edu

    Country: England

    England Research PublicationEngland Research Publication

    AGENCY: United States NCRR

    GRANT: P41 RR-01081

    ACRONYM: RR

    MEDLINETA: J Mol Biol

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