Literature DB >> 15150235

Bacteriophage Tuc2009 encodes a tail-associated cell wall-degrading activity.

John G Kenny1, Stephen McGrath, Gerald F Fitzgerald, Douwe van Sinderen.   

Abstract

Tuc2009 is a P335-type member of the tailed-phage supergroup Siphoviridae and was originally identified as a resident prophage of the gram-positive bacterium Lactococcus lactis UC509. A Tuc2009 gene designated tal2009 which is located within the morphogenic module was shown to specify a lytic activity within the 3' portion of its coding region. Comparative sequence analysis indicated that the cell wall-degrading part of Tal2009 is a member of the M37 protein family and that Tal2009 lacks a cell-binding domain, a finding supported by binding studies. Tal2009 appears to undergo self-mediated posttranslational processing in both L. lactis and Escherichia coli. Antibodies directed against a purified C-terminal portion of Tal2009 were used for immunoelectron microscopy, which showed that Tal2009 is located at the tail tip of Tuc2009. Antibody neutralization studies demonstrated that Tal2009-directed antibodies inhibited the ability of phage to mediate host lysis by more than 100-fold. These data indicate that tal2009 encodes a tail-associated lysin involved in localized cell wall degradation, thus allowing the Tuc2009 DNA injection machinery access to the membrane of its bacterial host.

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Year:  2004        PMID: 15150235      PMCID: PMC415775          DOI: 10.1128/JB.186.11.3480-3491.2004

Source DB:  PubMed          Journal:  J Bacteriol        ISSN: 0021-9193            Impact factor:   3.490


  48 in total

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Review 4.  Acquisition and rearrangement of sequence motifs in the evolution of bacteriophage tail fibres.

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  47 in total

1.  Identification of the lower baseplate protein as the antireceptor of the temperate lactococcal bacteriophages TP901-1 and Tuc2009.

Authors:  Christina S Vegge; Finn K Vogensen; Stephen Mc Grath; Horst Neve; Douwe van Sinderen; Lone Brøndsted
Journal:  J Bacteriol       Date:  2006-01       Impact factor: 3.490

2.  Anatomy of a lactococcal phage tail.

Authors:  Stephen Mc Grath; Horst Neve; Jos F M L Seegers; Robyn Eijlander; Christina S Vegge; Lone Brøndsted; Knut J Heller; Gerald F Fitzgerald; Finn K Vogensen; Douwe van Sinderen
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3.  Crystal and cryoEM structural studies of a cell wall degrading enzyme in the bacteriophage phi29 tail.

Authors:  Ye Xiang; Marc C Morais; Daniel N Cohen; Valorie D Bowman; Dwight L Anderson; Michael G Rossmann
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4.  The peptidoglycan hydrolase of Staphylococcus aureus bacteriophage 11 plays a structural role in the viral particle.

Authors:  Lorena Rodríguez-Rubio; Nuria Quiles-Puchalt; Beatriz Martínez; Ana Rodríguez; José R Penadés; Pilar García
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5.  Structure and functional analysis of the host recognition device of lactococcal phage tuc2009.

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Journal:  J Virol       Date:  2013-05-22       Impact factor: 5.103

6.  The opening of the SPP1 bacteriophage tail, a prevalent mechanism in Gram-positive-infecting siphophages.

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Journal:  J Biol Chem       Date:  2011-05-26       Impact factor: 5.157

Review 7.  A common evolutionary origin for tailed-bacteriophage functional modules and bacterial machineries.

Authors:  David Veesler; Christian Cambillau
Journal:  Microbiol Mol Biol Rev       Date:  2011-09       Impact factor: 11.056

8.  The lactococcal phages Tuc2009 and TP901-1 incorporate two alternate forms of their tail fiber into their virions for infection specialization.

Authors:  Stephen R Stockdale; Jennifer Mahony; Pascal Courtin; Marie-Pierre Chapot-Chartier; Jan-Peter van Pijkeren; Robert A Britton; Horst Neve; Knut J Heller; Bashir Aideh; Finn K Vogensen; Douwe van Sinderen
Journal:  J Biol Chem       Date:  2013-01-08       Impact factor: 5.157

9.  Identification of tail genes in the temperate phage 16-3 of Sinorhizobium meliloti 41.

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10.  Viral infection modulation and neutralization by camelid nanobodies.

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Journal:  Proc Natl Acad Sci U S A       Date:  2013-03-25       Impact factor: 11.205

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