Bacteriophage SP01 Gene Product 56 Inhibits Bacillus subtilis Cell Division by Interacting with FtsL and Disrupting Pbp2B and FtsW Recruitment

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dc.citation.articleNumbere00463-20en_US
dc.citation.issueNumber2en_US
dc.citation.journalTitleJournal of Bacteriologyen_US
dc.citation.volumeNumber203en_US
dc.contributor.authorBhambhani, Amiten_US
dc.contributor.authorIadicicco, Isabellaen_US
dc.contributor.authorLee, Julesen_US
dc.contributor.authorAhmed, Syeden_US
dc.contributor.authorBelfatto, Maxen_US
dc.contributor.authorHeld, Daviden_US
dc.contributor.authorMarconi, Alexiaen_US
dc.contributor.authorParks, Aaronen_US
dc.contributor.authorStewart, Charles R.en_US
dc.contributor.authorMargolin, Williamen_US
dc.contributor.authorLevin, Petra Anneen_US
dc.contributor.authorHaeusser, Daniel P.en_US
dc.date.accessioned2021-06-17T13:20:55Zen_US
dc.date.available2021-06-17T13:20:55Zen_US
dc.date.issued2020en_US
dc.description.abstractPrevious work identified gene product 56 (gp56), encoded by the lytic bacteriophage SP01, as being responsible for inhibition of Bacillus subtilis cell division during its infection. Assembly of the essential tubulin-like protein FtsZ into a ring-shaped structure at the nascent site of cytokinesis determines the timing and position of division in most bacteria. This FtsZ ring serves as a scaffold for recruitment of other proteins into a mature division-competent structure permitting membrane constriction and septal cell wall synthesis. Here, we show that expression of the predicted 9.3-kDa gp56 of SP01 inhibits later stages of B. subtilis cell division without altering FtsZ ring assembly. Green fluorescent protein-tagged gp56 localizes to the membrane at the site of division. While its localization does not interfere with recruitment of early division proteins, gp56 interferes with the recruitment of late division proteins, including Pbp2b and FtsW. Imaging of cells with specific division components deleted or depleted and two-hybrid analyses suggest that gp56 localization and activity depend on its interaction with FtsL. Together, these data support a model in which gp56 interacts with a central part of the division machinery to disrupt late recruitment of the division proteins involved in septal cell wall synthesis.IMPORTANCE Studies over the past decades have identified bacteriophage-encoded factors that interfere with host cell shape or cytokinesis during viral infection. The phage factors causing cell filamentation that have been investigated to date all act by targeting FtsZ, the conserved prokaryotic tubulin homolog that composes the cytokinetic ring in most bacteria and some groups of archaea. However, the mechanisms of several phage factors that inhibit cytokinesis, including gp56 of bacteriophage SP01 of Bacillus subtilis, remain unexplored. Here, we show that, unlike other published examples of phage inhibition of cytokinesis, gp56 blocks B. subtilis cell division without targeting FtsZ. Rather, it utilizes the assembled FtsZ cytokinetic ring to localize to the division machinery and to block recruitment of proteins needed for septal cell wall synthesis.en_US
dc.identifier.citationBhambhani, Amit, Iadicicco, Isabella, Lee, Jules, et al.. "Bacteriophage SP01 Gene Product 56 Inhibits Bacillus subtilis Cell Division by Interacting with FtsL and Disrupting Pbp2B and FtsW Recruitment." <i>Journal of Bacteriology,</i> 203, no. 2 (2020) American Society for Microbiology: https://doi.org/10.1128/JB.00463-20.en_US
dc.identifier.doihttps://doi.org/10.1128/JB.00463-20en_US
dc.identifier.urihttps://hdl.handle.net/1911/110731en_US
dc.language.isoengen_US
dc.publisherAmerican Society for Microbiologyen_US
dc.rightsArticle is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use.en_US
dc.subject.keywordBacillus subtilisen_US
dc.subject.keywordFtsZen_US
dc.subject.keywordSP01en_US
dc.subject.keywordcell divisionen_US
dc.titleBacteriophage SP01 Gene Product 56 Inhibits Bacillus subtilis Cell Division by Interacting with FtsL and Disrupting Pbp2B and FtsW Recruitmenten_US
dc.typeJournal articleen_US
dc.type.dcmiTexten_US
dc.type.publicationpublisher versionen_US
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