Lysis Cassette-Mediated Exoprotein Release in Yersinia entomophaga Is Controlled by a PhoB-Like Regulator

Schoof, Marion; O’Callaghan, Maureen; Hefer, Charles A.; Glare, Travis R.; Paulson, Amber Rose; Hurst, Mark R. H.

doi:10.1128/spectrum.00364-23

Cited by 4 publications

(9 citation statements)

References 62 publications

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“…This is consistent with a report from Y. enterocolitica , where a phage-related holin/endolysin pair was suggested to be important for the release of its insecticidal toxin complex 29 . A similar LC has been identified by a transposon screen in Y. entomophaga WT, but the LC was not encoded in the vicinity of the YenTc gene cluster 25 , 30 . This LC encodes a holin ( holA ), an endolysin ( pepB ) and two spanin ( rz , rz1 ) genes (Fig.…”

Section: Resultssupporting

confidence: 54%

“…b , Schematic of the LC gene cluster in Y. entomophaga , which comprises a holin, an endolysin and two overlapping spanin open reading frames (gene names are indicated). This gene cluster has been previously identified, being involved in general exoproteome release 30 . c , Western blot analysis against YenA1 and RecA (loading control) of Y. entomophaga WT and ΔLC mutants showed that both strains expressed YenA1, but release into the supernatant (sup.)…”

Section: Resultsmentioning

confidence: 98%

“…This LC encodes a holin ( holA ), an endolysin ( pepB ) and two spanin ( rz , rz1 ) genes (Fig. 4b ), and was shown to be required for general exoprotein release 30 .…”

Section: Resultsmentioning

confidence: 99%

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Stepwise assembly and release of Tc toxins from Yersinia entomophaga

Feldmüller,

Ericson,

Afanasyev

et al. 2024

Nat Microbiol

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Tc toxins are virulence factors of bacterial pathogens. Although their structure and intoxication mechanism are well understood, it remains elusive where this large macromolecular complex is assembled and how it is released. Here we show by an integrative multiscale imaging approach that Yersinia entomophaga Tc (YenTc) toxin components are expressed only in a subpopulation of cells that are ‘primed’ with several other potential virulence factors, including filaments of the protease M66/StcE. A phage-like lysis cassette is required for YenTc release; however, before resulting in complete cell lysis, the lysis cassette generates intermediate ‘ghost’ cells, which may serve as assembly compartments and become packed with assembled YenTc holotoxins. We hypothesize that this stepwise mechanism evolved to minimize the number of cells that need to be killed. The occurrence of similar lysis cassettes in diverse organisms indicates a conserved mechanism for Tc toxin release that may apply to other extracellular macromolecular machines.

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Section: Resultssupporting

confidence: 54%

Section: Resultsmentioning

confidence: 98%

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Stepwise assembly and release of Tc toxins from Yersinia entomophaga

Feldmüller,

Ericson,

Afanasyev

et al. 2024

Nat Microbiol

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“…1b ). Importantly, another group independently verified the importance of YenLC and RoeA for lytic protein release and YenTc production during review of this study 44 . To avoid potential confusion, we have adopted YenLC component nomenclature from that study.…”

Section: Resultsmentioning

confidence: 60%

Yersinia entomophaga Tc toxin is released by T10SS-dependent lysis of specialized cell subpopulations

Sitsel,

Wang,

Janning

et al. 2024

Nat Microbiol

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Disease-causing bacteria secrete numerous toxins to invade and subjugate their hosts. Unlike many smaller toxins, the secretion machinery of most large toxins remains enigmatic. By combining genomic editing, proteomic profiling and cryo-electron tomography of the insect pathogen Yersinia entomophaga, we demonstrate that a specialized subset of these cells produces a complex toxin cocktail, including the nearly ribosome-sized Tc toxin YenTc, which is subsequently exported by controlled cell lysis using a transcriptionally coupled, pH-dependent type 10 secretion system (T10SS). Our results dissect the Tc toxin export process by a T10SS, identifying that T10SSs operate via a previously unknown lytic mode of action and establishing them as crucial players in the size-insensitive release of cytoplasmically folded toxins. With T10SSs directly embedded in Tc toxin operons of major pathogens, we anticipate that our findings may model an important aspect of pathogenesis in bacteria with substantial impact on agriculture and healthcare.

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“…The data presented here corroborates that the sef-tc island likely existed before becoming associated with the STAMP backbone. that Yersinia Holin (lysis cassette), which is associated with secreting Tcs, is only expressed in a subset of the population (<10%) (Schoof et al, 2023). Through TEM, it was established that only ~10% of WT S. entomophila A1MO2 cells were observed to be fimbriated.…”

Section: Expression and Deletion Of Sef Operon Confirms Fimbriae Prod...mentioning

confidence: 99%

Serratia‐based toxin cluster elements are associated with a type I fimbria

Sitter,

Schoof,

Glare

et al. 2024

MicrobiologyOpen

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A soil bacterium in the Serratia genus, carrying a 153 kb conjugative amber disease‐associated plasmid (pADAP), is commercially exploited for population control of the New Zealand endemic pest beetle Costelytra giveni (Coleoptera: Scarabaeidae). The main insecticidal elements are an anti‐feeding prophage and the Sep ABC toxin complex (Tc). Homologs of pADAP, encoding variant Tcs, convey different beetle disease phenotypes. To investigate the correlation between variable bioactivity and the Tc variant, 76 Serratia plasmids were sequenced, resulting in the identification of four additional tc variants. All Serratia tc variants were found to be colocated with a conserved type 1 sef fimbrial‐like operon, indicating a conserved sef‐tc genetic island not observed outside of the Serratia genus. The conserved co‐location of the fimbrial and tc genes suggests the fimbriae somehow contribute to the lifestyle of Tc‐producing cells. Expression of the sef operon in a fim‐null Escherichia coli strain revealed fimbriae presence while a constructed sef‐deficient mutant showed no reduction of virulence or host colonization. Although no detectable contribution of Sef to amber disease in C. giveni was observed, the Sef adhesin sequences clustered similarly to the Serratia species encoding it, suggesting Sef has a species‐specific function.

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Lysis Cassette-Mediated Exoprotein Release in Yersinia entomophaga Is Controlled by a PhoB-Like Regulator

Cited by 4 publications

References 62 publications

Stepwise assembly and release of Tc toxins from Yersinia entomophaga

Stepwise assembly and release of Tc toxins from Yersinia entomophaga

Yersinia entomophaga Tc toxin is released by T10SS-dependent lysis of specialized cell subpopulations

Serratia‐based toxin cluster elements are associated with a type I fimbria

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