Whole genome sequence analysis reveals the broad distribution of the RtxA type 1 secretion system and four novel putative type 1 secretion systems throughout the Legionella genus

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dc.contributor.authorBrown, Connor L.en
dc.contributor.authorGarner, Emilyen
dc.contributor.authorJospin, Guillaumeen
dc.contributor.authorCoil, David A.en
dc.contributor.authorSchwake, David Ottoen
dc.contributor.authorEisen, Jonathan A.en
dc.contributor.authorMukhopadhyay, Biswarupen
dc.contributor.authorPruden, Amyen
dc.contributor.departmentCivil and Environmental Engineeringen
dc.contributor.departmentBiochemistryen
dc.date.accessioned2020-02-09T12:56:05Zen
dc.date.available2020-02-09T12:56:05Zen
dc.date.issued2020-01-01en
dc.date.updated2020-02-09T12:56:01Zen
dc.description.abstractType 1 secretion systems (T1SSs) are broadly distributed among bacteria and translocate effectors with diverse function across the bacterial cell membrane. Legionella pneumophila, the species most commonly associated with Legionellosis, encodes a T1SS at the lssXYZABD locus which is responsible for the secretion of the virulence factor RtxA. Many investigations have failed to detect lssD, the gene encoding the membrane fusion protein of the RtxA T1SS, in non-pneumophila Legionella, which has led to the assumption that this system is a virulence factor exclusively possessed by L. pneumophila. Here we discovered RtxA and its associated T1SS in a novel Legionella taurinensis strain, leading us to question whether this system may be more widespread than previously thought. Through a bioinformatic analysis of publicly available data, we classified and determined the distribution of four T1SSs including the RtxA T1SS and four novel T1SSs among diverse Legionella spp. The ABC transporter of the novel Legionella T1SS Legionella repeat protein secretion system shares structural similarity to those of diverse T1SS families, including the alkaline protease T1SS in Pseudomonas aeruginosa. The Legionella bacteriocin (1–3) secretion systems T1SSs are novel putative bacteriocin transporting T1SSs as their ABC transporters include C-39 peptidase domains in their N-terminal regions, with LB2SS and LB3SS likely constituting a nitrile hydratase leader peptide transport T1SSs. The LB1SS is more closely related to the colicin V T1SS in Escherichia coli. Of 45 Legionella spp. whole genomes examined, 19 (42%) were determined to possess lssB and lssD homologs. Of these 19, only 7 (37%) are known pathogens. There was no difference in the proportions of disease associated and non-disease associated species that possessed the RtxA T1SS (p = 0.4), contrary to the current consensus regarding the RtxA T1SS. These results draw into question the nature of RtxA and its T1SS as a singular virulence factor. Future studies should investigate mechanistic explanations for the association of RtxA with virulence.en
dc.description.versionPublished (Publication status)en
dc.format.extentPages e0223033en
dc.format.mimetypeapplication/pdfen
dc.identifier.doihttps://doi.org/10.1371/journal.pone.0223033en
dc.identifier.eissn1932-6203en
dc.identifier.issn1932-6203en
dc.identifier.issue1en
dc.identifier.orcidMukhopadhyay, Biswarup [0000-0003-0736-0298]en
dc.identifier.otherPONE-D-19-25375 (PII)en
dc.identifier.pmid31935215en
dc.identifier.urihttp://hdl.handle.net/10919/96769en
dc.identifier.volume15en
dc.language.isoenen
dc.publisherPLoSen
dc.relation.urihttps://www.ncbi.nlm.nih.gov/pubmed/31935215en
dc.rightsCreative Commons Attribution 4.0 Internationalen
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/en
dc.titleWhole genome sequence analysis reveals the broad distribution of the RtxA type 1 secretion system and four novel putative type 1 secretion systems throughout the Legionella genusen
dc.title.serialPLoS ONEen
dc.typeArticle - Refereeden
dc.type.dcmitypeTexten
dc.type.otherJournal Articleen
dcterms.dateAccepted2019-12-17en
pubs.organisational-group/Virginia Tech/Engineeringen
pubs.organisational-group/Virginia Tech/All T&R Facultyen
pubs.organisational-group/Virginia Tech/Engineering/Civil & Environmental Engineeringen
pubs.organisational-group/Virginia Tech/Engineering/COE T&R Facultyen
pubs.organisational-group/Virginia Tech/University Research Institutes/Fralin Life Sciences/Durelle Scotten
pubs.organisational-group/Virginia Techen
pubs.organisational-group/Virginia Tech/University Research Institutes/Fralin Life Sciencesen
pubs.organisational-group/Virginia Tech/University Research Institutesen
pubs.organisational-group/Virginia Tech/Agriculture & Life Sciencesen
pubs.organisational-group/Virginia Tech/Faculty of Health Sciencesen
pubs.organisational-group/Virginia Tech/Agriculture & Life Sciences/Biochemistryen
pubs.organisational-group/Virginia Tech/Agriculture & Life Sciences/CALS T&R Facultyen

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