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Genome evolution and plasticity of Serratia marcescens, an important multidrug-resistant nosocomial pathogen.

Iguchi A, Nagaya Y, Pradel E, Ooka T, Ogura Y, Katsura K, Kurokawa K, Oshima K, Hattori M, Parkhill J, Sebaihia M, Coulthurst SJ, Gotoh N, Thomson NR, Ewbank JJ, Hayashi T - Genome Biol Evol (2014)

Bottom Line: Naturally, it is found in many environmental niches, and is capable of infecting plants and animals.We further show that pSMC1 is most closely related to plasmids circulating in Pseudomonas species.Our data will provide a valuable basis for future studies on S. marcescens and new insights into the genetic mechanisms that underlie the emergence of pathogens highly resistant to multiple antimicrobial agents.

View Article: PubMed Central - PubMed

Affiliation: Interdisciplinary Research Organization, University of Miyazaki, JapanPresent address: Department of Animal and Grassland Sciences, Faculty of Agriculture, University of Miyazaki, Japan.

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Gene clusters for hemolysin/hemagglutin-like two-partner Type V secretion systems identified in SM39 and Db11. (A) The gene organization of the gene clusters for hemolysin/hemagglutin-like two-partner systems in SM39 and Db11 is shown. TpsA components are the passenger proteins (including the ShlA hemolysin and CdiA proteins) and TpsB components are the cognate translocator proteins (including ShlB and CdiB proteins). Although the shlBA operon (image 1) is conserved in the two strains, three additional gene clusters were found only in SM39. Two of these, SM39_2080-2077 (image 3) and SM39_3145-3141 (image 4), based on homology, encode Cdi systems. In addition to CdiA and CdiB proteins, a third component conferring resistance to the C-terminal toxin domain of CdiA is encoded downstream of CdiA, the CdiI immunity protein (SM39_2078 and SM39_3143, respectively). A putative “orphan” CdiA C-terminus (including a distinct potential toxin domain) and cognate CdiI pair is encoded by SM39_3142-3141. The function of the third SM39-specific cluster, SM39_0386-0387 (image 2), is unknown. (B) Similarities between the TpsA hemolysin/hemagglutin-related proteins (amino acid sequence identity) are shown, with those newly identified in SM39 showing partial similarity to ShlA.
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evu160-F5: Gene clusters for hemolysin/hemagglutin-like two-partner Type V secretion systems identified in SM39 and Db11. (A) The gene organization of the gene clusters for hemolysin/hemagglutin-like two-partner systems in SM39 and Db11 is shown. TpsA components are the passenger proteins (including the ShlA hemolysin and CdiA proteins) and TpsB components are the cognate translocator proteins (including ShlB and CdiB proteins). Although the shlBA operon (image 1) is conserved in the two strains, three additional gene clusters were found only in SM39. Two of these, SM39_2080-2077 (image 3) and SM39_3145-3141 (image 4), based on homology, encode Cdi systems. In addition to CdiA and CdiB proteins, a third component conferring resistance to the C-terminal toxin domain of CdiA is encoded downstream of CdiA, the CdiI immunity protein (SM39_2078 and SM39_3143, respectively). A putative “orphan” CdiA C-terminus (including a distinct potential toxin domain) and cognate CdiI pair is encoded by SM39_3142-3141. The function of the third SM39-specific cluster, SM39_0386-0387 (image 2), is unknown. (B) Similarities between the TpsA hemolysin/hemagglutin-related proteins (amino acid sequence identity) are shown, with those newly identified in SM39 showing partial similarity to ShlA.

Mentions: Multiple type V secretion systems (T5SSs) are present in SM39 and Db11. T5SSs include both autotransporters and two-partner systems (Grijpstra et al. 2013; Jacob-Dubuisson et al. 2013). An archetypal example of a two-partner T5SS is ShlBA; the hemolysin ShlA is one of the known major virulence factors in S. marcescens (Goluszko and Nowacki 1989). The shlBA operon is conserved in both strains. In contrast, three additional gene clusters, encoding two-partner systems with partial similarity to ShlA and other haemagglutinin-like proteins, were identified only in SM39 (fig. 5). Two of these, SM39_2080-2077 and SM39_3145-3141, appear to encode contact-dependent inhibition (Cdi) systems. In such systems, CdiB is a translocator protein that assembles the large, hemagglutinin domain-containing CdiA passenger protein on the cell surface (Aoki et al. 2010). Variable toxin domains are found at the C-terminus of CdiA (CdiACt), which mediate contact-dependent growth inhibition of competitor bacteria. Additionally, immunity proteins (CdiI) cognate to the CdiACt are encoded downstream of CdiA. Both loci contain a typical cdiBAI arrangement. The SM39_3144 locus also includes an “orphan” CdiACt–CdiI paizr (SM39_3142-3141). Orphan CdiACt–CdiI pairs contain truncated CdiA C-termini thought to represent remnants or reservoirs of alternative toxin domains, which can be exchanged to provide new antibacterial capability (Poole et al. 2011).Fig. 5.—


Genome evolution and plasticity of Serratia marcescens, an important multidrug-resistant nosocomial pathogen.

Iguchi A, Nagaya Y, Pradel E, Ooka T, Ogura Y, Katsura K, Kurokawa K, Oshima K, Hattori M, Parkhill J, Sebaihia M, Coulthurst SJ, Gotoh N, Thomson NR, Ewbank JJ, Hayashi T - Genome Biol Evol (2014)

Gene clusters for hemolysin/hemagglutin-like two-partner Type V secretion systems identified in SM39 and Db11. (A) The gene organization of the gene clusters for hemolysin/hemagglutin-like two-partner systems in SM39 and Db11 is shown. TpsA components are the passenger proteins (including the ShlA hemolysin and CdiA proteins) and TpsB components are the cognate translocator proteins (including ShlB and CdiB proteins). Although the shlBA operon (image 1) is conserved in the two strains, three additional gene clusters were found only in SM39. Two of these, SM39_2080-2077 (image 3) and SM39_3145-3141 (image 4), based on homology, encode Cdi systems. In addition to CdiA and CdiB proteins, a third component conferring resistance to the C-terminal toxin domain of CdiA is encoded downstream of CdiA, the CdiI immunity protein (SM39_2078 and SM39_3143, respectively). A putative “orphan” CdiA C-terminus (including a distinct potential toxin domain) and cognate CdiI pair is encoded by SM39_3142-3141. The function of the third SM39-specific cluster, SM39_0386-0387 (image 2), is unknown. (B) Similarities between the TpsA hemolysin/hemagglutin-related proteins (amino acid sequence identity) are shown, with those newly identified in SM39 showing partial similarity to ShlA.
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evu160-F5: Gene clusters for hemolysin/hemagglutin-like two-partner Type V secretion systems identified in SM39 and Db11. (A) The gene organization of the gene clusters for hemolysin/hemagglutin-like two-partner systems in SM39 and Db11 is shown. TpsA components are the passenger proteins (including the ShlA hemolysin and CdiA proteins) and TpsB components are the cognate translocator proteins (including ShlB and CdiB proteins). Although the shlBA operon (image 1) is conserved in the two strains, three additional gene clusters were found only in SM39. Two of these, SM39_2080-2077 (image 3) and SM39_3145-3141 (image 4), based on homology, encode Cdi systems. In addition to CdiA and CdiB proteins, a third component conferring resistance to the C-terminal toxin domain of CdiA is encoded downstream of CdiA, the CdiI immunity protein (SM39_2078 and SM39_3143, respectively). A putative “orphan” CdiA C-terminus (including a distinct potential toxin domain) and cognate CdiI pair is encoded by SM39_3142-3141. The function of the third SM39-specific cluster, SM39_0386-0387 (image 2), is unknown. (B) Similarities between the TpsA hemolysin/hemagglutin-related proteins (amino acid sequence identity) are shown, with those newly identified in SM39 showing partial similarity to ShlA.
Mentions: Multiple type V secretion systems (T5SSs) are present in SM39 and Db11. T5SSs include both autotransporters and two-partner systems (Grijpstra et al. 2013; Jacob-Dubuisson et al. 2013). An archetypal example of a two-partner T5SS is ShlBA; the hemolysin ShlA is one of the known major virulence factors in S. marcescens (Goluszko and Nowacki 1989). The shlBA operon is conserved in both strains. In contrast, three additional gene clusters, encoding two-partner systems with partial similarity to ShlA and other haemagglutinin-like proteins, were identified only in SM39 (fig. 5). Two of these, SM39_2080-2077 and SM39_3145-3141, appear to encode contact-dependent inhibition (Cdi) systems. In such systems, CdiB is a translocator protein that assembles the large, hemagglutinin domain-containing CdiA passenger protein on the cell surface (Aoki et al. 2010). Variable toxin domains are found at the C-terminus of CdiA (CdiACt), which mediate contact-dependent growth inhibition of competitor bacteria. Additionally, immunity proteins (CdiI) cognate to the CdiACt are encoded downstream of CdiA. Both loci contain a typical cdiBAI arrangement. The SM39_3144 locus also includes an “orphan” CdiACt–CdiI paizr (SM39_3142-3141). Orphan CdiACt–CdiI pairs contain truncated CdiA C-termini thought to represent remnants or reservoirs of alternative toxin domains, which can be exchanged to provide new antibacterial capability (Poole et al. 2011).Fig. 5.—

Bottom Line: Naturally, it is found in many environmental niches, and is capable of infecting plants and animals.We further show that pSMC1 is most closely related to plasmids circulating in Pseudomonas species.Our data will provide a valuable basis for future studies on S. marcescens and new insights into the genetic mechanisms that underlie the emergence of pathogens highly resistant to multiple antimicrobial agents.

View Article: PubMed Central - PubMed

Affiliation: Interdisciplinary Research Organization, University of Miyazaki, JapanPresent address: Department of Animal and Grassland Sciences, Faculty of Agriculture, University of Miyazaki, Japan.

Show MeSH
Related in: MedlinePlus