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Gliding Motility and the Type IX Secretion System

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  • Author: Mark J. McBride1
  • Editors: Maria Sandkvist2, Eric Cascales3, Peter J. Christie4
  • VIEW AFFILIATIONS HIDE AFFILIATIONS
    Affiliations: 1: Department of Biological Sciences, University of Wisconsin-Milwaukee, Milwaukee, WI 53201; 2: Department of Microbiology and Immunology, University of Michigan, Ann Arbor, Michigan; 3: CNRS Aix-Marseille Université, Mediterranean Institute of Microbiology, Marseille, France; 4: Department of Microbiology and Molecular Genetics, McGovern Medical School, Houston, Texas
  • Source: microbiolspec February 2019 vol. 7 no. 1 doi:10.1128/microbiolspec.PSIB-0002-2018
  • Received 16 August 2018 Accepted 07 January 2019 Published 15 February 2019
  • Mark J. McBride, [email protected]
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  • Abstract:

    Members of the phylum have many unique features, including gliding motility and the type IX protein secretion system (T9SS). gliding and T9SSs are common in, but apparently confined to, this phylum. Most, but not all, members of the phylum secrete proteins using the T9SS, and most also exhibit gliding motility. T9SSs secrete cell surface components of the gliding motility machinery and also secrete many extracellular or cell surface enzymes, adhesins, and virulence factors. The components of the T9SS are novel and are unrelated to those of other bacterial secretion systems. Proteins secreted by the T9SS rely on the Sec system to cross the cytoplasmic membrane, and they use the T9SS for delivery across the outer membrane. Secreted proteins typically have conserved C-terminal domains that target them to the T9SS. Some of the T9SS components were initially identified as proteins required for gliding motility. Gliding does not involve flagella or pili and instead relies on the rapid movement of motility adhesins, such as SprB, along the cell surface by the gliding motor. Contact of the adhesins with the substratum provides the traction that results in cell movement. SprB and other motility adhesins are delivered to the cell surface by the T9SS. Gliding and the T9SS appear to be intertwined, and components of the T9SS that span the cytoplasmic membrane may energize both gliding and protein secretion. The functions of the individual proteins in each process are the subject of ongoing investigations.

  • Citation: McBride M. 2019. Gliding Motility and the Type IX Secretion System. Microbiol Spectrum 7(1):PSIB-0002-2018. doi:10.1128/microbiolspec.PSIB-0002-2018.

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/content/journal/microbiolspec/10.1128/microbiolspec.PSIB-0002-2018
2019-02-15
2019-06-26

Abstract:

Members of the phylum have many unique features, including gliding motility and the type IX protein secretion system (T9SS). gliding and T9SSs are common in, but apparently confined to, this phylum. Most, but not all, members of the phylum secrete proteins using the T9SS, and most also exhibit gliding motility. T9SSs secrete cell surface components of the gliding motility machinery and also secrete many extracellular or cell surface enzymes, adhesins, and virulence factors. The components of the T9SS are novel and are unrelated to those of other bacterial secretion systems. Proteins secreted by the T9SS rely on the Sec system to cross the cytoplasmic membrane, and they use the T9SS for delivery across the outer membrane. Secreted proteins typically have conserved C-terminal domains that target them to the T9SS. Some of the T9SS components were initially identified as proteins required for gliding motility. Gliding does not involve flagella or pili and instead relies on the rapid movement of motility adhesins, such as SprB, along the cell surface by the gliding motor. Contact of the adhesins with the substratum provides the traction that results in cell movement. SprB and other motility adhesins are delivered to the cell surface by the T9SS. Gliding and the T9SS appear to be intertwined, and components of the T9SS that span the cytoplasmic membrane may energize both gliding and protein secretion. The functions of the individual proteins in each process are the subject of ongoing investigations.

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Figures

Image of FIGURE 1
FIGURE 1

Gliding of cells. Characteristic movements of cells. Spreading colonies formed by wild-type cells and nonspreading colonies formed by cells of a nonmotile mutant. Bar corresponds to 1 mm. Model of gliding. Gld proteins in the cell envelope form the PMF-powered rotary motors that are attached to the cell wall and propel adhesins, such as SprB and RemA, along looped helical tracks on the cell surface. The action of the motors on adhesins that are attached to the substratum results in forward movement and rotation of the cell. Two rotary motors are shown. Rotation of one motor propels a baseplate carrying SprB and RemA adhesins and delivers it to the next motor. Modified from reference 13 .

Source: microbiolspec February 2019 vol. 7 no. 1 doi:10.1128/microbiolspec.PSIB-0002-2018
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Image of FIGURE 2
FIGURE 2

T9SS and gliding motility proteins. Proteins in blue are associated with the T9SS, and proteins in green are motility proteins that are not directly associated with the T9SS. Orthologous T9SS proteins between panels A and B are shown in the same relative positions, color, and shapes. GldK, GldL, GldM, GldN, SprA, SprE, and SprT correspond to PorK, PorL, PorM, PorN, Sov, PorW, and PorT, respectively. Black lines are lipid tails on lipoproteins. Proteins secreted by the T9SS have predicted N-terminal signal peptides (yellow) that target them to the Sec system for export across the cytoplasmic membrane (CM) and C-terminal domains (red) that target them to the T9SS for secretion across the outer membrane (OM). Proteins are not drawn to scale, and stoichiometry of components is not illustrated. T9SS proteins. Where protein names were not available, locus tags (from strain W83) were used. The gingipain protease RgpB is shown covalently attached to the outer membrane acidic lipopolysaccharide (A-LPS). Secretion complex and attachment complex are indicated by the large and small blue barrels, respectively. T9SS and gliding motility proteins. SprB is a motility adhesin that is propelled by some of the other proteins shown. SprF is required for secretion of SprB but not for secretion of other proteins. SprF and nine other proteins are related to PorP. PorV is required for secretion of ChiA and many other proteins, but not for secretion of SprB.

Source: microbiolspec February 2019 vol. 7 no. 1 doi:10.1128/microbiolspec.PSIB-0002-2018
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Tables

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TABLE 1

T9SS components

Source: microbiolspec February 2019 vol. 7 no. 1 doi:10.1128/microbiolspec.PSIB-0002-2018

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