The 1.59Å resolution structure of the minor pseudopilin EpsH of Vibrio cholerae reveals a long flexible loop

Raghunathan, K.; Vago, Frank S.; Grindem, David; Ball, Terry; Wedemeyer, William J.; Bagdasarian, Michael; Arvidson, Dennis N.

doi:10.1016/j.bbapap.2013.11.013

Cited by 6 publications

(7 citation statements)

References 57 publications

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“…The role of XcpU in the pseudopilus tip complex still needs to be elucidated, though its structure in Vibrio cholera has been elucidated[ 16 , 38 ]. Similar to the studies of pulH in K .…”

Section: Discussionmentioning

confidence: 99%

Structure-guided disruption of the pseudopilus tip complex inhibits the Type II secretion in Pseudomonas aeruginosa

Zhang

Faucher

Zhang³

et al. 2018

PLoS Pathog

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Pseudomonas aeruginosa utilizes the Type II secretion system (T2SS) to translocate a wide range of large, structured protein virulence factors through the periplasm to the extracellular environment for infection. In the T2SS, five pseudopilins assemble into the pseudopilus that acts as a piston to extrude exoproteins out of cells. Through structure determination of the pseudopilin complexes of XcpVWX and XcpVW and function analysis, we have confirmed that two minor pseudopilins, XcpV and XcpW, constitute a core complex indispensable to the pseudopilus tip. The absence of either XcpV or -W resulted in the non-functional T2SS. Our small-angle X-ray scattering experiment for the first time revealed the architecture of the entire pseudopilus tip and established the working model. Based on the interaction interface of complexes, we have developed inhibitory peptides. The structure-based peptides not only disrupted of the XcpVW core complex and the entire pseudopilus tip in vitro but also inhibited the T2SS in vivo. More importantly, these peptides effectively reduced the virulence of P. aeruginosa towards Caenorhabditis elegans.

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“…The role of XcpU in the pseudopilus tip complex still needs to be elucidated, though its structure in Vibrio cholera has been elucidated[ 16 , 38 ]. Similar to the studies of pulH in K .…”

Section: Discussionmentioning

confidence: 99%

Structure-guided disruption of the pseudopilus tip complex inhibits the Type II secretion in Pseudomonas aeruginosa

Zhang

Faucher

Zhang³

et al. 2018

PLoS Pathog

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“…8). In the pseudopilin, this region was proposed to participate in selection of secretion substrates (51). There is no evidence that the T4aP system of P. aeruginosa is involved in secretion, and the short uncharged loop in the corresponding position of FimU may reflect this divergence in function.…”

Section: Identification Of a Putative Minor Pilin-pily1mentioning

confidence: 99%

“…In addition, EpsH has a long, partly disordered loop between swapped ␤-strands 5 and 6, which extends from the core of the protein. Those residues that could be resolved in this disordered region have different conformations in the two structures, as well as in separate monomers in the asymmetric unit (51). Based on its charged and apparently dynamic properties, this region of EpsH was suggested to be involved in recognition of T2S system secretion substrates (51).…”

Section: Pilvwx and Pily1mentioning

confidence: 99%

“…Those residues that could be resolved in this disordered region have different conformations in the two structures, as well as in separate monomers in the asymmetric unit (51). Based on its charged and apparently dynamic properties, this region of EpsH was suggested to be involved in recognition of T2S system secretion substrates (51). In FimU, the corresponding segment (connecting ␤-strands 4 and 5) is much shorter (five amino acids) and lacks charged residues, resulting in a more compact protein.…”

Section: Pilvwx and Pily1mentioning

confidence: 99%

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Pseudomonas aeruginosa Minor Pilins Prime Type IVa Pilus Assembly and Promote Surface Display of the PilY1 Adhesin

Nguyen

Sugiman-Marangos

Harvey

et al. 2015

Journal of Biological Chemistry

120

142

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Background: Type IV pili (T4P) are virulence factors composed of major and minor pilins. Results: Minor pilins prime pilus assembly and traffic anti-retraction protein PilY1 to the surface; FimU and GspH are structurally similar. Conclusion: Minor pilins are essential for pilus assembly and function. Significance: This work expands the structural and functional similarities between the T4P and T2S systems.

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“…The rest of the pseudopilus constitutes a helical filament formed by the major pseudopilin GspG (Campos et al, 2010; Köhler et al, 2004; López‐Castilla et al, 2017). All the pseudopilins have a characteristic fold comprising an N‐terminal α‐helix, a short variable region, and a four‐stranded C‐terminal antiparallel β‐sheet (López‐Castilla et al, 2017; Raghunathan et al, 2014; Yanez et al, 2008). GspGHI has a conserved glutamic acid at amino acid position 5 (Glu5) within the mature sequence.…”

Section: Introductionmentioning

confidence: 99%

The structure and mechanism of the bacterial type II secretion system

Naskar

Höhl

Tassinari

et al. 2020

Molecular Microbiology

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The T2SS is a macromolecular complex that spans the cell envelope of many Gram-negative bacteria. It is part of a much larger superfamily of type IV filament containing systems all of which share homologous components and conserved mechanistic principles. These include the type 4a and 4b pilus (Craig et al., 2019), tight adherence (Tad) pilus (Tomich et al., 2007), mannose-sensitive hemagglutinin pilus (Marsh and Taylor, 1999), competence pilus (Piepenbrink, 2019) and archaeal T4 pilus and flagellum (Makarova et al., 2016). These systems are ancient and fundamental to both bacterial and archaeal kingdoms with phylogeny analyses suggesting a lineage split from within the last universal common ancestor (LUCA) (Denise et al., 2019). The T2SS is particularly concentrated in the Alpha-, Beta-, Gamma-and Delta-proteobacteria, as well as the Bacteroidetes and Deferribacteres (Denise et al., 2019).

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The 1.59Å resolution structure of the minor pseudopilin EpsH of Vibrio cholerae reveals a long flexible loop

Cited by 6 publications

References 57 publications

Structure-guided disruption of the pseudopilus tip complex inhibits the Type II secretion in Pseudomonas aeruginosa

Structure-guided disruption of the pseudopilus tip complex inhibits the Type II secretion in Pseudomonas aeruginosa

Pseudomonas aeruginosa Minor Pilins Prime Type IVa Pilus Assembly and Promote Surface Display of the PilY1 Adhesin

The structure and mechanism of the bacterial type II secretion system

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