<i>In vitro</i>
            self-assembly of tailorable nanotubes from a simple protein building block

Ballister, Edward R.; Lai, Angela H.; Zuckermann, Ronald N.; Cheng, Yifan; Mougous, Joseph D.

doi:10.1073/pnas.0712247105

Cited by 276 publications

(255 citation statements)

References 31 publications

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“…The macromolecular structure of the T6SS has not yet been fully resolved, and it is not known how the T6SS machine assembles or delivers effectors. Based on recent studies (Ballister et al, 2008;Basler et al, 2012;Hood et al, 2010;Leiman et al, 2009;Pukatzki et al, 2007), Hcps and VgrGs are believed to form a pilus that is displayed on the bacterial surface. The VgrG ΔvgrG1/pBR322 ΔvgrG1/comp Fig.…”

Section: Discussionmentioning

confidence: 99%

Evaluation of the roles played by Hcp and VgrG type 6 secretion system effectors in Aeromonas hydrophila SSU pathogenesis

et al. 2013

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Aeromonas hydrophila, a Gram-negative bacterium, is an emerging human pathogen equipped with both a type 3 and a type 6 secretion system (T6SS). In this study, we evaluated the roles played by paralogous T6SS effector proteins, hemolysin co-regulated proteins (Hcp-1 and -2) and valine glycine repeat G (VgrG-1, -2 and -3) protein family members in A. hydrophila SSU pathogenesis by generating various combinations of deletion mutants of the their genes. In addition to their predicted roles as structural components and effector proteins of the T6SS, our data clearly demonstrated that paralogues of Hcp and VgrG also influenced bacterial motility, protease production and biofilm formation. Surprisingly, there was limited to no observed functional redundancy among and/or between the aforementioned T6SS effector paralogues in multiple assays. Our data indicated that Hcp and VgrG paralogues located within the T6SS cluster were more involved in forming T6SS structures, while the primary roles of Hcp-1 and VgrG-1, located outside of the T6SS cluster, were as T6SS effectors. In terms of influence on bacterial physiology, Hcp-1, but not Hcp-2, influenced bacterial motility and protease production, and in its absence, increases in both of the aforementioned activities were observed. Likewise, VgrG-1 played a major role in regulating bacterial protease production, while VgrG-2 and VgrG-3 were critical in regulating bacterial motility and biofilm formation. In an intraperitoneal murine model of infection, all Hcp and VgrG paralogues were required for optimal bacterial virulence and dissemination to mouse peripheral organs. Importantly, the observed phenotypic alterations of the T6SS mutants could be fully complemented. Taking these results together, we have further established the roles played by the two known T6SS effectors of A. hydrophila by defining their contributions to T6SS function and virulence in both in vitro and in vivo models of infection.

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Section: Discussionmentioning

confidence: 99%

Evaluation of the roles played by Hcp and VgrG type 6 secretion system effectors in Aeromonas hydrophila SSU pathogenesis

et al. 2013

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“…1a) 29 . Owing to its defined geometrical shape, it has been used and characterized as nanotechnological building block for protein fibres 30,31 and the assembly of quantum dot biohybrid structures by our group 32 .…”

Section: Resultsmentioning

confidence: 99%

Molecular protein adaptor with genetically encoded interaction sites guiding the hierarchical assembly of plasmonically active nanoparticle architectures

et al. 2015

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The control over the defined assembly of nano-objects with nm-precision is important to create systems and materials with enhanced properties, for example, metamaterials. In nature, the precise assembly of inorganic nano-objects with unique features, for example, magnetosomes, is accomplished by efficient and reliable recognition schemes involving protein effectors. Here we present a molecular approach using protein-based 'adaptors/ connectors' with genetically encoded interaction sites to guide the assembly and functionality of different plasmonically active gold nanoparticle architectures (AuNP). The interaction of the defined geometricaly shaped protein adaptors with the AuNP induces the self-assembly of nanoarchitectures ranging from AuNP encapsulation to one-dimensional chain-like structures, complex networks and stars. Synthetic biology and bionanotechnology are applied to co-translationally encode unnatural amino acids as additional site-specific modification sites to generate functionalized biohybrid nanoarchitectures. This protein adaptor-based nanoobject assembly approach might be expanded to other inorganic nano-objects creating biohybrid materials with unique electronic, photonic, plasmonic and magnetic properties.

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“…Hcp1 is absolutely required for both the assembly of the type VI secretion apparatus and for the localization of ClpV1, a AAAϩ family protein that provides the energy for Hcp1 secretion (24). The proclivity for Hcp1 to form tail-like tubes in solution has been demonstrated by engineering a disulfide bond at the hexamer-hexamer interface observed in the crystal structure (26). Also, the accompanying article reports that a homologue of Hcp1 is able to form tubes spontaneously.…”

Section: Structural Similarity Between Gpvn and A Tail Tube Protein Fmentioning

confidence: 98%

The phage λ major tail protein structure reveals a common evolution for long-tailed phages and the type VI bacterial secretion system

Pell

Kanelis

Donaldson

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

258

276

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Most bacteriophages possess long tails, which serve as the conduit for genome delivery. We report the solution structure of the N-terminal domain of gpV, the protein comprising the major portion of the noncontractile phage tail tube. This structure is very similar to a previously solved tail tube protein from a contractile-tailed phage, providing the first direct evidence of an evolutionary connection between these 2 distinct types of phage tails. A remarkable structural similarity is also seen to Hcp1, a component of the bacterial type VI secretion system. The hexameric structure of Hcp1 and its ability to form long tubes are strikingly reminiscent of gpV when it is polymerized into a tail tube. These data coupled with other similarities between phage and type VI secretion proteins support an evolutionary relationship between these systems. Using Hcp1 as a model, we propose a polymerization mechanism for gpV involving several disorder-toorder transitions.NMR structure ͉ disordered regions ͉ macromolecular assembly

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In vitro self-assembly of tailorable nanotubes from a simple protein building block

Cited by 276 publications

References 31 publications

Evaluation of the roles played by Hcp and VgrG type 6 secretion system effectors in Aeromonas hydrophila SSU pathogenesis

Evaluation of the roles played by Hcp and VgrG type 6 secretion system effectors in Aeromonas hydrophila SSU pathogenesis

Molecular protein adaptor with genetically encoded interaction sites guiding the hierarchical assembly of plasmonically active nanoparticle architectures

The phage λ major tail protein structure reveals a common evolution for long-tailed phages and the type VI bacterial secretion system

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