Structure of the Bacterial Sex F Pilus Reveals an Assembly of a Stoichiometric Protein-Phospholipid Complex

Costa, Tiago; Ilangovan, Aravindan; Ukleja, Marta; Redzej, Adam; Santini, Joanne M.; Smith, Terry; Waksman, Gabriel

doi:10.1016/j.cell.2016.08.025

Cited by 124 publications

(176 citation statements)

References 40 publications

(44 reference statements)

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“…Extending from the core complex outside of the cell is an appendage called a pilus, which is a polymer of VirB2 and is essential for making the connection between the recipient and donor cells. Recent high‐resolution cryo EM structure of the pilus isolated from the F‐like plasmid shows that the inside of the pilus is covered with lipid head groups, which might facilitate the transfer of the DNA between cells (Costa et al , 2016; Hospenthal et al , 2017). …”

Section: Introductionmentioning

confidence: 99%

Structure of a VirD4 coupling protein bound to a VirB type IV secretion machinery

et al. 2017

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Type IV secretion (T4S) systems are versatile bacterial secretion systems mediating transport of protein and/or DNA. T4S systems are generally composed of 11 VirB proteins and 1 VirD protein (VirD4). The VirB1‐11 proteins assemble to form a secretion machinery and a pilus while the VirD4 protein is responsible for substrate recruitment. The structure of VirD4 in isolation is known; however, its structure bound to the VirB1‐11 apparatus has not been determined. Here, we purify a T4S system with VirD4 bound, define the biochemical requirements for complex formation and describe the protein–protein interaction network in which VirD4 is involved. We also solve the structure of this complex by negative stain electron microscopy, demonstrating that two copies of VirD4 dimers locate on both sides of the apparatus, in between the VirB4 ATPases. Given the central role of VirD4 in type IV secretion, our study provides mechanistic insights on a process that mediates the dangerous spread of antibiotic resistance genes among bacterial populations.

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Section: Introductionmentioning

confidence: 99%

Structure of a VirD4 coupling protein bound to a VirB type IV secretion machinery

et al. 2017

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“…The loop between α2 and α3 projects towards the lumen of the pilus whilst both Nand C-termini are located on the outside of the helical polymer 101 (for more details see FIG. 3c).…”

Section: Structure Of the Traa Pilinmentioning

confidence: 99%

“…The recent cryo-EM structures of two members of the F pilus family (F and pED208) allowed the atomic model of TraA to be built de novo in the context of a fully assembled pilus 101 . The electron density of the TraA pilin structure encoded by the pED208 plasmid revealed an all α-helical structure, containing three α-helices (α1-3).…”

Section: Structure Of the Traa Pilinmentioning

confidence: 99%

A comprehensive guide to pilus biogenesis in Gram-negative bacteria

2017

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Pili are critical virulence factors of many Gram-negative pathogens. These surface structures provide bacteria with a link to their outside environments, allowing bacteria to interact with their hosts, other surfaces or with each other. They can even provide a conduit for the exchange of information. The surface chemistries and other biophysical properties of pili are uniquely adapted to the environmental challenges faced by bacteria. The assembly of these surface structures presents a molecular engineering challenge, which bacteria have solved in a variety of unique ways. In this review, we examine recent advances in our structural understanding of various Gram-negative pilus systems and discuss their functional implications.

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“…During the classical conjugation process in Gram-negative bacteria, plasmid DNA travels through a type IV secretion system (T4SS) between donor and recipient bacteria (58,59). Conjugative plasmids carry all the genetic information required to synthetize the T4SS and the proteins needed to escort plasmid DNA to the new host (3).…”

Section: Conjugationmentioning

confidence: 99%

Fitness Costs of Plasmids: a Limit to Plasmid Transmission

2017

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Plasmids mediate the horizontal transmission of genetic information between bacteria, facilitating their adaptation to multiple environmental conditions. An especially important example of the ability of plasmids to catalyze bacterial adaptation and evolution is their instrumental role in the global spread of antibiotic resistance, which constitutes a major threat to public health. Plasmids provide bacteria with new adaptive tools, but they also entail a metabolic burden that, in the absence of selection for plasmid-encoded traits, reduces the competitiveness of the plasmid-carrying clone. Although this fitness reduction can be alleviated over time through compensatory evolution, the initial cost associated with plasmid carriage is the main constraint on the vertical and horizontal replication of these genetic elements. The fitness effects of plasmids therefore have a crucial influence on their ability to associate with new bacterial hosts and consequently on the evolution of plasmid-mediated antibiotic resistance. However, the molecular mechanisms underlying plasmid fitness cost remain poorly understood. Here, we analyze the literature in the field and examine the potential fitness effects produced by plasmids throughout their life cycle in the host bacterium. We also explore the various mechanisms evolved by plasmids and bacteria to minimize the cost entailed by these mobile genetic elements. Finally, we discuss potential future research directions in the field.

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Structure of the Bacterial Sex F Pilus Reveals an Assembly of a Stoichiometric Protein-Phospholipid Complex

Cited by 124 publications

References 40 publications

Structure of a VirD4 coupling protein bound to a VirB type IV secretion machinery

Structure of a VirD4 coupling protein bound to a VirB type IV secretion machinery

A comprehensive guide to pilus biogenesis in Gram-negative bacteria

Fitness Costs of Plasmids: a Limit to Plasmid Transmission

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