Type IV pili: dynamics, biophysics and functional consequences

Craig, Lisa; Forest, Katrina T.; Maier, Berenike

doi:10.1038/s41579-019-0195-4

Cited by 314 publications

(319 citation statements)

References 120 publications

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“…Many bacterial strains display surface pili, which are long (1–5 μM), fiber‐like appendages. In Gram‐negative organisms, these include the Type IV and chaperone‐usher pili . Type IV pili (T4P) are highly dynamic, and possess the remarkable ability to quickly extend and retract repeatedly.…”

Section: Assembly Of T4ps Secretinsmentioning

confidence: 99%

“…T4PS assembly is coordinated by a complex machinery that encompasses both inner and outer bacterial membranes, and the pilus itself is formed by polymerized pilin subunits arranged helically . The core T4PS machinery includes four main components: an ATPase, located at the base of the system and which provides energy for pilus extension; an IM platform; the pilus filament itself; and an outer membrane secretin . T4PS pilins are synthesized as prepilins in the cytoplasm and translocated toward the periplasmic side of the IM by the Sec system, as is the case of T2SS pseudopilins .…”

Section: Assembly Of T4ps Secretinsmentioning

confidence: 99%

“…In Gram-negative organisms, these include the Type IV and chaperone-usher pili. 93 Type IV pili (T4P) are highly dynamic, and possess the remarkable ability to quickly extend and retract repeatedly. This ability is crucial for multiple functions, including adherence, motility, DNA uptake, and protein secretion.…”

Section: Assembly Of T4ps Secretinsmentioning

confidence: 99%

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Bacterial secretins: Mechanisms of assembly and membrane targeting

et al. 2020

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Secretion systems are employed by bacteria to transport macromolecules across membranes without compromising their integrities. Processes including virulence, colonization, and motility are highly dependent on the secretion of effector molecules toward the immediate cellular environment, and in some cases, into the host cytoplasm. In Type II and Type III secretion systems, as well as in Type IV pili, homomultimeric complexes known as secretins form large pores in the outer bacterial membrane, and the localization and assembly of such 1 MDa molecules often relies on pilotins or accessory proteins. Significant progress has been made toward understanding details of interactions between secretins and their partner proteins using approaches ranging from bacterial genetics to cryo electron microscopy. This review provides an overview of the mode of action of pilotins and accessory proteins for T2SS, T3SS, and T4PS secretins, highlighting recent near‐atomic resolution cryo‐EM secretin complex structures and underlining the importance of these interactions for secretin functionality.

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Section: Assembly Of T4ps Secretinsmentioning

confidence: 99%

Section: Assembly Of T4ps Secretinsmentioning

confidence: 99%

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Bacterial secretins: Mechanisms of assembly and membrane targeting

et al. 2020

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“…In many species, Tfp retraction also controls important properties of bacterial aggregates/microcolonies, including local order, viscosity and shape (Craig, Forest, & Maier, ; Welker et al, ). Microcolonies formed by N. meningitidis or N. gonorrhoeae display a heterogeneous motility behaviour, bacteria close to the microcolony surface exhibiting higher motility than those located in the centre.…”

Section: Role Of Type IV Pili In Meningococcal Pathogenesismentioning

confidence: 99%

Meningococcal disease: A paradigm of type‐IV pilus dependent pathogenesis

Souza

Maïssa

Ziveri

et al. 2020

Cellular Microbiology

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Neisseria meningitidis (meningococcus) is a Gram‐negative bacterium responsible for two devastating forms of invasive diseases: purpura fulminans and meningitis. Interaction with both peripheral and cerebral microvascular endothelial cells is at the heart of meningococcal pathogenesis. During the last two decades, an essential role for meningococcal type IV pili in vascular colonisation and disease progression has been unravelled. This review summarises 20 years of research on meningococcal type IV pilus‐dependent virulence mechanisms, up to the identification of promising anti‐virulence compounds that target type IV pili.

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“…Systematic mutagenesis studies have shown that filament biogenesis requires 15‐17 proteins (Pelicic, ): a pilin, several minor (low abundance) pilins (four in N. meningitidis , five in P. aeruginosa ), a prepilin peptidase, a platform protein, an extension ATPase, an assembly sub‐complex (PilM, PilN and PilO), a secretin pore (PilQ) in the outer membrane (OM), a linker (PilP) between the assembly sub‐complex and secretin, an OM lipoprotein stabilising PilQ (PilW in N. meningitidis ) and an OM protein involved in the late stages of Tfp biogenesis (PilC1/PilC2 in N. meningitidis ). Filament retraction is powered by PilT, which is dispensable for piliation (Craig et al , ). In S. sanguinis , the only monoderm in which a systematic genetic analysis of piliation has been performed, filament biogenesis relies on a very similar machinery, even more than we previously appreciated (Gurung et al , ).…”

Section: Tfp Biogenesis Machineries In Monoderm Bacteria: the Beauty mentioning

confidence: 99%

Monoderm bacteria: the new frontier for type IV pilus biology

Pelicic

2019

Molecular Microbiology

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Summary In the diverse world of bacterial pili, type IV pili (Tfp) are unique for two reasons: their multifunctionality and ubiquity. This latter feature offers an extraordinary possibility, that is, to perform comparative studies in evolutionarily distant species in order to improve our fragmentary understanding of Tfp biology. Regrettably, such potential has remained largely untapped, because, for 20 years, Tfp have only been characterised in diderm bacteria. However, recent studies of Tfp in monoderms have started closing the gap, revealing many interesting commonalities and a few significant differences, extending the frontiers of knowledge of Tfp biology. Here, I review the current state of the art of the Tfp field in monoderm bacteria and discuss resulting implications for our general understanding of the assembly and function of these widespread filamentous nanomachines.

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Type IV pili: dynamics, biophysics and functional consequences

Cited by 314 publications

References 120 publications

Bacterial secretins: Mechanisms of assembly and membrane targeting

Bacterial secretins: Mechanisms of assembly and membrane targeting

Meningococcal disease: A paradigm of type‐IV pilus dependent pathogenesis

Monoderm bacteria: the new frontier for type IV pilus biology

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