Bacterial motility: machinery and mechanisms

Nature Reviews Microbiology, Год журнала: 2021, Номер 20(3), С. 161 - 173

Опубликована: Сен. 21, 2021

Язык: Английский

---

Bridging Bacteria and the Gut: Functional Aspects of Type IV Pili

Trends in Microbiology, Год журнала: 2020, Номер 28(5), С. 340 - 348

Опубликована: Март 5, 2020

Pili are key interaction molecules in the context of gut microbiota.Type IV pili (T4P) ubiquitous bacteria and great functional importance.About 30%, potentially even up to 45%, microbiota members thought express T4P, illustrating their importance microbiota–host interactions.Functions diverse include (but not limited to): adhesion, biofilm formation, motility, molecule exchange [e.g., double stranded (ds)DNA proteins].T4P found all monoderm diderm Archaea. Cell-surface-located proteinaceous appendages, such as flagella fimbriae or pili, bacterial communities. Here, we focus on conserved type produced by intestinal tract, one most densely populated human ecosystems. Computational analysis revealed that approximately 30% known predicted produce T4P. To rationalize how T4P allow interact with environment, other members, host cells, review established role commensals pathogens respect adherence, well protein secretion DNA uptake. This work indicates widely spread among contribution health might be underestimated. Microbial interactions essential for growth survival. These microbes abiotic environment including microbes, viruses, eukaryotic cells. In many cases these promoted cell-surface-located structures form protruding (see Glossary). hair-like appendages offer a wide range adaptations. Especially gut, which is colonized large communities, can crucial adhesion cells molecules. The an extremely versatile characterized constant turnover flow result food intake, mucin renewal, epithelial cell turnover, peristalsis [1.Tytgat H.L.P. et al.Bowel biofilms: tipping points between healthy compromised gut?.Trends Microbiol. 2019; 27: 17-25Abstract Full Text PDF PubMed Scopus (42) Google Scholar]. Previous deep metagenomic analyses have identified I major factor enhancing survival persistence low-abundant species [2.Arumugam M. al.Enterotypes microbiome.Nature. 2011; 473: 174-180Crossref (3679) While microscopic observations were used initial identification, presently classified based structure mode biogenesis. since they spread, functionally diverse, share similar genetic organization, composition (Box 1), biogenesis 2) [3.Denise R. al.Diversification filament superfamily into machines secretion, uptake, motility.PLoS Biol. 17e3000390Crossref (33) involved (Figure 1, Key Figure). Like surface also exploited bacteriophages use receptors [4.Bradley D.E. Pitt T.L. Pilus-dependence four Pseudomonas aeruginosa non-contractile tails.J. Gen. Virol. 1974; 24: 1-15Crossref (55) typically 5–8 nanometers diameter several micrometers length, exceeding size [5.Craig L. al.Type pilus pathogenicity.Nat. Rev. 2004; 2: 363-378Crossref (525) Scholar].Box 1T4P ArchitectureThe striking structural feature pilus, primarily consists pilin subunits. subunit called PilA model organism P. aeruginosa, TcpA BfpA resp. V. cholerae E. coli. [52.Giltner C.L. proteins: molecular modules.Microbiol. Mol. 2012; 76: 740-772Crossref (236) pilins synthesized prepilins targeted membrane αN-terminal sequence motif, class III signal peptide. positively charged peptide ensures proper orientation inner [53.Craig cryo-electron microscopy crystallography: implications assembly functions.Mol. Cell. 2006; 23: 651-662Abstract (299) Once membrane, prepilin peptidase PilD cleaves off this leader methylates [54.Strom M.S. al.A single bifunctional enzyme, PilD, catalyzes cleavage N-methylation proteins belonging family.Proc. Natl. Acad. Sci. U. S. A. 1993; 90: 2404-2408Crossref (216) After this, incorporated growing T4aP T4bP distinct, peptides being less than ten amino acid residues length mature ranging 140 160 [9.Strom Lory Structure–function pili.Annu. 47: 565-596Crossref (398) T4bP, longer, namely 15–30 acids, precede larger 180–200 thus mainly built but further decorated minor pilins. expressing T4aP, group pilins, PilV, PilW, PilX, FimU, PilE, priming complex [55.Nguyen Y. al.Pseudomonas prime IVa promote display PilY1 adhesin.J. Chem. 2015; 290: 601-611Crossref (56) Prepilin shown process similarly PilA, cleaving methylating [56.Giltner pili.J. 2010; 398: 444-461Crossref (97) short stem reduces energy barrier extension both at tip throughout Finally, complexes accommodate additional adhesins confer extra specificity functionality – example, ComP Neisseria binds [57.Cehovin al.Specific recognition mediated pilin.Proc. 2013; 110: 3065-3070Crossref (91) Scholar], PilY1, aids An overview given Box 2.Box 2Biogenesis T4PBiogenesis strongly conserved, them harbor genes, related T2SS [44.Ayers al.Architecture II machineries.Future 5: 1203-1218Crossref (90) first step attachment ATPase, PilB (yellow, Figure I), cytoplasmic ring formed PilM (blue) platform PilC (green) [58.Chang Y.-W. machine.Science. 2016; 351aad2001Crossref (182) Scholar] I). ring, PilM, forms together subunits PilN (light gray), PilO (dark PilP (orange), alignment PilMNOP Attachment causes conformational changes PilO, resulting cage-like periplasm Scholar,59.McCallum al.The dynamic pilus.Microbiol. Spectr. 7: 1-12Crossref (14) allows (black) enter complex, enabling [60.Leighton al.Novel PilNO retraction subcomplex mutations.J. Bacteriol. 197: 2229-2238Crossref (21) ATPase attached PilC, incorporation elongating [61.Takhar H.K. biogenesis.J. 288: 9721-9728Crossref (67) Minor fashion (cf. 1). They mostly tip, along Gram-negative bacteria, needs outer pore facilitate transfer through during (de-)polymerization [62.Tammam al.PilMNOPQ from system transenvelope network interacts PilA.J. 195: 2126-2135Crossref (65) PilQ (red) linked has two internal gates, secretin gate periplasmic gate, closed absence prevent leakage [63.Gold V.A.M. al.Structure machinery open state.eLife. 4: (66) Obviously, absent Gram-positive where directly sticking out peptidoglycan layer. fully assembled, attach surface, inducing tension pilus. PilT (brown) responsible retraction. released allowing after back I) [14.Wolfgang al.PilT mutations lead simultaneous defects competence natural transformation twitching motility piliated gonorrhoeae.Mol. 1998; 29: 321-330Crossref (256) occurs independently [17.Anantha R.P. al.Role BfpF, member family putative nucleotide-binding proteins, enteropathogenic Escherichia coli cells.Infect. Immun. 66: 122-131Crossref Scholar,18.Ng D. Vibrio TcpB initiates toxin-coregulated pilus.PLoS Pathog. 12e1006109Crossref (30) Scholar].Figure 1Key Figure. Various Functions Type Gut-Related Species.Show full captionT4P-carrying indicated cartoon bacillus covered throughout; however, only potential manifestations abundant may polarly localized. roles interactions, commensal pathogenic bacteria. One motility: move around attaching it finally pulling themselves forward sometimes help (tip) adherence surfaces ultimately formation. play bacterium its environment: bind subsequently take secrete proteins. latter process, pushes manner piston. It will exciting see if dedicated studies uncover general, specific gut. Abbreviation: IEC, cell.View Large Image ViewerDownload Hi-res image Download (PPT) 2. Biogenesis T4P-carrying cell. distributed gonorrhoeae, cholerae, Clostridium sp., Archaea [6.Hospenthal M.K. comprehensive guide bacteria.Nat. 2017; 15: 365-379Crossref (114) Scholar, 7.Danne C. Dramsi bacteria: colonization.Res. 163: 645-658Crossref (78) 8.Pohlschroder Esquivel R.N. Archaeal involvement formation.Front. 6: 190Crossref (37) Bacterial divided subtypes, (T4aP), IVb (T4bP), Tad recently been designated IVc (T4cP) Scholar,9.Strom assembled using mechanisms 2). presence generate mechanical forces (nanoNewton range) [10.Biais N. al.Cooperative bundled enables nanonewton force generation.PLoS 2008; 6e87Crossref (103) [11.Berry J.-L. Pelicic Exceptionally widespread nanomachines composed pilins: prokaryotic Swiss Army knives.FEMS 39: 134-154Crossref (124) However, retract [12.Ellison C.K. al.Retraction DNA-bound uptake cholerae.Nat. 2018; 3: 773-780Crossref (94) studied detail [13.Bradley A function PAO polar pili: motility.Can. J. 1980; 26: 146-154Crossref (232) gonorrhoeae prevalent uniform, (EPEC) [15.Sohel I. al.Enteropathogenic coli: identification gene cluster coding bundle-forming morphogenesis.J. 1996; 178: 2613-2628Crossref [toxin coregulated (TCP)] [16.Sun al.Domains within toxin mediate colonization.Gene. 1997; 192: 79-85Crossref (29) amongst others. lack PilT, another BfpF EPEC different mechanism entirely, TCP triggered leading spontaneous disassembly [18.Ng Tight-adherence (Tad) smaller encoded locus. considered subclass recent phylogenetic showed distinct clade, T4cP Scholar,19.Ellison al.Obstruction stimulates sensing.Science. 358: 535-538Crossref (105) takes place PilT. For Caulobacter crescentus, was regulated CpaF, motor [20.Ellison drives tad retraction.Sci. Adv. 5eaay2591Crossref (11) Several omics cultivation efforts generated insights pres

Язык: Английский

---

Architecture, Function, and Substrates of the Type II Secretion System

EcoSal Plus, Год журнала: 2019, Номер 8(2)

Опубликована: Фев. 15, 2019

The type II secretion system (T2SS) delivers toxins and a range of hydrolytic enzymes, including proteases, lipases, carbohydrate-active to the cell surface or extracellular space Gram-negative bacteria. Its contribution survival both intracellular pathogens as well environmental species proteobacteria is evident. This dynamic, multicomponent machinery spans entire envelope consists cytoplasmic ATPase, several inner membrane proteins, periplasmic pseudopilus, secretin pore embedded in outer membrane. Despite trans -envelope configuration T2S nanomachine, proteins be secreted engage with first once they enter compartment via Sec TAT export system. Thus, T2SS specifically dedicated their translocation. many sequence structural similarities between IV pili suggest common origin argue for pilus-mediated mechanism secretion. minireview describes structures, functions, interactions individual components general architecture assembled briefly summarizes transport function growing list exoproteins. Recent advances cryo-electron microscopy, which have led an increased understanding structure-function relationship channel are emphasized.

Язык: Английский

---

The Rich Tapestry of Bacterial Protein Translocation Systems

The Protein Journal, Год журнала: 2019, Номер 38(4), С. 389 - 408

Опубликована: Авг. 12, 2019

Язык: Английский

---

Bacterial growth in multicellular aggregates leads to the emergence of complex life cycles

Current Biology, Год журнала: 2022, Номер 32(14), С. 3059 - 3069.e7

Опубликована: Июнь 30, 2022

Язык: Английский

---

CryoEM reveals the structure of an archaeal pilus involved in twitching motility

Nature Communications, Год журнала: 2024, Номер 15(1)

Опубликована: Июнь 14, 2024

Abstract Amongst the major types of archaeal filaments, several have been shown to closely resemble bacterial homologues Type IV pili (T4P). Within Sulfolobales , member species encode for three T4P, namely archaellum, UV-inducible pilus system (Ups) and adhesive (Aap). Whereas archaellum functions primarily in swimming motility, Ups UV-induced cell aggregation DNA-exchange, Aap plays an important role adhesion twitching motility. Here, we present a cryoEM structure model organism Sulfolobus acidocaldarius . We identify component subunit as AapB find that while its follows canonical T4P blueprint, it adopts distinct conformations within pilus. The tri-conformer describe challenges our current understanding sheds new light on principles

Язык: Английский

---

PilY1 regulates the dynamic architecture of the type IV pilus machine in Pseudomonas aeruginosa

Nature Communications, Год журнала: 2024, Номер 15(1)

Опубликована: Окт. 30, 2024

Язык: Английский

---

Tad and toxin-coregulated pilus structures reveal unexpected diversity in bacterial type IV pili

Proceedings of the National Academy of Sciences, Год журнала: 2023, Номер 120(49)

Опубликована: Ноя. 27, 2023

Type IV pili (T4P) are ubiquitous in both bacteria and archaea. They polymers of the major pilin protein, which has an extended protruding N-terminal helix, α1, a globular C-terminal domain. Cryo-EM structures have revealed key differences between bacterial archaeal T4P their domain structure packing continuity α1. This segment forms continuous α-helix but is partially melted all published due to conserved helix breaking proline at position 22. The tad (tight adhesion) found archaea thought been acquired by through horizontal transfer from Tad pilins unique among T4 pilins, being only 40 60 residues length entirely lacking also lack Pro22 high-resolution structures. We show using cryo-EM that pilus Caulobacter crescentus composed helical subunits that, like portion seen other share arrangement T4P. further T4P, Vibrio cholerae toxin coregulated pilus, lacks not family, α-helix, yet its α1 s arranged similar those Our results highlight role melting support evolutionary relationship

Язык: Английский

---

The type IV pilus protein PilU functions as a PilT-dependent retraction ATPase

PLoS Genetics, Год журнала: 2019, Номер 15(9), С. e1008393 - e1008393

Опубликована: Сен. 16, 2019

Type IV pili are dynamic cell surface appendages found throughout the bacteria. The ability of these structures to undergo repetitive cycles extension and retraction underpins their crucial roles in adhesion, motility natural competence for transformation. In best-studied systems a dedicated ATPase PilT powers pilus retraction. Curiously, second presumed PilU is often encoded immediately downstream pilT. However, despite presence two potential ATPases, pilT deletions lead total loss function, raising question why fails take over. Here, using DNA-uptake mannose-sensitive haemagglutinin (MSHA) Vibrio cholerae as model systems, we show that inactivated variants, defective either ATP-binding or hydrolysis, have unexpected intermediate phenotypes PilU-dependent. addition demonstrating can function bona fide ATPase, go on make surprising discovery functions exclusively PilT-dependent manner identify naturally occurring pandemic V. variant renders essential function. Finally, Pseudomonas aeruginosa also providing evidence functional coupling between could be widespread mechanism optimal

Язык: Английский

---

Computational prediction of secreted proteins in gram-negative bacteria

Computational and Structural Biotechnology Journal, Год журнала: 2021, Номер 19, С. 1806 - 1828

Опубликована: Янв. 1, 2021

Gram-negative bacteria harness multiple protein secretion systems and secrete a large proportion of the proteome. Proteins can be exported to periplasmic space, integrated into membrane, transported extracellular milieu, or translocated cytoplasm contacting cells. It is important for accurate, genome-wide annotation secreted proteins their pathways. In this review, we systematically classified according types in bacteria, summarized known features these proteins, reviewed algorithms tools prediction.

Язык: Английский

---