<scp>P</scp>il<scp>T</scp>2 enhances the speed of gonococcal type <scp>IV</scp> pilus retraction and of twitching motility

Kurre, Rainer; Höne, Andrea; Clausen, Martin; Meel, Claudia; Maier, Berenike

doi:10.1111/mmi.12022

Cited by 25 publications

(35 citation statements)

References 29 publications

(60 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…That the retractile Tfp fibers of pilT L201C cells cannot stimulate the mechanosensitive EGFR pathway implies that Tfp retraction dynamics (force, speed, and/or frequency) modulate the host response to N. gonorrhoeae infection. In this context, it is also interesting to note that environmental cues influence Tfp retraction speed and force (25–27, 49, 50). Oxygen influences the retraction speed of a Tfp fiber (26).…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Attenuation of the Type IV Pilus Retraction Motor Influences Neisseria gonorrhoeae Social and Infection Behavior

Hockenberry

Hutchens

Agellon

et al. 2016

mBio

View full text Add to dashboard Cite

Retraction of the type IV pilus (Tfp) mediates DNA uptake, motility, and social and infection behavior in a wide variety of prokaryotes. To date, investigations into Tfp retraction-dependent activities have used a mutant deleted of PilT, the ATPase motor protein that causes the pilus fiber to retract. ΔpilT cells are nontransformable, nonmotile, and cannot aggregate into microcolonies. We tested the hypothesis that these retraction-dependent activities are sensitive to the strength of PilT enzymatic activity by using the pathogen Neisseria gonorrhoeae as a model. We constructed an N. gonorrhoeae mutant with an amino acid substitution in the PilT Walker B box (a substitution of cysteine for leucine at position 201, encoded by pilTL201C). Purified PilTL201C forms a native hexamer, but mutant hexamers hydrolyze ATP at half the maximal rate. N. gonorrhoeae pilTL201C cells produce Tfp fibers, crawl at the same speed as the wild-type (wt) parent, and are equally transformable. However, the social behavior of pilTL201C cells is intermediate between the behaviors of wt and ΔpilT cells. The infection behavior of pilTL201C is also defective, due to its failure to activate the epidermal growth factor receptor (EGFR)-heparin-binding EGF-like growth factor (HB-EGF) pathway. Our study indicates that pilus retraction, per se, is not sufficient for N. gonorrhoeae microcolony formation or infectivity; rather, these activities are sensitive to the strength of PilT enzymatic activity. We discuss the implications of these findings for Neisseria pathogenesis in the context of mechanobiology.

show abstract

Section: Discussionmentioning

confidence: 99%

“…The cultures were incubated at 37°C, 5% CO 2 for 1 h to allow bacteria to settle and then measured for motility as described previously (27). Fifty individual bacteria were analyzed, each for 30 s per time point.…”

Section: Methodsmentioning

confidence: 99%

Attenuation of the Type IV Pilus Retraction Motor Influences Neisseria gonorrhoeae Social and Infection Behavior

Hockenberry

Hutchens

Agellon

et al. 2016

mBio

View full text Add to dashboard Cite

show abstract

“…A second PilT-like traffic NTPase gene, TTC1415, not associated with the pilF locus, is present in the T. thermophilus genome (29). The deduced protein is 46% identical to PilT2 from N. gonorrhoeae (46). Therefore, TTC1415 was designated PilT2.…”

Section: Resultsmentioning

confidence: 99%

Type IV Pilus Biogenesis, Twitching Motility, and DNA Uptake in Thermus thermophilus: Discrete Roles of Antagonistic ATPases PilF, PilT1, and PilT2

Salzer

Joos

Averhoff

2014

Appl Environ Microbiol

View full text Add to dashboard Cite

Natural transformation has a large impact on lateral gene flow and has contributed significantly to the ecological diversification and adaptation of bacterial species. Thermus thermophilus HB27 has emerged as the leading model organism for studies of DNA transporters in thermophilic bacteria. Recently, we identified a zinc-binding polymerization nucleoside triphosphatase (NTPase), PilF, which is essential for the transport of DNA through the outer membrane. Here, we present genetic evidence that PilF is also essential for the biogenesis of pili. One of the most challenging questions was whether T. thermophilus has any depolymerization NTPase acting as a counterplayer of PilF. We identified two depolymerization NTPases, PilT1 (TTC1621) and PilT2 (TTC1415), both of which are required for type IV pilus (T4P)-mediated twitching motility and adhesion but dispensable for natural transformation. This suggests that T4P dynamics are not required for natural transformation. The latter finding is consistent with our suggestion that in T. thermophilus, T4P and natural transformation are linked but distinct systems.

show abstract

“…Disassembly of T4P with retraction occurs when PilF is replaced by the hexameric ATPase PilT (7,16). PilU, a PilT paralog, is involved in retraction to a lesser extent (17). The alignment complex consisting of PilM, PilN, PilO, and PilP is proposed to connect the IM motor complex and the OM pore complex, and it is also thought to be involved in the stability and/or gating of the OM complex (18)(19)(20).…”

mentioning

confidence: 99%

Peptidoglycan-binding protein TsaP functions in surface assembly of type IV pili

Siewering

Jain

Friedrich

et al. 2014

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

View full text Add to dashboard Cite

Type IV pili (T4P) are ubiquitous and versatile bacterial cell surface structures involved in adhesion to host cells, biofilm formation, motility, and DNA uptake. In Gram-negative bacteria, T4P pass the outer membrane (OM) through the large, oligomeric, ring-shaped secretin complex. In the β-proteobacterium Neisseria gonorrhoeae, the native PilQ secretin ring embedded in OM sheets is surrounded by an additional peripheral structure, consisting of a peripheral ring and seven extending spikes. To unravel proteins important for formation of this additional structure, we identified proteins that are present with PilQ in the OM. One such protein, which we name T4P secretin-associated protein (TsaP), was identified as a phylogenetically widely conserved component of the secretin complex that co-occurs with genes for T4P in Gram-negative bacteria. TsaP contains an N-terminal carbohydrate-binding lysin motif (LysM) domain and a C-terminal domain of unknown function. In N. gonorrhoeae, lack of TsaP results in the formation of membrane protrusions containing multiple T4P, concomitant with reduced formation of surface-exposed T4P. Lack of TsaP did not affect the oligomeric state of PilQ, but resulted in loss of the peripheral structure around the PilQ secretin. TsaP binds peptidoglycan and associates strongly with the OM in a PilQ-dependent manner. In the δ-proteobacterium Myxococcus xanthus, TsaP is also important for surface assembly of T4P, and it accumulates and localizes in a PilQ-dependent manner to the cell poles. Our results show that TsaP is a novel protein associated with T4P function and suggest that TsaP functions to anchor the secretin complex to the peptidoglycan.

show abstract

PilT2 enhances the speed of gonococcal type IV pilus retraction and of twitching motility

Cited by 25 publications

References 29 publications

Attenuation of the Type IV Pilus Retraction Motor Influences Neisseria gonorrhoeae Social and Infection Behavior

Attenuation of the Type IV Pilus Retraction Motor Influences Neisseria gonorrhoeae Social and Infection Behavior

Type IV Pilus Biogenesis, Twitching Motility, and DNA Uptake in Thermus thermophilus: Discrete Roles of Antagonistic ATPases PilF, PilT1, and PilT2

Peptidoglycan-binding protein TsaP functions in surface assembly of type IV pili

Contact Info

Product

Resources

About