Abstract

In order to persist, bacteria need to adjust their physiological state in response to external and internal cues. External stimuli are often referred to as stressors. The stringent response, mediated by the alarmone (p)ppGpp, is central to the stress response in many bacteria; yet, there is limited knowledge regarding the role of (p)ppGpp signaling in bacteria belonging to the phylum Bacteroidetes. Like its counterparts in the gut (e.g., Bacteroides thetaiotaomicron and Bacteroides fragilis), Porphyromonas gingivalis persists in close association with its human host. Given the potential for numerous perturbations in the oral cavity, and the fact that P. gingivalis can enter and replicate within host cells, we hypothesized that (p)ppGpp is a key signaling molecule for stress adaptation and persistence. Here, we show that accumulation of ppGpp in P. gingivalis is governed by two homologous enzymes, designated Rel, and RshB, and that ppGpp signaling affects growth rate, survival, biofilm formation, production of outer membrane vesicles, and expression of genes encoding type IX secretion structural and cargo proteins. Overall, our findings provide a potential mechanism by which biofilm formation and virulence of P. gingivalis are integrated via ppGpp signaling, a regulatory mechanism central to bacterial survival in dynamic environments.

Highlights

  • Since ppGpp and ppGpp; guanosine pentaphosphate (pppGpp) accumulate in Enterococcus faecalis in the presence of mupirocin,[37] cells of E. faecalis were used as a positive control of ppGpp and pppGpp

  • The ppGpp profiles of Δrel and ΔrshB mutants revealed that RshB is the major enzyme responsible for the accumulation of ppGpp, while Rel appears to be responsible for maintaining basal levels under these growth conditions

  • Having determined that deletion of rel or rshB affects the levels of ppGpp in P. gingivalis, we evaluated the impact of a lack of ppGpp synthesis and hydrolysis on bacterial growth rate and viability

Read more

Summary

Introduction

The type IX secretion system (T9SS), which is restricted to the phylum Bacteroidetes, is a complex translocon that accomplishes the secretion of over 30 P. gingivalis proteins bearing a specific Cterminal domain, including the trypsin-like gingipains, which are key virulence determinants.[9] Another key secretion mechanism exploited by P. gingivalis is production of outer membrane vesicles (OMVs). P. gingivalis is highly proficient in OMV production, and not surprisingly, these secreted vesicles are decorated with T9SS cargo proteins, providing an effective means to promote the spread of proteolytic enzymes into the surroundings for nutrient acquisition, as well as the spread of virulence determinants.[10,11]

Methods
Results
Conclusion
Full Text
Published version (Free)

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call