2023
DOI: 10.1172/jci166710
|View full text |Cite
|
Sign up to set email alerts
|

BosR and PlzA reciprocally regulate RpoS function to sustain Borrelia burgdorferi in ticks and mammals

Abstract: The alternative sigma factor RpoS in Borrelia burgdorferi (Bb), the Lyme disease pathogen, is responsible for programmatic positive and negative gene regulation essential for the spirochete's dual-host enzootic cycle. RpoS is expressed during tick-to-mammal transmission and throughout mammalian infection.Although the mammalian-phase RpoS regulon is well described, its counterpart during the transmission blood meal is unknown. Here, we used Bb-specific transcript enrichment by TBDCapSeq to compare the transcrip… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
3
1
1

Citation Types

1
16
1

Year Published

2023
2023
2024
2024

Publication Types

Select...
5
1

Relationship

0
6

Authors

Journals

citations
Cited by 19 publications
(32 citation statements)
references
References 106 publications
(220 reference statements)
1
16
1
Order By: Relevance
“…During vertebrate infection, no c-di-GMP is produced, favoring apo-PlzA functions such as RNA chaperone activity (Van Gundy et al ., 2023). When c-di-GMP is present, holo-PlzA can also anneal RNAs and potentially interact with RNAP (Grassmann et al ., 2023; Van Gundy et al ., 2023). At lower levels of c-di-GMP, PlzA nucleic-acid binding affinity is low for certain target genes such as glpFKD .…”
Section: Discussionmentioning
confidence: 99%
See 3 more Smart Citations
“…During vertebrate infection, no c-di-GMP is produced, favoring apo-PlzA functions such as RNA chaperone activity (Van Gundy et al ., 2023). When c-di-GMP is present, holo-PlzA can also anneal RNAs and potentially interact with RNAP (Grassmann et al ., 2023; Van Gundy et al ., 2023). At lower levels of c-di-GMP, PlzA nucleic-acid binding affinity is low for certain target genes such as glpFKD .…”
Section: Discussionmentioning
confidence: 99%
“…Mutation of plzA has been implicated in many B. burgdorferi phenotypes, including mis-regulation of alternative carbohydrate utilization, decreased motility, and virulence defects (Pitzer et al ., 2011; He et al ., 2014; Mallory et al ., 2016; Zhang et al ., 2018; Groshong et al ., 2021). Binding of c-di-GMP induces conformational changes in PlzA structure, which has led to the hypothesis that c-di-GMP binding acts as a switching mechanism providing the holo and apo-forms of PlzA with distinct functions (Mallory et al ., 2016; Groshong et al ., 2021; Grassmann et al ., 2023). Specifically, c-di-GMP bound PlzA is thought to regulate genes required for survival in the tick host, while apo-PlzA is speculated to play a role in regulation during vertebrate infection (Groshong et al ., 2021; Grassmann et al ., 2023).…”
Section: Introductionmentioning
confidence: 99%
See 2 more Smart Citations
“…citri [94, 95]. While the C-terminal domain binds cyclic di-GMP, the N-terminal domain of PlzA, a tandem xPilZ-PilZ domain protein of the Lyme disease spirochete Borrelia burgdorferi , has been shown to be involved in DNA and RNA binding [96, 97]. In tandem xPilZ-PilZ domain proteins, such as in the flagellar motor break protein YcgR, the non-canonical xPilZ domain is often highly degraded giving rise to novel domain subclasses (Table 1; [98]).…”
Section: Variability Of Cyclic Di-gmp Binding In Receptor Familiesmentioning
confidence: 99%