Insights into the mechanism regulating the differential expression of the P28-OMP outer membrane proteins in obligatory intracellular pathogen Ehrlichia chaffeensis

Autor: Xiaohui Ma, Zhouyi Chai, Weihui Wu, Yingxing Feng, Fang Bai, Heting Cui, Zhihui Cheng, Zhexuan Wang, Yongxin Jin, Xiaoxiao Li, Yu Cao, Nan Duan, Yasuko Rikihisa, Jiaqi Yan
Jazyk: angličtina
Rok vydání: 2021
Předmět:
0301 basic medicine
Ehrlichiosis
Hot Temperature
Epidemiology
THP-1 Cells
030106 microbiology
Immunology
Biology
Microbiology
Tr1
Intracellular pathogen
03 medical and health sciences
Ticks
Bacterial Proteins
Species Specificity
Virology
parasitic diseases
Drug Discovery
Consensus Sequence
medicine
Escherichia coli
Ehrlichia chaffeensis
Animals
Humans
Differential expression
differential gene expression
Promoter Regions
Genetic

Mechanism (biology)
General Medicine
P28-OMP outer membrane proteins
Gene Expression Regulation
Bacterial

medicine.disease
biology.organism_classification
bacterial infections and mycoses
human monocytic ehrlichiosis
030104 developmental biology
Infectious Diseases
Parasitology
Bacterial outer membrane
Research Article
Bacterial Outer Membrane Proteins
Transcription Factors
Zdroj: Emerging Microbes & Infections
article-version (VoR) Version of Record
ISSN: 2222-1751
Popis: Ehrlichia chaffeensis causes human monocytic ehrlichiosis (HME), which is one of the most prevalent, life-threatening emerging infectious zoonoses. The life cycle of E. chaffeensis includes ticks and mammals, in which E. chaffeensis proteins are expressed differentially contributing to bacterial survival and infection. Among the E. chaffeensis P28-OMP outer membrane proteins, OMP-1B and P28 are predominantly expressed in tick cells and mammalian macrophages, respectively. The mechanisms regulating this differential expression have not been comprehensively studied. Here, we demonstrate that the transcriptional regulators EcxR and Tr1 regulate the differential expression of omp-1B and p28 in E. chaffeensis. Recombinant E. chaffeensis Tr1 bound to the promoters of omp-1B and p28, and transactivated omp-1B and p28 promoter-EGFP fusion constructs in Escherichia coli. The consensus sequence of Tr1 binding motifs was AC/TTATA as determined with DNase I footprint assay. Tr1 showed a higher affinity towards the p28 promoter than the omp-1B promoter as determined with surface plasmon resonance. EcxR activated the tr1 expression in response to a temperature decrease. At 37°C low level of Tr1 activated the p28 expression. At 25°C high level of Tr1 activated the omp-1B expression, while repressing the p28 expression by binding to an additional site upstream of the p28 gene. Our data provide insights into a novel mechanism mediated by Tr1 regulating E. chaffeensis differential gene expression, which may aid in the development of new therapeutics for HME.
Databáze: OpenAIRE