Interaction of Rickettsia felis with histone H2B facilitates the infection of a tick cell line

Thepparit, Chutima; Bourchookarn, Apichai; Petchampai, Natthida; Barker, Steven A.; Macaluso, Kevin R.

doi:10.1099/mic.0.041400-0

Cited by 23 publications

(20 citation statements)

References 48 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…A moonlighting function as an adhesin was reported for R . felis PrsA, which was shown to interact with tick histone H2B, a protein known to localize to the surface of eukaryotic cells (Thepparit et al ., 2010) . Despite identical gene sequences, electrophoretic PrsA variants are known across R .…”

Section: Secretory Proteins At the Host Interfacementioning

confidence: 99%

Secretome of obligate intracellularRickettsia

et al. 2014

View full text Add to dashboard Cite

The genus Rickettsia (Alphaproteobacteria; Rickettsiales; Rickettsiaceae) is comprised of obligate intracellular parasites, with virulent species of interest both as causes of emerging infectious diseases and for their potential deployment as bioterrorism agents. Currently there are no effective commercially available vaccines, with treatment limited primarily to tetracycline antibiotics, though others (e.g., josamycin, ciprofloxacin, chloramphenicol and azithromycin) are also effective. Much of the recent research geared towards understanding mechanisms underlying rickettsial pathogenicity has centered on characterization of secreted proteins that directly engage eukaryotic cells. Herein, we review all aspects of the Rickettsia secretome, including six secretion systems, 19 characterized secretory proteins, and potential moonlighting proteins identified on surfaces of multiple Rickettsia species. Employing bioinformatics and phylogenomics, we present novel structural and functional insight on each secretion system. Unexpectedly, our investigation revealed that the majority of characterized secretory proteins have not been assigned to their cognate secretion pathways. Furthermore, for most secretion pathways, the requisite signal sequences mediating translocation are poorly understood. As a blueprint for all known routes of protein translocation into host cells, this resource will assist research aimed at uniting characterized secreted proteins with their apposite secretion pathways. Furthermore, our work will help in the identification of novel secreted proteins involved in rickettsial “life on the inside”.

show abstract

Section: Secretory Proteins At the Host Interfacementioning

confidence: 99%

Secretome of obligate intracellularRickettsia

et al. 2014

View full text Add to dashboard Cite

show abstract

“…It is recognized that rickettsiae enter host cells through receptor-mediated endocytosis [13]–[14]. Tick-derived histone H2B was demonstrated to play a role in tick cell infection by a non-SFG species, R. felis , in a tick-derived cell line [15], corroborating findings of a role for nuclear proteins in SFG Rickettsia mammalian cell invasion [16]. More recently, dysregulation of tick-derived α-catenin [17] and vacuolar-ATPase [18] were associated with rickettsial infection of tick-derived cell lines and whole organs.…”

Section: Introductionmentioning

confidence: 99%

Novel Identification of Dermacentor variabilis Arp2/3 Complex and Its Role in Rickettsial Infection of the Arthropod Vector

et al. 2014

Self Cite

View full text Add to dashboard Cite

Tick-borne spotted fever group (SFG) Rickettsia species must be able to infect both vertebrate and arthropod host cells. The host actin-related protein 2/3 (Arp2/3) complex is important in the invasion process and actin-based motility for several intracellular bacteria, including SFG Rickettsia in Drosophila and mammalian cells. To investigate the role of the tick Arp2/3 complex in tick-Rickettsia interactions, open reading frames of all subunits of the protein including Arp2, Arp3, ARPC1, ARPC2, ARPC3, ARPC4, and ARPC5 were identified from Dermacentor variabilis. Amino acid sequence analysis showed variation (ranging from 25–88%) in percent identity compared to the corresponding subunits of the complex from Drosophila melanogaster, Mus musculus, Homo sapiens, and Saccharomyces cerevisiae. Potential ATP binding sites were identified in D. variabilis (Dv) Arp2 and Arp3 subunits as well as five putative WD (Trp-Asp) motifs which were observed in DvARPC1. Transcriptional profiles of all subunits of the DvArp2/3 complex revealed greater mRNA expression in both Rickettsia-infected and -uninfected ovary compared to midgut and salivary glands. In response to R. montanensis infection of the tick ovary, the mRNA level of only DvARPC4 was significantly upregulated compared to uninfected tissues. Arp2/3 complex inhibition bioassays resulted in a decrease in the ability of R. montanensis to invade tick tissues with a significant difference in the tick ovary, indicating a role for the Arp2/3 complex in rickettsial invasion of tick cells. Characterization of tick-derived molecules associated with rickettsial infection is imperative in order to better comprehend the ecology of tick-borne rickettsial diseases.

show abstract

“…Also, recent studies have identified a core set of actin‐associated cytoskeletal proteins coupled with motility of Rickettsia parkeri in Drosophila cells (Serio et al ., 2010). In an Ixodes scapularis cell line (ISE6), Rickettsia felis , a flea‐borne transitional group rickettsiosis agent interacts with tick cell surface histone H2B and depletion of histone H2B by RNA interference and enzymatic treatment decreased rickettsial infection in the tick cells, suggesting a role of histone H2B in R. felis internalization into tick cells (Thepparit et al ., 2010). Despite progress in understanding rickettsial entry into host cells, the molecules and mechanisms of invasion of tick cells by SFG Rickettsia in ticks have not been identified.…”

Section: Introductionmentioning

confidence: 99%

Molecular characterization and tissue‐specific gene expression of Dermacentor variabilis α‐catenin in response to rickettsial infection

Sunyakumthorn

Petchampai

Kearney

et al. 2012

Insect Molecular Biology

View full text Add to dashboard Cite

Alpha catenin is a cytoskeleton protein that acts as a regulator of actin rearrangement by forming an E-cadherin adhesion complex. In Dermacentor variabilis, a putative α-catenin (Dvα-catenin) was previously identified as differentially regulated in ovaries of ticks chronically infected with Rickettsia montanensis. To begin characterizing the role(s) of Dvα-catenin during rickettsial infection, the full-length Dvα-catenin cDNA was cloned and analyzed. Comparative sequence analysis demonstrates a 3069 basepair cDNA with a 2718 bp open reading frame with a sequence similar to Ixodes scapularis α-catenin. A portion of Dvα-catenin is homologous to the vinculin-conserved domain containing a putative actin binding region and β-catenin binding and dimerization regions. Quantitative RT-PCR analysis demonstrated that Dvα-catenin is predominantly expressed in tick ovaries and is responsive to tick feeding. The tissue-specific gene expression analysis of ticks exposed to Rickettsia demonstrates that Dvα-catenin expression was significantly downregulated at 12 hours post-exposure to R. montanensis, but not in R. amblyommii-exposed ovaries, compared to Rickettsia-unexposed ticks. Studying tick-derived molecules associated with rickettsial infection will provide a better understanding of the transmission dynamics of tick-borne rickettsial diseases.

show abstract

Interaction of Rickettsia felis with histone H2B facilitates the infection of a tick cell line

Cited by 23 publications

References 48 publications

Secretome of obligate intracellularRickettsia

Secretome of obligate intracellularRickettsia

Novel Identification of Dermacentor variabilis Arp2/3 Complex and Its Role in Rickettsial Infection of the Arthropod Vector

Molecular characterization and tissue‐specific gene expression of Dermacentor variabilis α‐catenin in response to rickettsial infection

Contact Info

Product

Resources

About