Histone-like DNA binding protein of Streptococcus intermedius induces the expression of pro-inflammatory cytokines in human monocytes via activation of ERK1/2 and JNK pathways

Liu, Dali; Yumoto, Hiromichi; Hirota, Kaoru; Murakami, Keiji; Takahashi, Kanako; Hirao, Kazuyuki; Matsuo, Takashi; Ohkura, Kazuto; Nagamune, Hideaki; Miyake, Yoichiro

doi:10.1111/j.1462-5822.2007.01040.x

Cited by 25 publications

(38 citation statements)

References 59 publications

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“…Our data demonstrate that endogenous HlpA is preferentially expressed at the bacterial surface in the stationary growth phase, which is in line with the study of Katsube et al, who reported that the histone-like protein MDP1 of Mycobacterium smegmatis accumulates in cell wall fractions in the stationary phase (18). Furthermore, our findings correlate with previous studies reporting the release of HlpA during the stationary growth phase (22,35). In the exponential phase, HlpA is required intracellularly to execute its physiological role in nucleoid formation (1), but even though endogenous HlpA is maintained intracellularly, recombinant HlpA-His was not able to bind to the bacterial surface.…”

Section: Discussionsupporting

confidence: 83%

“…Interestingly, the heparin-binding histone-like protein A (HlpA) from S. bovis was recently shown to be present in cell wall extracts and was a target of the humoral immune response in patients with colon cancer (38). Several other studies confirmed that this conserved bacterial protein from Streptococcus pyogenes, which is 95.6% identical to S. gallolyticus HlpA, had affinity for lipoteichoic acid (LTA), an intrinsic component of the gram-positive cell wall (22,35,43). Furthermore, proteomic analysis of the bacterial surface of S. pyogenes revealed that HlpA is a surface-linked protein (33).…”

mentioning

confidence: 71%

“…However, HlpA from Streptococcus mitis by itself has been shown to activate an immune response in murine macrophages in vitro, which is mediated by the induction of interleukin-1 and tumor necrosis factor alpha (43). Similarly, Liu et al have shown that HlpA of S. intermedius can induce cytokine production in human macrophages (22). However, none of these studies has determined the net effect of the HlpA-mediated shielding of LTA from intact bacteria on the interaction with, and activation of, macrophages; this will be a subject of our future investigations.…”

Section: Discussionmentioning

confidence: 99%

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Surface-Exposed Histone-Like Protein A Modulates Adherence of Streptococcus gallolyticus to Colon Adenocarcinoma Cells

Boleij¹,

Schaeps²,

Kleijn

et al. 2009

Infect Immun

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Streptococcus gallolyticus (formerly known as Streptococcus bovis biotype I) is a low-grade opportunistic pathogen which is considered to be associated with colon cancer. It is thought that colon polyps or tumors are the main portal of entry for this bacterium and that heparan sulfate proteoglycans (HSPGs) at the colon tumor cell surface are involved in bacterial adherence during the first stages of infection. In this study, we have shown that the histone-like protein A (HlpA) of S. gallolyticus is a genuine anchorless bacterial surface protein that binds to lipoteichoic acid (LTA) of the gram-positive cell wall in a growth phase-dependent manner. In addition, HlpA was shown to be one of the major heparin-binding proteins of S. gallolyticus able to bind to the HSPG-expressing colon tumor cell lines HCT116 and HT-29. Strikingly, although wild-type levels of HlpA appeared to contribute to adherence, coating of additional HlpA at the bacterial surface resulted in reduced binding to colon tumor cells. This may be explained by the fact that heparan sulfate and LTA compete for the same binding site in HlpA. Altogether, this study implies that HlpA serves as a fine-tuning factor for bacterial adherence.

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Section: Discussionsupporting

confidence: 83%

mentioning

confidence: 71%

Section: Discussionmentioning

confidence: 99%

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Surface-Exposed Histone-Like Protein A Modulates Adherence of Streptococcus gallolyticus to Colon Adenocarcinoma Cells

Boleij¹,

Schaeps²,

Kleijn

et al. 2009

Infect Immun

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“…The stimulatory effect of rS.i.-HLP was cooperative by costimulation with LTA. 29 Upregulation of serum pro-inflammatory cytokines, complements, and soluble interleukin 2 receptor in PBC was reported. 30 Therefore, kinetic studies including cytokine and complement changes in our mice model are needed.…”

Section: Discussionmentioning

confidence: 99%

Long-term bacterial exposure can trigger nonsuppurative destructive cholangitis associated with multifocal epithelial inflammation

Haruta

Kikuchi

Hashimoto

et al. 2010

Laboratory Investigation

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“…Along with other streptococci, S. mutans encodes a single NAP, known as HLP (SMU.589), which is an essential protein in streptococci (48). Previous studies have shown that HLPs of streptococci resemble E. coli HU protein in terms of nucleoid structuring (24,47,51) and may play a potential role in infection-induced inflammation during streptococcal pathogenesis (66,67,77). In this study, we found that HLP also plays an important role in silencing the expression of foreign genes acquired by S. mutans.…”

Section: Discussionmentioning

confidence: 99%

CovR Alleviates Transcriptional Silencing by a Nucleoid-Associated Histone-Like Protein in Streptococcus mutans

Biswas

Mohapatra

2012

J Bacteriol

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In Streptococcus mutans, the global response regulator CovR plays an important role in biofilm formation, stress tolerance response, and caries production. We have previously demonstrated that CovR activates a large gene cluster, which is a part of a genomic island, TnSmu2. In this article, we have further characterized CovR at the molecular level to understand the gene activation mechanism. Toward this end, we mapped the transcription start site of the operon that lies upstream of the SMU.1348 gene (P SMU.1348 ), the first gene of the cluster. We constructed a transcriptional reporter fusion and showed that CovR induces expression from P SMU.1348 . We also demonstrated that purified CovR protects the sequence surrounding the ؊10 region of P SMU.1348 . In an in vitro transcription assay, we showed that histone-like protein (HLP), a homologue of Escherichia coli HU protein, represses transcription from P SMU.1348 . In vivo overexpression of HLP in trans also represses transcription from P SMU.1348 . Addition of CovR to the HLP-repressed P SMU.1348 resulted in increased transcription from the promoter, suggesting a role for CovR in countering HLP silencing. Moreover, addition of SMU.1349, a transcriptional activator of the operon, to the in vitro assay further stimulated the transcription. Based on our in vivo and in vitro results, we propose a model for transcriptional activation of the operon.

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Histone-like DNA binding protein of Streptococcus intermedius induces the expression of pro-inflammatory cytokines in human monocytes via activation of ERK1/2 and JNK pathways

Abstract: Summary Streptococcus intermedius

Cited by 25 publications

References 59 publications

Surface-Exposed Histone-Like Protein A Modulates Adherence of Streptococcus gallolyticus to Colon Adenocarcinoma Cells

Surface-Exposed Histone-Like Protein A Modulates Adherence of Streptococcus gallolyticus to Colon Adenocarcinoma Cells

Long-term bacterial exposure can trigger nonsuppurative destructive cholangitis associated with multifocal epithelial inflammation

CovR Alleviates Transcriptional Silencing by a Nucleoid-Associated Histone-Like Protein in Streptococcus mutans

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