Extracellular Mycobacterial DNA-binding Protein 1 Participates in Mycobacterium-Lung Epithelial Cell Interaction through Hyaluronic Acid

Aoki, Keiko M.; Matsumoto, Sohkichi; Hirayama, Yukio; Wada, Takayuki; Ozeki, Yuriko; Niki, Makoto; Domenech, Pilar; Umemori, Kiyoko; Yamamoto, Saburo; Mineda, Amao; Matsumoto, Makoto; Kobayashi, Keiko

doi:10.1074/jbc.m402677200

Cited by 81 publications

(89 citation statements)

References 49 publications

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“…Although the heparin-binding motifs, XBBXBX and XBBBXXBX (where B represents basic amino acids and X represents hydrophobic amino acids) have been known for many years (Cardin and Weintraub, 1989), more recent studies indicate that various combinations of clustered basic amino acids can bind heparin (Aoki et al, 2004). P159 is rich in lysine (K) and arginine (R) residues (15.6% and 13.9% of F3 P159 and F4 P159 sequences, respectively, are K and R), and further studies aim to more accurately delineate the heparin binding domains within regions of P159.…”

Section: Discussionmentioning

confidence: 99%

P159 is a proteolytically processed, surface adhesin ofMycoplasma hyopneumoniae: defined domains of P159 bind heparin and promote adherence to eukaryote cells

Burnett

Dinkla

Rohde

et al. 2006

Molecular Microbiology

185

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SummaryMycoplasma hyopneumoniae , the causative agent of porcine enzootic pneumonia, colonizes the respiratory cilia of affected swine causing significant economic losses to swine production worldwide. Heparin is known to inhibit adherence of M. hyopneumoniae to porcine respiratory epithelial cilia. M. hyopneumoniae cells bind heparin but the identity of the heparinbinding proteins is limited. Proteomic analysis of M. hyopneumoniae lysates identified 27 kDa (P27), 110 kDa (P110) and 52 kDa (P52) proteins representing different regions of a 159 kDa (P159) protein derived from mhp494. These cleavage fragments were surface located and present at all growth stages.

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Section: Discussionmentioning

confidence: 99%

P159 is a proteolytically processed, surface adhesin ofMycoplasma hyopneumoniae: defined domains of P159 bind heparin and promote adherence to eukaryote cells

Burnett

Dinkla

Rohde

et al. 2006

Molecular Microbiology

185

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“…Expression and Purification of Recombinant MDP1-Recombinant MDP1 was obtained as described previously (30). Briefly, the oligonucleotide primers (forward, 5Ј-CCCCATATGAAC-AAAGCAGAGCTCATTGAC-3Ј; reverse, 5Ј-CCCAAGCTT-TTTGCGACCCCGCCGAGCGG-3Ј) were synthesized based on the nucleotide sequences of BCG and M. tuberculosis mdp1.…”

Section: Reduction Of Nitroblue Tetrazolium (Nbt)-this Test Detects Imentioning

confidence: 99%

A Novel Mechanism of Growth Phase-dependent Tolerance to Isoniazid in Mycobacteria

Niki

Tateishi

Ozeki

et al. 2012

Journal of Biological Chemistry

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Background:The mechanism underlying mycobacterial phenotypic tolerance to isoniazid is unknown. Results: MDP1, a mycobacterial histone-like protein, down-regulates KatG expression. Conclusion: Down-regulation of KatG by MDP1 causes growth phase-dependent phenotypic tolerance to isoniazid in mycobacteria. Significance: Understanding the mechanism by which mycobacteria acquire tolerance to isoniazid is important for developing novel therapies.

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Section: Introductionmentioning

confidence: 99%

“…This adhesion is, therefore, a promising target for the development of new antimicrobial therapeutics [3]. In the adhesion, heparin or heparin-related oligosaccharides are one of the extracellular matrix molecules of the host recognized by cell surface proteins of bacteria [4][5][6][7][8].Due to the lack of appropriate techniques for the study of the interactions of heparin-living bacteria, most heparin-bacteria binding studies have been conducted with isolated bacterial proteins [9,10]. Although useful information can be obtained from such studies, one potential drawback is the exclusion of membrane phenomena such as ligand-induced receptor oligomerization that can affect the overall binding affinity [11].…”

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confidence: 99%

Characterization of heparin–living bacteria interactions by chemiluminescence electrophoretic mobility shift assay

Kang

Lee

Gorenstein

2007

Analytical Biochemistry

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Keywordschemiluminescence; nonradioisotopic detection; EMSA; heparin-bacteria interactions; heparin; bacteriaThe electrophoretic mobility shift assay [EMSA]1 is one of the most sensitive methods for studying DNA-protein interactions. Chemiluminescence [CL]1 has been used as an alternative to radioisotopic detection of samples in the EMSA [1,2], as it has advantages such as safety and stability (no isotopic decay) of the sample. In this study, we examined the feasibility of the application of CL EMSA to studying heparin-living bacteria interactions. As an example, binding of biotinylated heparin to Escherichia coli was examined.The pathogenesis of most infections is initiated by microbial adhesion to host tissue. This adhesion is, therefore, a promising target for the development of new antimicrobial therapeutics [3]. In the adhesion, heparin or heparin-related oligosaccharides are one of the extracellular matrix molecules of the host recognized by cell surface proteins of bacteria [4][5][6][7][8].Due to the lack of appropriate techniques for the study of the interactions of heparin-living bacteria, most heparin-bacteria binding studies have been conducted with isolated bacterial proteins [9,10]. Although useful information can be obtained from such studies, one potential drawback is the exclusion of membrane phenomena such as ligand-induced receptor oligomerization that can affect the overall binding affinity [11]. Therefore, it is desirable to examine the adhesion process using bacteria in the intact state to include the membrane phenomena. With this purpose, scintillation counting of radioisotope radiation [12] and sodium dodecyl sulfate-polyacrylamide gel electrophoresis [8] were used to assess the binding of heparin to living bacteria. More recently, atomic force microscopy was successfully used to investigate heparin-living bacteria interactions and producing quantitative data [13]. However, these methods are qualitative [8], require radioisotope labeling [12], an instrument, which may not be readily available in common laboratories [13].EMSA has been widely employed to detect DNA-protein interactions since its first application [14]. In this study, CL EMSA is introduced to complement the existing methods to study heparin-bacteria interactions. CL has advantages such as safety and sample stability (no

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Extracellular Mycobacterial DNA-binding Protein 1 Participates in Mycobacterium-Lung Epithelial Cell Interaction through Hyaluronic Acid

Cited by 81 publications

References 49 publications

P159 is a proteolytically processed, surface adhesin ofMycoplasma hyopneumoniae: defined domains of P159 bind heparin and promote adherence to eukaryote cells

P159 is a proteolytically processed, surface adhesin ofMycoplasma hyopneumoniae: defined domains of P159 bind heparin and promote adherence to eukaryote cells

A Novel Mechanism of Growth Phase-dependent Tolerance to Isoniazid in Mycobacteria

Characterization of heparin–living bacteria interactions by chemiluminescence electrophoretic mobility shift assay

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