Characterization of Hemoglobin Binding to Actinobacillus actinomycetemcomitans

Nagata, Hideki; Ikawa, Yasuko; Kuboniwa, Masae; Maeda, Kengo; Shizukuishi, Satoshi

doi:10.1006/anae.2002.0425

“…The strongest binding activity was observed at pH 5.0. Similar pH-dependent hemoglobin-binding activity has also been documented in other periodontal pathogens, such as Porphyromonas gingivalis [16,18], Prevotella nigrescens [19] and Actinobacillus actinomycetemcomitans [20]. Hemoglobin displays conformational changes depending on oxygenation state.…”

Section: Resultssupporting

confidence: 58%

Purification and characterization of a hemoglobin-binding outer membrane protein of Prevotella intermedia

Guan

¹

,

Nagata

²

,

Maeda

³

et al. 2004

FEMS Microbiology Letters

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An outer membrane hemoglobin-binding protein of Prevotella intermedia was identified and purified in the present study. Hemoglobin-binding protein was purified via a series of column chromatographic methods. The molecular mass of the purified protein, which was approximately 60 kDa, was determined by SDS-PAGE. Hemoglobin binding of the protein was examined by Western blot and dot blot assays. Hemoglobin-binding activity was pH dependent; the strongest binding activity occurred at pH 5.0. Globin greatly decreased the binding activity, whereas transferrin, cytochrome C, and catalase exerted no effect. Dissociation constant between the 60-kDa protein and hemoglobin was 1.48 x 10(-8) M as measured by surface plasmon resonance. These results suggest that P. intermedia binds hemoglobin specifically through the 60-kDa outer membrane protein.

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“…The strongest binding activity was observed at pH 5.0. Similar pH‐dependent hemoglobin‐binding activity has also been documented in other periodontal pathogens, such as Porphyromonas gingivalis [16,18], Prevotella nigrescens [19] and Actinobacillus actinomycetemcomitans [20]. Hemoglobin displays conformational changes depending on oxygenation state.…”

Section: Resultssupporting

confidence: 57%

Purification and characterization of a hemoglobin-binding outer membrane protein ofPrevotella intermedia

Guan

¹

,

Nagata

²

,

Maeda

³

et al. 2004

FEMS Microbiology Letters

Self Cite

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An outer membrane hemoglobin-binding protein of Prevotella intermedia was identified and purified in the present study. Hemoglobin-binding protein was purified via a series of column chromatographic methods. The molecular mass of the purified protein, which was approximately 60 kDa, was determined by SDS-PAGE. Hemoglobin binding of the protein was examined by Western blot and dot blot assays. Hemoglobin-binding activity was pH dependent; the strongest binding activity occurred at pH 5.0. Globin greatly decreased the binding activity, whereas transferrin, cytochrome C, and catalase exerted no effect. Dissociation constant between the 60-kDa protein and hemoglobin was 1.48 x 10(-8) M as measured by surface plasmon resonance. These results suggest that P. intermedia binds hemoglobin specifically through the 60-kDa outer membrane protein.

show abstract

“…For example, A. actinomycetemcomitans has a lipopolysaccharide that binds to haemoglobin and could play a role in iron acquisition (55). One study has shown that A. actinomycetemcomitans can utilize haemoglobin as an iron source, and that bacterial binding to haemoglobin depends on at least two cell‐surface proteins with molecular masses of 40 and 65 kDa (157). A comparison of A. actinomycetemcomitans strains for binding to iron‐binding proteins such as haemoglobin revealed that none could bind to transferrin due to the presence of a non‐functional tbpA gene encoding transferrin binding protein.…”

Section: Iron Acquisitionmentioning

confidence: 99%

Aggregatibacter (Actinobacillus) actinomycetemcomitans: a triple A* periodontopathogen?

Henderson¹,

Ward²,

Ready³

2010

Periodontology 2000

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Characterization of Hemoglobin Binding to Actinobacillus actinomycetemcomitans

Cited by 5 publications

References 16 publications

Purification and characterization of a hemoglobin-binding outer membrane protein of Prevotella intermedia

Purification and characterization of a hemoglobin-binding outer membrane protein of Prevotella intermedia

Purification and characterization of a hemoglobin-binding outer membrane protein ofPrevotella intermedia

Aggregatibacter (Actinobacillus) actinomycetemcomitans: a triple A* periodontopathogen?

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