The Human‐Specific Action of Intermedilysin, a Homolog of Streptolysin O, Is Dictated by Domain 4 of the Protein
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- Hideaki Nagamune
- Department of Biological Science and Technology, Faculty of Engineering The University of Tokushima Tokushima Tokushima 770‐8506 Japan
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- Kazuto Ohkura
- Department of Biological Science and Technology, Faculty of Engineering The University of Tokushima Tokushima Tokushima 770‐8506 Japan
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- Akiko Sukeno
- Department of Biological Science and Technology, Faculty of Engineering The University of Tokushima Tokushima Tokushima 770‐8506 Japan
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- Graeme Cowan
- Division of Infection and Immunity, Institute of Biomedical and Life Sciences University of Glasgow Glasgow G12 8QQ United Kingdom
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- Timothy J. Mitchell
- Division of Infection and Immunity, Institute of Biomedical and Life Sciences University of Glasgow Glasgow G12 8QQ United Kingdom
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- Wataru Ito
- Department of Biological Science and Technology, Faculty of Engineering The University of Tokushima Tokushima Tokushima 770‐8506 Japan
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- Ooki Ohnishi
- Department of Biological Science and Technology, Faculty of Engineering The University of Tokushima Tokushima Tokushima 770‐8506 Japan
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- Kanako Hattori
- Department of Biological Science and Technology, Faculty of Engineering The University of Tokushima Tokushima Tokushima 770‐8506 Japan
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- Miki Yamato
- Department of Biological Science and Technology, Faculty of Engineering The University of Tokushima Tokushima Tokushima 770‐8506 Japan
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- Katsuhiko Hirota
- Department of Oral Microbiology, School of Dentistry The University of Tokushima Tokushima Tokushima 770‐8503 Japan
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- Yoichiro Miyake
- Department of Oral Microbiology, School of Dentistry The University of Tokushima Tokushima Tokushima 770‐8503 Japan
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- Takuya Maeda
- Department of Biological Science and Technology, Faculty of Engineering The University of Tokushima Tokushima Tokushima 770‐8506 Japan
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- Hiroki Kourai
- Department of Biological Science and Technology, Faculty of Engineering The University of Tokushima Tokushima Tokushima 770‐8506 Japan
Abstract
<jats:title>Abstract</jats:title><jats:p>Intermedilysin is a pore‐forming cytolysin belonging to the streptolysin O gene family known as the ‘Cholesterol‐binding/dependent cytolysins’ and is unique within the family in that it is highly human‐specific. This specificity suggests interaction with a component of human cells other than cholesterol, the proposed receptor for the other toxins of the gene family. Indeed, intermedilysin showed no significant degree of affinity to free or liposome‐embedded cholesterol. Characterization of intermedilysin undecapeptide mutants revealed that this lack of affinity to cholesterol was a result of the substitutions of intermedilysin in this region. Absorption assays with erythrocyte membranes from various animals, competitive inhibition with domain 4 of intermedilysin and liposome‐binding assays of streptolysin O and intermedilysin indicated that cell membrane binding is the human‐specific step of intermedilysin action, that the host cell membrane‐binding site is located within domain 4 in common with other members of the family and that the receptor for this toxin is not cholesterol. The species specificity of undecapeptide mutants of intermedilysin and streptolysin O and chimeric mutants between intermedilysin and streptolysin O, and intermedilysin and pneumolysin indicated that domain 4 of intermedilysin determines the human‐specific action step and the cell‐binding site of domain 4 lies within the 56 amino acids of the C‐terminal, excluding the undecapeptide region.</jats:p>
Journal
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- Microbiology and Immunology
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Microbiology and Immunology 48 (9), 677-692, 2004-09
Wiley
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Details 詳細情報について
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- CRID
- 1360574096461212800
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- ISSN
- 13480421
- 03855600
- http://id.crossref.org/issn/03855600
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- Data Source
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- Crossref