Pili of <i>Aeromonas hydrophila</i>
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- HONMA Yasuko
- Department of Bacteriology, University of the Ryukyus School of Medicine
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- NAKASONE Noboru
- Department of Bacteriology, University of the Ryukyus School of Medicine
抄録
Aeromonas hydrophila (Ae6) has 2 morphologically distinctive kinds of pili. One appeared rigid, channeled, and straight with a diameter of 9nm (Ae6-R pili). The other looked flexible, wavy, and having helical structure with a diameter of 7nm (Ae6-W pili). Ae6-R pili were purified and characterized. The pili consisted of a subunit protein with a molecular weight of 18kDa as estimated by SDS-PAGE, and contained 42.3% hydrophobic amino acids and one cysteine residue. The pilus was solubilized to 18kDa subunit protein by 2-mercaptoethanol, dithiothreitol, hydrochloric acid, or heating at 120C for 5min. The organism Ae6 was strongly adhesive to rabbit intestines as well as human intestines, and agglutinated erythrocytes. Anti-pili antibody (Fab fraction) did not block the adhesion. Purified Ae6-R pili did not adhere to the intestine or to the erythrocytes. However, the anti-pili Fab inhibited pellicle formation of the organisms culured in broth, and also inhibited salt agglutination with ammonium sulfate. From these results, Ae6-R pili are not likely a colonization factor but probably play a role in the autoaggregation of the organisms.
収録刊行物
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- MICROBIOLOGY and IMMUNOLOGY
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MICROBIOLOGY and IMMUNOLOGY 34 (2), 83-98, 1990
Center For Academic Publications Japan
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詳細情報 詳細情報について
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- CRID
- 1570854178105124736
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- NII論文ID
- 130003483649
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- ISSN
- 03855600
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- 本文言語コード
- en
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- データソース種別
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- CiNii Articles