Soluble pilin of Neisseria gonorrhoeae interacts with human target cells and tissue
(2001) In Infection and Immunity 69(10). p.6419-6426- Abstract
- Pili of Neisseria gonorrhoeae are phase-variable surface structures that mediate adherence to host target cells. Each pilus is composed of thousands of major pilus subunits, pilins, pilus-associated protein PilC, and possibly other components. Piliated and nonpiliated gonococcal clones may secrete a soluble smaller pilin (S-pilin) that is cleaved after amino acid 39 of the mature pilin protein. Here, purified S-pilin was found to migrate as a 61- to 64-kDa double band on nondenaturing gels, suggesting the formation of tetrameric S-pilin proteins with two isomeric forms. In situ studies of binding to formalin-fixed tissue sections demonstrated the binding of S-pilin to human tissue but not to tissue from mouse or rat organs, showing the... (More)
- Pili of Neisseria gonorrhoeae are phase-variable surface structures that mediate adherence to host target cells. Each pilus is composed of thousands of major pilus subunits, pilins, pilus-associated protein PilC, and possibly other components. Piliated and nonpiliated gonococcal clones may secrete a soluble smaller pilin (S-pilin) that is cleaved after amino acid 39 of the mature pilin protein. Here, purified S-pilin was found to migrate as a 61- to 64-kDa double band on nondenaturing gels, suggesting the formation of tetrameric S-pilin proteins with two isomeric forms. In situ studies of binding to formalin-fixed tissue sections demonstrated the binding of S-pilin to human tissue but not to tissue from mouse or rat organs, showing the presence of a human-specific receptor-binding domain within the pilin polypeptide. Pretreatment of the target tissues with proteinase K decreased gonococcal binding dramatically, whereas pretreatment with neuraminidase and meta-periodate, which cleave carbon-carbon linkages between vicinal hydroxyl groups in carbohydrates, did not affect gonococcal binding. In overlay assays, purified S-pilin bound to a band with a migration pattern and size similar to those of CD46, a cellular pilus receptor. Further, binding of N. gonorrhoeae to target cells and tissues could be blocked by both CD46 antibodies and purified S-pilin. These data argue that S-pilin interacts with a protein domain(s) of the CD46 receptor on human cells. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1119879
- author
- Rytkonen, Anne ; Johansson, Linda ; Asp, Vendela ; Albiger, Barbara LU and Jonsson, Ann-Beth
- publishing date
- 2001
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Infection and Immunity
- volume
- 69
- issue
- 10
- pages
- 6419 - 6426
- publisher
- American Society for Microbiology
- external identifiers
-
- pmid:11553586
- scopus:0034830977
- ISSN
- 1098-5522
- DOI
- 10.1128/IAI.69.10.6419-6426.2001
- language
- English
- LU publication?
- no
- id
- 93b10b65-d1a0-434d-983e-1b52f5bdc513 (old id 1119879)
- date added to LUP
- 2016-04-01 11:49:33
- date last changed
- 2022-01-26 18:46:56
@article{93b10b65-d1a0-434d-983e-1b52f5bdc513,
abstract = {{Pili of Neisseria gonorrhoeae are phase-variable surface structures that mediate adherence to host target cells. Each pilus is composed of thousands of major pilus subunits, pilins, pilus-associated protein PilC, and possibly other components. Piliated and nonpiliated gonococcal clones may secrete a soluble smaller pilin (S-pilin) that is cleaved after amino acid 39 of the mature pilin protein. Here, purified S-pilin was found to migrate as a 61- to 64-kDa double band on nondenaturing gels, suggesting the formation of tetrameric S-pilin proteins with two isomeric forms. In situ studies of binding to formalin-fixed tissue sections demonstrated the binding of S-pilin to human tissue but not to tissue from mouse or rat organs, showing the presence of a human-specific receptor-binding domain within the pilin polypeptide. Pretreatment of the target tissues with proteinase K decreased gonococcal binding dramatically, whereas pretreatment with neuraminidase and meta-periodate, which cleave carbon-carbon linkages between vicinal hydroxyl groups in carbohydrates, did not affect gonococcal binding. In overlay assays, purified S-pilin bound to a band with a migration pattern and size similar to those of CD46, a cellular pilus receptor. Further, binding of N. gonorrhoeae to target cells and tissues could be blocked by both CD46 antibodies and purified S-pilin. These data argue that S-pilin interacts with a protein domain(s) of the CD46 receptor on human cells.}},
author = {{Rytkonen, Anne and Johansson, Linda and Asp, Vendela and Albiger, Barbara and Jonsson, Ann-Beth}},
issn = {{1098-5522}},
language = {{eng}},
number = {{10}},
pages = {{6419--6426}},
publisher = {{American Society for Microbiology}},
series = {{Infection and Immunity}},
title = {{Soluble pilin of Neisseria gonorrhoeae interacts with human target cells and tissue}},
url = {{http://dx.doi.org/10.1128/IAI.69.10.6419-6426.2001}},
doi = {{10.1128/IAI.69.10.6419-6426.2001}},
volume = {{69}},
year = {{2001}},
}