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Soluble pilin of Neisseria gonorrhoeae interacts with human target cells and tissue

Rytkonen, Anne; Johansson, Linda; Asp, Vendela; Albiger, Barbara LU and Jonsson, Ann-Beth (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)
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author
publishing date
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
2008-07-14 08:58:29
date last changed
2018-01-07 05:25:46
@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},
  volume       = {69},
  year         = {2001},
}