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Attachment of Neisseria gonorrhoeae to the cellular pilus receptor CD46: identification of domains important for bacterial adherence

Källström, Helena; Blackmer Gill, Darcy; Albiger, Barbara LU ; Liszewski, M. Kathryn; Atkinson, John P. and Jonsson, Ann-Beth (2001) In Cellular Microbiology 3(3). p.133-143
Abstract
Pili of Neisseria gonorrhoeae mediate binding of the bacteria to human host cells. Membrane cofactor protein (MCP or CD46), a human cell-surface protein involved in regulation of complement activation, acts as a cellular pilus receptor. In this work, we examined which domains of CD46 mediate bacterial adherence. The CD46 expression was quantified and characterized in human epithelial cell lines. N. gonorrhoeae showed the highest adherence to ME180 cells, which have BC1 as the dominant phenotype. The BC isoforms of CD46 were expressed in all cell lines tested. The adherence was not enhanced by high expression of other isoforms, showing that the BC domain of CD46 is important in adherence of N. gonorrhoeae to human cells. To characterize the... (More)
Pili of Neisseria gonorrhoeae mediate binding of the bacteria to human host cells. Membrane cofactor protein (MCP or CD46), a human cell-surface protein involved in regulation of complement activation, acts as a cellular pilus receptor. In this work, we examined which domains of CD46 mediate bacterial adherence. The CD46 expression was quantified and characterized in human epithelial cell lines. N. gonorrhoeae showed the highest adherence to ME180 cells, which have BC1 as the dominant phenotype. The BC isoforms of CD46 were expressed in all cell lines tested. The adherence was not enhanced by high expression of other isoforms, showing that the BC domain of CD46 is important in adherence of N. gonorrhoeae to human cells. To characterize the pilus-binding site within the CD46 molecule, a set of CD46-BC1 deletion constructs were transfected into COS-7 cells. Piliated N. gonorrhoeae attached well to CD46-BC1-expressing COS-7 cells. We show that the complement control protein repeat 3 (CCP-3) and the serine-threonine-proline (STP)-rich domain of CD46 are important for efficient adherence to host cells. Further, partial deletion of the cytoplasmic tail of CD46 results in low bacterial binding, indicating that the cytoplasmic tail takes part in the process of establishing a stable interaction between N. gonorrhoeae and host cells. (Less)
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author
publishing date
type
Contribution to journal
publication status
published
subject
in
Cellular Microbiology
volume
3
issue
3
pages
133 - 143
publisher
Wiley-Blackwell
external identifiers
  • pmid:11260136
  • scopus:0035076258
ISSN
1462-5814
DOI
10.1046/j.1462-5822.2001.00095.x
language
English
LU publication?
no
id
a37d7a82-7cb0-4660-b84a-b077f2f71d48 (old id 1119897)
date added to LUP
2008-07-01 11:16:33
date last changed
2018-02-11 03:27:48
@article{a37d7a82-7cb0-4660-b84a-b077f2f71d48,
  abstract     = {Pili of Neisseria gonorrhoeae mediate binding of the bacteria to human host cells. Membrane cofactor protein (MCP or CD46), a human cell-surface protein involved in regulation of complement activation, acts as a cellular pilus receptor. In this work, we examined which domains of CD46 mediate bacterial adherence. The CD46 expression was quantified and characterized in human epithelial cell lines. N. gonorrhoeae showed the highest adherence to ME180 cells, which have BC1 as the dominant phenotype. The BC isoforms of CD46 were expressed in all cell lines tested. The adherence was not enhanced by high expression of other isoforms, showing that the BC domain of CD46 is important in adherence of N. gonorrhoeae to human cells. To characterize the pilus-binding site within the CD46 molecule, a set of CD46-BC1 deletion constructs were transfected into COS-7 cells. Piliated N. gonorrhoeae attached well to CD46-BC1-expressing COS-7 cells. We show that the complement control protein repeat 3 (CCP-3) and the serine-threonine-proline (STP)-rich domain of CD46 are important for efficient adherence to host cells. Further, partial deletion of the cytoplasmic tail of CD46 results in low bacterial binding, indicating that the cytoplasmic tail takes part in the process of establishing a stable interaction between N. gonorrhoeae and host cells.},
  author       = {Källström, Helena and Blackmer Gill, Darcy and Albiger, Barbara and Liszewski, M. Kathryn and Atkinson, John P. and Jonsson, Ann-Beth},
  issn         = {1462-5814},
  language     = {eng},
  number       = {3},
  pages        = {133--143},
  publisher    = {Wiley-Blackwell},
  series       = {Cellular Microbiology},
  title        = {Attachment of Neisseria gonorrhoeae to the cellular pilus receptor CD46: identification of domains important for bacterial adherence},
  url          = {http://dx.doi.org/10.1046/j.1462-5822.2001.00095.x},
  volume       = {3},
  year         = {2001},
}