Curli, fibrous surface proteins of Escherichia coli, interact with major histocompatibility complex class I molecules
(1998) In Infection and Immunity 66(3). p.649-944- Abstract
- Curli are thin, coiled fibers expressed on the surface of Escherichia coli that bind several matrix and plasma proteins such as fibronectin, laminin, plasminogen, tissue plasminogen activator, and H-kininogen. In this work, we examined the interactions between curli-expressing E. coli and human major histocompatibility complex class I (MHC-I) and class II (MHC-II) molecules. Curliated E. coli was found to interact with an MHC-I-expressing lymphoma cell line as shown by scanning electron microscopy, whereas the binding to a mutant variant of this cell line expressing small amounts of MHC-I molecules was significantly lower. Moreover, curli-expressing E. coli bound purified radiolabeled MHC-I but not MHC-II molecules, whereas an isogenic... (More)
- Curli are thin, coiled fibers expressed on the surface of Escherichia coli that bind several matrix and plasma proteins such as fibronectin, laminin, plasminogen, tissue plasminogen activator, and H-kininogen. In this work, we examined the interactions between curli-expressing E. coli and human major histocompatibility complex class I (MHC-I) and class II (MHC-II) molecules. Curliated E. coli was found to interact with an MHC-I-expressing lymphoma cell line as shown by scanning electron microscopy, whereas the binding to a mutant variant of this cell line expressing small amounts of MHC-I molecules was significantly lower. Moreover, curli-expressing E. coli bound purified radiolabeled MHC-I but not MHC-II molecules, whereas an isogenic curli-deficient mutant strain showed no affinity for either MHC-I or MHC-II. Purified insoluble curli could also bind 125I-labeled MHC-I molecules, and in Western blot experiments the 15-kDa curlin subunit protein bound intact MHC-I molecules as well as beta2-microglobulin, the light chain of MHC-I molecules. A direct interaction between monomeric MHC-I molecules and a bacterial surface protein has previously not been reported. The binding of curli to MHC-I molecules, which are present on virtually all cells in higher vertebrates, will provide curliated E. coli with ample opportunities to interact with a great variety of hosts and host cells. This should facilitate the adaptation of E. coli to different ecological niches, and in human infections the interaction between curli and MHC-I molecules could contribute to adherence and colonization. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1113503
- author
- Olsén, Arne LU ; Wick, Mary Jo LU ; Mörgelin, Matthias LU and Björck, Lars LU
- organization
- publishing date
- 1998
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Infection and Immunity
- volume
- 66
- issue
- 3
- pages
- 649 - 944
- publisher
- American Society for Microbiology
- external identifiers
-
- pmid:9488380
- scopus:0031935943
- ISSN
- 1098-5522
- language
- English
- LU publication?
- yes
- id
- fed09114-d054-4e56-9311-66715bc2ba5a (old id 1113503)
- alternative location
- http://iai.asm.org/cgi/content/full/66/3/944
- date added to LUP
- 2016-04-01 12:18:56
- date last changed
- 2022-01-27 01:56:11
@article{fed09114-d054-4e56-9311-66715bc2ba5a, abstract = {{Curli are thin, coiled fibers expressed on the surface of Escherichia coli that bind several matrix and plasma proteins such as fibronectin, laminin, plasminogen, tissue plasminogen activator, and H-kininogen. In this work, we examined the interactions between curli-expressing E. coli and human major histocompatibility complex class I (MHC-I) and class II (MHC-II) molecules. Curliated E. coli was found to interact with an MHC-I-expressing lymphoma cell line as shown by scanning electron microscopy, whereas the binding to a mutant variant of this cell line expressing small amounts of MHC-I molecules was significantly lower. Moreover, curli-expressing E. coli bound purified radiolabeled MHC-I but not MHC-II molecules, whereas an isogenic curli-deficient mutant strain showed no affinity for either MHC-I or MHC-II. Purified insoluble curli could also bind 125I-labeled MHC-I molecules, and in Western blot experiments the 15-kDa curlin subunit protein bound intact MHC-I molecules as well as beta2-microglobulin, the light chain of MHC-I molecules. A direct interaction between monomeric MHC-I molecules and a bacterial surface protein has previously not been reported. The binding of curli to MHC-I molecules, which are present on virtually all cells in higher vertebrates, will provide curliated E. coli with ample opportunities to interact with a great variety of hosts and host cells. This should facilitate the adaptation of E. coli to different ecological niches, and in human infections the interaction between curli and MHC-I molecules could contribute to adherence and colonization.}}, author = {{Olsén, Arne and Wick, Mary Jo and Mörgelin, Matthias and Björck, Lars}}, issn = {{1098-5522}}, language = {{eng}}, number = {{3}}, pages = {{649--944}}, publisher = {{American Society for Microbiology}}, series = {{Infection and Immunity}}, title = {{Curli, fibrous surface proteins of Escherichia coli, interact with major histocompatibility complex class I molecules}}, url = {{http://iai.asm.org/cgi/content/full/66/3/944}}, volume = {{66}}, year = {{1998}}, }