| The PagN protein mediates invasion via interaction with proteoglycan. | |
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MedLine Citation:
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PMID: 19552707 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Heparan sulphate proteoglycans are major components of the mammalian cell membrane. Here we show that PagN of Salmonella enterica serovar Typhimurium utilizes heparinated proteoglycan to successfully invade mammalian cells. Mutants defective in the production of the outer membrane protein PagN displayed similar levels of invasiveness of glycosylation-deficient pgsA-745 cells in comparison with wild-type Salmonella. Furthermore, pgsA-745 cells were invaded c. 400-fold less efficiently than CHO-K1 cells by Escherichia coli expressing PagN. PagN is likely to interact with heparinated proteoglycan as heparin could inhibit PagN-mediated invasion in a dose-dependent manner. Finally, we show, by deletion analysis, that all four extracellular loops of PagN are crucial for invasion of mammalian cells. |
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Authors:
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Matthew A Lambert; Stephen G J Smith |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2009-06-03 |
Journal Detail:
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Title: FEMS microbiology letters Volume: 297 ISSN: 1574-6968 ISO Abbreviation: FEMS Microbiol. Lett. Publication Date: 2009 Aug |
Date Detail:
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Created Date: 2009-07-23 Completed Date: 2009-10-22 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 7705721 Medline TA: FEMS Microbiol Lett Country: England |
Other Details:
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Languages: eng Pagination: 209-16 Citation Subset: IM |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Animals CHO Cells Cricetinae Cricetulus Humans Molecular Sequence Data Protein Binding Proteoglycans / metabolism* Salmonella Infections / metabolism*, microbiology Salmonella typhimurium / chemistry, genetics, metabolism* |
| Chemical | |
Reg. No./Substance:
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0/Proteoglycans |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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