Document Detail


The PagN protein mediates invasion via interaction with proteoglycan.
MedLine Citation:
PMID:  19552707     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Matthew A Lambert; Stephen G J Smith
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2009-06-03
Journal Detail:
Title:  FEMS microbiology letters     Volume:  297     ISSN:  1574-6968     ISO Abbreviation:  FEMS Microbiol. Lett.     Publication Date:  2009 Aug 
Date Detail:
Created Date:  2009-07-23     Completed Date:  2009-10-22     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  7705721     Medline TA:  FEMS Microbiol Lett     Country:  England    
Other Details:
Languages:  eng     Pagination:  209-16     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
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:
0/Proteoglycans

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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