RRC ID 35244
Author Lambert MA, Smith SG.
Title The PagN protein mediates invasion via interaction with proteoglycan.
Journal FEMS Microbiol Lett
Abstract 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.
Volume 297(2)
Pages 209-16
Published 2009-8-1
DOI 10.1111/j.1574-6968.2009.01666.x
PII FML1666
PMID 19552707
MeSH Amino Acid Sequence Animals CHO Cells Cricetinae Cricetulus Humans Molecular Sequence Data Protein Binding Proteoglycans / metabolism* Salmonella Infections / metabolism* Salmonella Infections / microbiology Salmonella typhimurium / chemistry Salmonella typhimurium / genetics Salmonella typhimurium / metabolism*
IF 1.987
Times Cited 26
WOS Category MICROBIOLOGY
Resource
Prokaryotes E. coli