
Specific binding of recombinant Listeria monocytogenes p60 protein to Caco‐2 cells
Author(s) -
Park JungHyun,
Lee YongSoon,
Lim YoonKyu,
Kwon SoonHwan,
Lee ChilU,
Yoon ByoungSu
Publication year - 2000
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2000.tb09078.x
Subject(s) - listeria monocytogenes , internalization , enterocyte , listeria , microbiology and biotechnology , flow cytometry , escherichia coli , biology , caco 2 , recombinant dna , bacteria , extracellular , cell membrane , cell , biochemistry , gene , genetics , small intestine
The Listeria monocytogenes p60 is a major extracellular protein, which is believed to be involved in the invasion of these bacteria into their host cells. So far the mechanism by which p60 participates in the internalization or penetration of L. monocytogenes is still veiled. To determine the possibility of a direct interaction of p60 with the host cell surface, the iap gene was recombinantly expressed in Escherichia coli and used for binding studies with the enterocyte‐like Caco‐2 cells. Fluorescence activated flow cytometry and confocal laser scanning microscopy revealed a cell membrane specific staining with p60, which implications in Listeria virulence are discussed.