The integrin-binding domain of invasin is sufficient to allow bacterial entry into mammalian cells.
Yersinia pseudotuberculosis is able to enter normally nonphagocytic host cells by multiple pathways, the most efficient of which is mediated by invasin, a 986-amino-acid bacterial outer membrane protein. It has previously been shown that the C-terminal 192 amino acids of invasin are sufficient to bind mammalian cells. To determine if additional regions of the invasin protein are necessary to promote entry, we developed a novel assay that tests the ability of various invasin derivatives to confer on Staphylococcus aureus the ability to enter animal cells. We determined that the 192-amino-acid cell-binding region of invasin, when used to coat the bacterial cell surface, was also sufficient to promote cellular penetration. These results suggest that the simple binding of invasin to its receptors is sufficient to mediate entry and that the bacterium plays a largely passive role in the entry process.
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Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, Massachusetts 02111.
Isberg
R R
RR
Leong
J M
JM
D018829:Adhesins, Bacterial; D000818:Animals; D001426:Bacterial Proteins / Q000276:immunology*; D001665:Binding Sites; D002352:Carrier Proteins / Q000378:metabolism*; D002460:Cell Line; D016023:Integrins / Q000378:metabolism*; D058619:Maltose-Binding Proteins; D013211:Staphylococcus aureus / Q000502:physiology*
D018829:Adhesins, Bacterial; D001426:Bacterial Proteins; D002352:Carrier Proteins; D016023:Integrins; D058619:Maltose-Binding Proteins; C053476:invasin, Yersinia