A human endothelial cell membrane protein that binds Staphylococcus aureus in vitro

David C. Tompkins, Victor B. Hatcher, Daxa Patel, George A. Orr, Lore L. Higgins, Franklin D. Lowy

Research output: Contribution to journalArticlepeer-review

42 Scopus citations


We have investigated S. aureus adherence to human endothelial cells utilizing an in vitro model. Staphylococcus binding to confluent endothelial cell monolayers was saturable in both dose and time response studies suggesting that the binding interaction was specific. We have developed a technique, based on the pH dependent affinity of iminobiotin for streptavidin, for the isolation of an endothelial cell membrane component that binds S. aureus, in vitro. A 50-kD membrane component was isolated and purified using this approach. This component was trypsin sensitive, periodate insensitive, and did not label with [3H]glucosamine. [35S]Methionine and [125I]iodine labeling confirmed that the protein was synthesized by and expressed on the endothelial cell surface. Functional binding studies demonstrated that staphylococci, but not endothelial cells, bound to the protein when immobilized on microtiter wells. Preincubation of staphylococci with the purified protein significantly (P < 0.001) reduced staphylococcal binding to cultured endothelial cells. The capacity of S. aureus to colonize and invade endovascular surfaces may in part be a consequence of staphylococcal interaction with this endothelial cell membrane protein.

Original languageEnglish (US)
Pages (from-to)1248-1254
Number of pages7
JournalJournal of Clinical Investigation
Issue number4
StatePublished - Apr 1990
Externally publishedYes


  • Adherence
  • Endocarditis
  • Endothelial cells
  • Staphylococcus aureus

ASJC Scopus subject areas

  • Medicine(all)


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