Specific detection of Salmonella typhimurium proteins synthesized intracellularly

Lisa L. Burns-Keliher, Andrew Portteus, Roy Curtiss

Research output: Contribution to journalArticlepeer-review

20 Scopus citations


Studies of the proteins Salmonella typhimurium synthesizes under conditions designed to more closely approximate the in vivo environment, i.e., in cell and tissue culture, are not easily interpreted because they have involved chemical inhibition of host cell protein synthesis during infection. The method which we have developed allows specific labeling of bacterial proteins without interfering with host cell metabolic activities by using a labeled lysine precursor which mammalian cells cannot utilize. We have resolved the labeled proteins using two-dimensional electrophoresis and autofluorography. We were able to detect 57 proteins synthesized by S. typhimurium during growth within a human intestinal epithelial cell line. Of the 57 proteins detected, 34 appear to be unique to the intracellular environment, i.e., they are not seen during growth of the bacteria in tissue culture medium alone. Current (and future) efforts are directed at organizing the 34 proteins into known stress response groups, determining the cellular locations of the proteins (outer or inner membrane, etc.), and comparing the pattern of proteins synthesized within an intestinal epithelial cell to the pattern synthesized during growth within other tissues.

Original languageEnglish (US)
Pages (from-to)3604-3612
Number of pages9
JournalJournal of bacteriology
Issue number11
StatePublished - Jun 1997
Externally publishedYes

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology


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