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A mRNA Signal for the Type III Secretion of Yop Proteins by <i>Yersinia enterocolitica</i>
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resolves10.1046/j.1365-2958.1997.2731623.x
The <i>Yersinia</i> Yop virulon: a bacterial system for subverting eukaryotic cells
resolves10.1002/j.1460-2075.1994.tb06341.x
Target cell contact triggers expression and polarized transfer of Yersinia YopE cytotoxin into mammalian cells.
resolves10.1126/science.273.5279.1231
Modulation of Virulence Factor Expression by Pathogen Target Cell Contact
resolves10.1128/jb.173.5.1677-1685.1991
Secretion of hybrid proteins by the Yersinia Yop export system
resolves10.1073/pnas.92.26.11998
Identification of the YopE and YopH domains required for secretion and internalization into the cytosol of macrophages, using the cyaA gene fusion approach.
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GENETIC ANALYSIS OF PROTEIN EXPORT IN <i>ESCHERICHIA COLI</i> K12
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GENETIC ANALYSIS OF PROTEIN EXPORT IN <i>ESCHERICHIA COLI</i>
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Characterization of plasmids and plasmid-associated determinants of Yersinia enterocolitica pathogenesis
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Molecular genetic bases of <i>Salmonella</i> entry into host cells
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Functional conservation of the secretion and translocation machinery for virulence proteins of yersiniae, salmonellae and shigellae.
resolves10.1128/jb.178.24.7227-7233.1996
Delineation and mutational analysis of the Yersinia pseudotuberculosis YopE domains which mediate translocation across bacterial and eukaryotic cellular membranes
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resolves10.1016/0378-1119(87)90365-9
High-copy-number and low-copy-number plasmid vectors for lacZα-complementation and chloramphenicol- or kanamycin-resistance selection
resolves10.1016/0378-1119(82)90023-3
Nucleotide sequence and exact localization of the neomycin phosphotransferase gene from transposon Tn5
resolves10.1073/pnas.85.24.9557
Polarized apical distribution of glycosyl-phosphatidylinositol-anchored proteins in a renal epithelial cell line.
resolves10.1046/j.1365-2958.1997.3831750.x
Two independent type III secretion mechanisms for YopE in <i>Yersinia enterocolitica</i>
The 16 references without a DOI — listed, not checked
no DOI — not checkedBoland A., et al., ibid. 15, 5191 (1996).
no DOI — not checkedYopE was purified from the culture supernatant of Y. enterocolitica O:8 strain 8081 [
no DOI — not checked] by ammonium sulfate precipitation (46%). The precipitate was solubilized in 6 M guanidine hydrochloride 0.05 M phosphate buffer 0.01 M dithiothreitol (pH 7.5) and separated by reversed-phase high-performance liquid chromatography on a C8 column (BDS Hypersil 4.6 mm by 250 mm) with a linear gradient of acetonitrile from 5 to 95% (1%/min) in 0.1% trifluoroacetic acid. The NH 2 -terminal sequence of purified YopE was confirmed by Edman degradation and the molecule was subjected to electrospray ionization mass spectrometry. An average compound mass of 23 018.75 [mass-to-charge ratio ( m/z ) = 1212 1280 1355 1440 1645 1772 1919)] was observed in agreement with a calculated compound mass of 23 016.10 given a standard error rate of 0.01% (±2 daltons).
no DOI — not checkedTwo plasmids were present in Y. enterocolitica W22703: the virulence plasmid (pYV227) and a low–copy number plasmid expressing type III secretion substrates. The yopE and yopN genes were amplified by the polymerase chain reaction (PCR) from virulence plasmid as three separate DNA fragments one containing the promoter and upstream untranslated sequences a middle fragment specifying the open reading frame and a downstream fragment harboring a putative transcriptional terminator. All fragments were assembled as cassettes and inserted into pHSG575 [
no DOI — not checked]. To generate NH 2 - or COOH-terminal fusions we replaced the central Nde I to Bam HI cassette with two fragments joined at a Kpn I site. The npt gene [
no DOI — not checked] was amplified by PCR with abutted Kpn I and Bam HI sites. The YopE and YopN fusions were amplified with flanking Nde I and Kpn I sites. Fusions harboring the first 10 or 15 codons of Yop mRNA were created by annealing oligonucleotides with overlapping ends for cloning between the Nde I and Kpn I sites. All constructs were verified by DNA sequencing.
no DOI — not checkedOvernight cultures of Y. enterocolitica were diluted 1:50 into fresh M9 medium with casamino acids and grown for 2 hours at 26°C before incubation for 3 hours at 37°C. A portion (30 ml) of the induced culture (absorbance at 600 nm of 0.5) was centrifuged at 17 000 g for 13 min and 20 ml of supernatant was removed and precipitated with 5% trichloroacetic acid (TCA). The remainder of the supernatant was discarded and the sedimented material was suspended in water (750 μl). A portion (500 μl) of this suspension was precipitated with ice-cold 10% TCA (500 μl). All TCA precipitates were washed in acetone dissolved in sample buffer and analyzed by immunoblotting with rabbit antiserum. Immunoreactive species were identified as a chemiluminescent signal and quantitated by laser-densitometry scanning of developed x-ray films. Immunoblotting for cytoplasmic chloramphenicol acetyltransferase served as an internal control for correct fractionation of Yersinia cultures.
no DOI — not checkedThe location of pulse-labeled YopE-Npt and YopE 1 – 15 -Npt was investigated with the membrane-impermeable reagent sulfosuccinimidobiotin (Pierce) [
no DOI — not checked]. The amount of fusion protein covalently modified with sulfosuccinimidobiotin was similar to that found to be soluble in the supernatant of centrifuged Yersinia cultures suggesting that nonsecreted polypeptides remained within the bacterial cytosol. This result was confirmed by fractionating Yersinia cultures into medium periplasm cytosol and membrane compartments [
no DOI — not checked] followed by immunoblotting. Similar amounts of fusion proteins were found to be soluble in the culture medium and the bacterial cytosol. Upon ultracentrifugation of cell extracts a small amount of hybrid protein sedimented together with the membranes which may result from its association with the type III secretion machinery.
no DOI — not checkedOvernight cultures of Yersinia were diluted 1:20 into 20 ml of M9 minimal medium grown for 2 hours at 26°C and induced for 3 hours by temperature shift to 37°C. One milliliter of culture was labeled with 100 μCi of Pro-Mix for 1 min and precipitated with ice-cold TCA. The SDS-solubilized samples were immunoprecipitated with antiserum to purified YopH or Npt separated by SDS–polyacrylamide gel electrophoresis and quantified by PhosphorImager.
no DOI — not checkedPortions of induced Yersinia cultures (1.5 ml) were centrifuged and sedimented cells were lysed in 0.1 ml of 1 mM EDTA 5 mg/ml lysozyme. RNA was purified with the RNeasy (Qiagen). Total RNA (10 μg) was separated by formaldehyde-containing agarose gel electrophoresis and transferred to nylon membrane. The filter was hybridized with [ 32 P]cytidine 5′-triphosphate–labeled DNA sequences prepared by random primer labeling of restriction fragments corresponding to the full-length open reading frame of either npt or yopH.
no DOI — not checkedHybrid Npt proteins were purified with a fused COOH-terminal His 6 tag from the supernatant of induced Yersinia cultures. Briefly protein from 1-liter culture supernatant was precipitated with 46% ammonium sulfate collected by centrifugation dissolved and purified by chromatography on nickel-Sepharose. The NH 2 -terminal amino acid sequence was determined by Edman degradation.
no DOI — not checkedW22703 cells [pYV227 pDA54 (YopE 4S – A -Npt)] (2 × 10 10 ) grown in Luria broth (LB) supplemented with chloramphenicol (20 μg/ml) at 28°C were plated on tryptic soy broth (TSB) agar plates containing neomycin (50 μg/ml) chloramphenicol (20 μg/ml) and 5 mM EGTA. After 48 hours of growth at 30°C nitrocellulose filters were placed on the surface of the plates incubated for 30 min at room temperature and probed with antibodies to Npt. Neomycin-resistant revertants arose at a frequency of 10 − 9 and were picked from the plates and patched onto fresh TSB agar supplemented with neomycin chloramphenicol and EGTA. Nitrocellulose filters were placed directly on the colonies and incubated in 1% SDS and lysozyme for 10 min. Colonies that reacted with antibodies to Npt were subsequently analyzed by immunoblotting for secretion of the Npt hybrid. Plasmid was isolated and transformed into W22703 to determine the linkage of the suppressor mutations to this DNA. Mutations were identified by DNA sequencing.
no DOI — not checkedBurd C. G., Dreyfuss G., ibid. 265, 615 (1994).
no DOI — not checkedWe thank S. Daefler M. Russel R. Simons and members of our laboratory for critically reading the manuscript and G. R. Cornelis for the Y. enterocolitica strains. Supported by a grant from the Stein-Oppenheimer Foundation the Department of Microbiology and Immunology (O.S.) and the Microbial Pathogenesis Training grant AI 07323 from the Public Health Service to the Department of Microbiology and Immunology at UCLA School of Medicine (D.M.A).
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