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  • American Society for Microbiology  (4,492)
  • 1990-1994  (4,492)
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  • American Society for Microbiology  (4,492)
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  • 1990-1994  (4,492)
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  • 1
    Online Resource
    Online Resource
    Transferrin and lactoferrin undergo proteolytic cleavage in the Pseudomonas aeruginosa-infected lungs of patients with cystic fibrosis
    American Society for Microbiology ; 1993
    In:  Infection and Immunity Vol. 61, No. 12 ( 1993-12), p. 5049-5055
    Details
    In: Infection and Immunity, American Society for Microbiology, Vol. 61, No. 12 ( 1993-12), p. 5049-5055
    Abstract: Bacterium- and neutrophil-derived proteases have been suggested to contribute to tissue injury at sites of Pseudomonas aeruginosa infection. Pseudomonas elastase cleavage of transferrin enhances in vitro iron removal from this protein by the P. aeruginosa siderophore pyoverdin. This cleavage also generates new iron chelates which, in contrast to iron bound to transferrin, are able to catalyze formation of the highly cytotoxic hydroxyl radical from neutrophil-derived superoxide and hydrogen peroxide via the Haber-Weiss reaction. In order to determine whether this cleavage occurs in vivo, a chemiluminescence immunoblot system was developed to detect the presence of proteolysis products of transferrin or the related iron-binding protein, lactoferrin. Using this immunoblot system, we detected transferrin and lactoferrin cleavage products in bronchoalveolar lavage (BAL) samples from 21 of 22 and 20 of 21 cystic fibrosis (CF) patients, respectively. Three of eleven and two of nine BAL samples from individuals with other forms of chronic inflammatory lung disease had transferrin and lactoferrin cleavage products, respectively. Each patient in whom such products were detected was also infected with P. aeruginosa. No such products were detected in normal individuals. In the CF patients, there was no clear correlation between the extent of transferrin or lactoferrin cleavage and BAL neutrophil or P. aeruginosa concentration or the disease status of the patient. In contrast, in the non-CF patients with chronic inflammatory lung disease, transferrin and lactoferrin cleavage products were detected only in those BAL samples which contained the greatest concentration of both neutrophils and P. aeruginosa. These data provide evidence that P. aeruginosa- and/or human-derived protease cleavage of transferrin and lactoferrin occurs in vivo in the airways of individuals with CF and other forms of chronic lung disease, suggesting that this process could contribute to P. aeruginosa-associated lung injury in these patients.
    Type of Medium: Online Resource
    ISSN: 0019-9567 , 1098-5522
    URL: Article
    DOI: 10.1128/iai.61.12.5049-5055.1993
    RVK:
    XA 10000
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1993
    detail.hit.zdb_id: 1483247-1
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  • 2
    Online Resource
    Online Resource
    Cloning, expression, and occurrence of the Brucella Cu-Zn superoxide dismutase
    American Society for Microbiology ; 1990
    In:  Infection and Immunity Vol. 58, No. 9 ( 1990-09), p. 2935-2939
    Details
    In: Infection and Immunity, American Society for Microbiology, Vol. 58, No. 9 ( 1990-09), p. 2935-2939
    Abstract: Recently, the complete amino acid sequence of a protein expressed in Escherichia coli from cloned Brucella abortus DNA was reported. On the basis of amino acid homology, this protein was identified as a copper-zinc superoxide dismutase (Cu-Zn SOD) (B. L. Beck, L. B. Tabatabai, and J. E. Mayfield, Biochemistry 29:372-376, 1990). We demonstrate in this paper that the sequenced protein is the same as the previously studied salt-extractable protein BCSP20. The plasmid-encoded protein expressed from recombinant E. coli is identical to the Brucella-derived BCSP20 in molecular mass, N-terminal amino acid sequence, and cross-reactivity with homologous and heterologous rabbit sera against either the recombinant gene product or the Brucella-derived protein. A survey of the expression of the Cu-Zn SOD protein in Brucella biovars representing all species was done by Western blotting (immunoblotting) using antisera raised against the recombinant E. coli-derived protein. With the exception of B. neotomae and B. suis biovar 2, the Cu-Zn SOD protein was detectable in all Brucella species and biovars tested, including eight biovars of B. abortus.
    Type of Medium: Online Resource
    ISSN: 0019-9567 , 1098-5522
    URL: Article
    DOI: 10.1128/iai.58.9.2935-2939.1990
    RVK:
    XA 10000
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1990
    detail.hit.zdb_id: 1483247-1
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  • 3
    Online Resource
    Online Resource
    Development and application of an enzyme immunoassay for coronavirus OC43 antibody in acute respiratory illness
    American Society for Microbiology ; 1994
    In:  Journal of Clinical Microbiology Vol. 32, No. 10 ( 1994-10), p. 2372-2376
    Details
    In: Journal of Clinical Microbiology, American Society for Microbiology, Vol. 32, No. 10 ( 1994-10), p. 2372-2376
    Abstract: Study of coronavirus OC43 infections has been limited because of the lack of sensitive cell culture systems and serologic assays. To improve this circumstance, we developed an indirect enzyme immunoassay (EIA) to detect serum antibody to OC43. Antigen (100 ng) prepared by polyethylene glycol precipitation provided optimal results without a postcoat procedure. Evaluation of intraplate variation indicated that a 〉 or = 2.5-fold increase in serum titer was significant. Sixteen of 18 (89%) paired serum samples with previously identified, reproducible increases in the level of hemagglutination inhibition (HAI) antibody to OC43 also showed significant increases as detected by EIA. Specificity for the EIA was established with paired sera obtained from persons given influenza immunizations or experiencing a respiratory infection. No rise in antibody titers occurred among 33 persons with documented coronavirus 229E infection. EIA was then performed on each of 419 paired serum samples from ambulatory chronic obstructive pulmonary disease patients and healthy older adults, from asthmatic adults presenting for emergency room treatment, and from persons hospitalized with acute respiratory symptoms. Twenty-three antibody rises to OC43 were detected; only nine of these were detected by the HAI test, and the HAI test did not detect any increases in antibody titers that were not detected by EIA. Nineteen of 25 coronavirus OC43 infections for which a month of infection could be assigned occurred between November and February. Overall, 4.4% of acute respiratory illnesses in the studied populations were associated with a coronavirus OC43 infection.
    Type of Medium: Online Resource
    ISSN: 0095-1137 , 1098-660X
    URL: Article
    DOI: 10.1128/jcm.32.10.2372-2376.1994
    RVK:
    XA 10000
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1994
    detail.hit.zdb_id: 1498353-9
    SSG: 12
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  • 4
    Online Resource
    Online Resource
    Identification of viral determinants of macrophage tropism for simian immunodeficiency virus SIVmac
    American Society for Microbiology ; 1991
    In:  Journal of Virology Vol. 65, No. 11 ( 1991-11), p. 5798-5805
    Details
    In: Journal of Virology, American Society for Microbiology, Vol. 65, No. 11 ( 1991-11), p. 5798-5805
    Abstract: Simian immunodeficiency virus (SIV), a lymphocytopathic lentivirus, induces an AIDS-like disease in rhesus macaques (Macaca mulatta). A pathogenic molecular clone of rhesus macaque SIV (SIVmac), SIVmac-239, replicates and induces cytopathology in T lymphocytes but is restricted for replication in macrophages. In contrast, a nonpathogenic molecular clone of SIVmac, SIVmac-1A11, replicates and induces syncytia (multinucleated giant cells) in cultures of both T lymphocytes and macrophages. SIVmac-1A11 does not cause disease in macaques. To map the viral determinants of macrophage tropism, reciprocal recombinant genomes were constructed between molecular clones of SIVmac-239 and SIVmac-1A11. Infectious recombinant viruses were rescued by transfection of cloned viral genomes into permissive lymphoid cells. Analysis of one pair of reciprocal recombinants revealed that an internal 6.2-kb DNA fragment of SIVmac-1A11 was necessary and sufficient for both syncytium formation and efficient replication in macrophages. This region includes the coding sequences for a portion of the gag gene, all of the pol, vif, vpr, and vpx genes, the first coding exons of tat and rev, and the external env glycoprotein gp130. Thus, the transmembrane glycoprotein of env, the nef gene, the second coding exons of tat and rev, and the long terminal repeats are not essential for in vitro macrophage tropism. Analysis of additional recombinants revealed that syncytium formation, but not virus production, was controlled by a 1.4-kb viral DNA fragment in SIVmac-1A11 encoding only the external env glycoprotein gp130. Thus, gp130 env of SIVmac-1A11 is necessary for entry of virus into macrophages but is not sufficient for a complete viral replication cycle in this cell type. We therefore conclude that gp130 env and one or more genetic elements (exclusive of the long terminal repeats, transmembrane glycoprotein of env, and second coding exons of tat and rev, and nef) are essential for a complete replication cycle of SIVmac in rhesus macaque macrophages.
    Type of Medium: Online Resource
    ISSN: 0022-538X , 1098-5514
    URL: Article
    DOI: 10.1128/jvi.65.11.5798-5805.1991
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1991
    detail.hit.zdb_id: 1495529-5
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  • 5
    Online Resource
    Online Resource
    Repression of bovine papillomavirus type 1 transcription by the E1 replication protein
    American Society for Microbiology ; 1993
    In:  Journal of Virology Vol. 67, No. 9 ( 1993-09), p. 5079-5087
    Details
    In: Journal of Virology, American Society for Microbiology, Vol. 67, No. 9 ( 1993-09), p. 5079-5087
    Abstract: Bovine papillomavirus type 1 (BPV-1) is the prototype virus for the study of papillomavirus gene regulation. The functions of the BPV-1 E2 proteins in transcriptional regulation have been well characterized. The BPV-1 E1 protein is required for viral DNA replication and can bind to the origin of replication alone or in a complex with the E2 transactivator protein. In this study, we demonstrated that the BPV-1 E1 protein is also involved in transcriptional regulation. The E1 protein significantly repressed E2-transactivated transcription from the major early promoter P89. This activity is consistent with the elevated level of P89 transcription observed in BPV-1 E1 open reading frame mutants. Transcriptional repression by E1 correlated with the ability of an E1-E2 protein complex to bind the replication origin but was not dependent on viral DNA replication. These studies identify a new mechanism involved in the regulation of papillomavirus transcription which has implications regarding expression of the viral transforming functions.
    Type of Medium: Online Resource
    ISSN: 0022-538X , 1098-5514
    URL: Article
    DOI: 10.1128/jvi.67.9.5079-5087.1993
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1993
    detail.hit.zdb_id: 1495529-5
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  • 6
    Online Resource
    Online Resource
    Safety and pharmacokinetics of rimantadine small-particle aerosol
    American Society for Microbiology ; 1990
    In:  Antimicrobial Agents and Chemotherapy Vol. 34, No. 11 ( 1990-11), p. 2228-2233
    Details
    In: Antimicrobial Agents and Chemotherapy, American Society for Microbiology, Vol. 34, No. 11 ( 1990-11), p. 2228-2233
    Abstract: The safety and pharmacokinetics of rimantadine administered by small-particle aerosol were assessed in healthy adults and adults with acute influenza virus infection. Aerosolized rimantadine delivered at a concentration of 40 micrograms/liter of air was associated with nasal burning and irritation in normal volunteers. A concentration of 20 micrograms/liter of air was well tolerated for up to 12 h by normal volunteers and was not associated with any changes in pulmonary function, as measured by routine spirometry, plethysmography, or diffusion capacity of carbon monoxide. Mean peak levels of drug in serum were approximately 10-fold lower after 12 h of aerosol administration than they were after oral administration of 200 mg (29.7 versus 255 ng/ml, respectively), while mean nasal wash levels were approximately 100-fold higher (6,650 versus 66.6 ng/ml, respectively). Elimination half-lives were similar after both aerosol and oral administration (24.1 and 25.2 h, respectively), and rimantadine urinary excretion was less than 1% per 24 h in both groups. Twenty micrograms of aerosolized rimantadine per liter of air given 12 h daily for 3 days to nine adults with acute influenza virus infection was well tolerated. Levels in plasma after 12 h of aerosol inhalation were similar to those in normal volunteers, but were higher at the end of the third treatment than they were at the end of the first treatment (88.3 versus 47.9 ng/ml, respectively). Thus, rimantadine delivered via small-particle aerosol at a dose of 20 micrograms/liter of air was well tolerated in normal volunteers and in those with acute influenza and was associated with high local concentrations.
    Type of Medium: Online Resource
    ISSN: 0066-4804 , 1098-6596
    URL: Article
    DOI: 10.1128/AAC.34.11.2228
    RVK:
    XA 24552
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1990
    detail.hit.zdb_id: 1496156-8
    SSG: 12
    SSG: 15,3
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  • 7
    Online Resource
    Online Resource
    Isolation and characterization of insertion sequence elements from gram-negative bacteria by using new broad-host-range, positive selection vectors
    American Society for Microbiology ; 1991
    In:  Journal of Bacteriology Vol. 173, No. 4 ( 1991-02), p. 1502-1508
    Details
    In: Journal of Bacteriology, American Society for Microbiology, Vol. 173, No. 4 ( 1991-02), p. 1502-1508
    Abstract: On the basis of an RSF1010-derived broad-host-range vector, three different systems which enable positive detection and isolation of insertion sequence (IS) elements from gram-negative bacteria were constructed. Vectors pSUP104-pheS, pSUP104-rpsL, and pSUP104-sac were used successfully in a number of Rhizobium strains and in Xanthomonas campestris. More than 20 different IS elements were isolated and characterized. The 16 IS elements from Rhizobium meliloti were further used to characterize various R. meliloti strains by hybridization. The resulting hybridization patterns were different for every strain and gave a clear and definite IS fingerprint of each strain. These IS fingerprints can be used to identify and characterize R. meliloti strains rapidly and unequivocally, as they proved to be relatively stable. Some of the IS elements were found to be identical when the IS fingerprints from a given strain were compared. This method of IS fingerprinting can also establish whether IS elements are the same, related, or different.
    Type of Medium: Online Resource
    ISSN: 0021-9193 , 1098-5530
    URL: Article
    DOI: 10.1128/jb.173.4.1502-1508.1991
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1991
    detail.hit.zdb_id: 1481988-0
    SSG: 12
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  • 8
    Online Resource
    Online Resource
    Evidence for a methylation-blocking factor (mbf) locus involved in pap pilus expression and phase variation in Escherichia coli
    American Society for Microbiology ; 1991
    In:  Journal of Bacteriology Vol. 173, No. 5 ( 1991-03), p. 1789-1800
    Details
    In: Journal of Bacteriology, American Society for Microbiology, Vol. 173, No. 5 ( 1991-03), p. 1789-1800
    Abstract: Transcription of the pyelonephritis-associated pilus (pap) operon of Escherichia coli is subject to regulation by a phase variation control mechanism in which the pap pilin gene alternates between transcriptionally active (phase-on) and inactive (phase-off) states. Pap phase variation appears to involve differential inhibition of deoxyadenosine methylase (Dam) methylation of two pap GATC sites, GATC1028 and GATC1130, located in the regulatory region upstream of the papBA promoter. DNA from phase-on cells contains an unmethylated adenosine in the GATC1028 site, whereas DNA from phase-off cells contains an unmethylated adenosine in the GATC1130 site. papI and papB are two regulatory genes in the pap operon. Analysis of pap deletion mutants suggests that papI is required for methylation inhibition at the GATC1028 site; however, neither papI nor papB is required for inhibition of methylation at the GATC1130 site. We have identified a chromosomal locus, mbf (methylation-blocking factor), that is required for methylation protection of both the pap GATC1028 and GATC1130 sites. The mbf locus was identified after transposon mTn10 mutagenesis and mapped to 19.6 min on the E. coli chromosome. The effect of transposon mutations within mbf on pap pilin transcription was determined by using a papBAp-lac operon fusion which places lacZ under control of the papBA promoter. E. coli containing mbf::mTn10 and phase-off mbf+ E. coli cells both expressed beta-galactosidase levels about 30-fold lower than the beta-galactosidase level measured for phase-on mbf+ E. coli cells. These results indicated that mbf was necessary for pap pilin transcription and were supported by Northern (RNA) blotting and primer extension analyses. Moreover, transposon insertion within mbf greatly reduced Pap pilus expression. The mbf locus was isolated on a low-copy-number cosmid, pMBF1. Complementation analysis indicated that each of seven mbf::mTn10 mutants isolated contained a transposon insertion within the same gene or operon. The identification of the mbf locus, required for pap transcription, supports the hypothesis that pap phase variation is controlled by a mechanism involving alternation between different methylation states.
    Type of Medium: Online Resource
    ISSN: 0021-9193 , 1098-5530
    URL: Article
    DOI: 10.1128/jb.173.5.1789-1800.1991
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1991
    detail.hit.zdb_id: 1481988-0
    SSG: 12
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  • 9
    Online Resource
    Online Resource
    In vivo induction of nitrite and nitrate by tumor necrosis factor, lymphotoxin, and interleukin-1: possible roles in malaria
    American Society for Microbiology ; 1992
    In:  Infection and Immunity Vol. 60, No. 9 ( 1992-09), p. 3725-3730
    Details
    In: Infection and Immunity, American Society for Microbiology, Vol. 60, No. 9 ( 1992-09), p. 3725-3730
    Abstract: Tumor necrosis factor and related cytokines are thought to be implicated in cell-mediated immunity and pathophysiology in malaria, but their mechanism of action has not been ascertained. Tumor necrosis factor has been reported to generate nitric oxide in vitro, so we have measured levels of this molecule and its products in the plasma of mice after they have received an injection of tumor necrosis factor, lymphotoxin, interleukin-1, gamma interferon, or interleukin-6, all of which have been reported to be increased in malaria. Total reactive nitrogen intermediate levels in plasma were assayed spectrophotometrically after exposing plasma to a copper-cadmium-zinc catalyst to convert nitrate to nitrite and then to Griess reagent. Tumor necrosis factor, lymphotoxin, and interleukin-1 all induced reactive nitrogen intermediates in vivo, with interleukin-1 showing the most activity. Tumor necrosis factor was then examined more closely. It induced more reactive nitrogen intermediates in malaria-infected mice than in normal mice, and appreciably more was in the form of nitrate than was in the form of nitrite. NG-methyl-L-arginine inhibited the in vivo generation of reactive nitrogen intermediates by tumor necrosis factor in a dose-dependent manner, implying that these molecules were arginine derived. These results are consistent with the possibility that tumor necrosis factor, lymphotoxin, and interleukin-1 may contribute to host pathology and parasite suppression through generation of nitric oxide.
    Type of Medium: Online Resource
    ISSN: 0019-9567 , 1098-5522
    URL: Article
    DOI: 10.1128/iai.60.9.3725-3730.1992
    RVK:
    XA 10000
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1992
    detail.hit.zdb_id: 1483247-1
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  • 10
    Online Resource
    Online Resource
    Revised nucleotide sequence of the gltP gene, which encodes the proton-glutamate-aspartate transport protein of Escherichia coli K-12
    American Society for Microbiology ; 1992
    In:  Journal of Bacteriology Vol. 174, No. 7 ( 1992-04), p. 2391-2393
    Details
    In: Journal of Bacteriology, American Society for Microbiology, Vol. 174, No. 7 ( 1992-04), p. 2391-2393
    Abstract: The gene encoding the proton-glutamate carrier (GltP) of Escherichia coli K-12 was sequenced, and the primary structure of the protein was analyzed. The nucleotide sequence was found to differ in several aspects from the previously published sequence (B. Wallace, Y. Yang, J. Hong, and D. Lum, J. Bacteriol. 172:3214-3220, 1990). The corrected open reading frame encodes a protein of 437 (instead of 395) amino acids. Hydropathy analysis predicts 12 membrane-spanning alpha-helical regions. The complementary strand does contain an open reading frame possibly encoding a highly hydrophilic polypeptide of 272 amino acids.
    Type of Medium: Online Resource
    ISSN: 0021-9193 , 1098-5530
    URL: Article
    DOI: 10.1128/jb.174.7.2391-2393.1992
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1992
    detail.hit.zdb_id: 1481988-0
    SSG: 12
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