Phosphatase activity is a constant feature of all isolates of all major species of the family Enterobacteriaceae.Satta, G; Pompei, R; Grazi, G; Cornaglia, G
doi: N/Apmid: 2466048
In this study we evaluated phosphatase activity in members of the family Enterobacteriaceae by conventional methods and by a novel method. The novel method is based on the formation of bright-green-strained colonies by phosphatase-positive, but not phosphatase-negative, strains in the presence of a phosphate substrate, such as phenolphthalein monophosphate or 6-benzoylnaphthyl phosphate (6-BNP), and methyl green. A total of 1,055 strains belonging to 65 different species of Enterobacteriaceae were tested for green staining of the colonies in the presence of methyl green and either phenolphthalein monophosphate or 6-BNP and for phosphatase activity by three different conventional methods. With the sole exception of one Leminorella richardii type strain, all isolates of all of the species formed green-stained colonies in the presence of the substrate 6-BNP. All strains were phosphatase positive by all of the conventional methods. J Clin Microbiol. 1988 December; 26(12): 2637-2641
Comparison between radioimmunoassay and direct and indirect enzyme-linked immunosorbent assays for determination of antibodies against Haemophilus influenzae type b capsular polysaccharide.Lagergård, T; Trollfors, B; Claesson, B A; Schneerson, R; Robbins, J B
doi: N/Apmid: 3230133
Comparison between radioimmunoassay and direct and indirect enzyme-linked immunosorbent assays for determination of antibodies against Haemophilus influenzae type b capsular polysaccharide. T Lagergård , B Trollfors , B A Claesson , R Schneerson and J B Robbins Department of Medical Microbiology, University of Göteborg, Sweden. ABSTRACT Levels of antibodies against Haemophilus influenzae type b capsular polysaccharide were determined in acute-phase and convalescent-phase serum samples obtained from 21 children with invasive H. influenzae type b infections and from 44 children vaccinated with two H. influenzae type b vaccines. Amounts of immunoglobulin G (IgG), IgM, and IgA antibodies were measured by direct and indirect enzyme-linked immunosorbent assay (ELISA), and the total amount of antibodies was measured by radioimmunoassay (RIA). Results obtained by ELISA were calculated by multiple-point parallel-line comparison and by endpoint analysis. A very good correlation was obtained between direct and indirect ELISA values. In the lower range of antibody concentrations, the correlation between ELISA values obtained by endpoint analysis and those obtained by multiple-point parallel-line comparison was poor, since the latter method of calculation yielded values of up to 1 microgram/ml in sera that were negative according to endpoint analysis. These sera with negative endpoint titers also had undetectable or very low antibody concentrations as measured by RIA. Consistent with this finding, in acute-phase and prevaccination sera with undetectable or low antibody concentrations as measured by RIA, ELISA values calculated by multiple-point parallel-line comparison were much higher. In sera with higher antibody concentrations, however, parallel-line comparisons showed good correlation between RIA and ELISA values. Although no reference method for measuring true antibody concentrations is available, ELISA values as calculated by multiple-point parallel-line comparison appear to overestimate antibody concentrations in sera containing low antibody concentrations, whereas ELISA values obtained by endpoint analysis are less well correlated with RIA values at higher concentrations. CiteULike Connotea Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter What's this? « Previous | Next Article » Table of Contents This Article J. Clin. Microbiol. December 1988 vol. 26 no. 12 2554-2557 » Abstract PDF Classifications Research Article Services Email this article to a colleague Similar articles in ASM journals Alert me when this article is cited Alert me if a correction is posted Similar articles in this journal Similar articles in Web of Science Similar articles in PubMed Alert me to new issues of JCM Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Load citing article information Citing articles via Web of Science Citing articles via Google Scholar Google Scholar Articles by Lagergård, T. Articles by Robbins, J. B. Search for related content PubMed PubMed citation Articles by Lagergård, T. Articles by Robbins, J. B. Related Content Load related web page information Social Bookmarking CiteULike Connotea Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter What's this? current issue December 2011, volume 49, issue 12 Alert me to new issues of JCM About JCM Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JCM RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • [email protected] Print ISSN: 0095-1137 Online ISSN: 1098-660X Copyright © 2011 by the American Society for Microbiology. For an alternate route to JCM .asm.org, visit: http://intl- JCM .asm.org | More Info»
Recognition of mycobacterial antigens by sera from patients with leprosy.Vega-Lopez, F; Stoker, N G; Locniskar, M F; Dockrell, H M; Grant, K A; McAdam, K P
doi: N/Apmid: 3068245
Recognition of mycobacterial antigens by sera from patients with leprosy. F Vega-Lopez , N G Stoker , M F Locniskar , H M Dockrell , K A Grant and K P McAdam Department of Clinical Sciences, London School of Hygiene and Tropical Medicine, England. ABSTRACT Mycobacterium leprae sonic extracts prepared from armadillo-derived bacteria were subjected to sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Western blotting (immunoblotting) procedures and probed with serum or plasma samples from 20 patients with lepromatous leprosy and 14 healthy endemic controls. Five proteins of 33, 25, 18, 15, and 12 kilodaltons (kDa) were frequently recognized; the 33- and 15-kDa proteins were, respectively, recognized with high intensity by 16 and 13 of the 20 samples from patients with leprosy, whereas only one healthy donor had antibodies that recognized the 15-kDa protein. By the use of M. leprae-specific murine monoclonal antibodies it was demonstrated that the 33-, 25-, and 15-kDa antigens were different from those bound by the available murine monoclonal antibodies. The 18- and 12-kDa proteins detected had molecular masses similar to those detected by the corresponding murine monoclonal antibodies. The serum and plasma samples from patients with leprosy were also used to probe Western blots of a soluble extract of M. tuberculosis. They recognized, among others, antigens with molecular weights similar to those detected in the M. leprae antigenic preparations, although with less intensity and at a lower frequency. CiteULike Connotea Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter What's this? « Previous | Next Article » Table of Contents This Article J. Clin. Microbiol. December 1988 vol. 26 no. 12 2474-2479 » Abstract PDF Classifications Research Article Services Email this article to a colleague Similar articles in ASM journals Alert me when this article is cited Alert me if a correction is posted Similar articles in this journal Similar articles in Web of Science Similar articles in PubMed Alert me to new issues of JCM Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Load citing article information Citing articles via Web of Science Citing articles via Google Scholar Google Scholar Articles by Vega-Lopez, F. Articles by McAdam, K. P. Search for related content PubMed PubMed citation Articles by Vega-Lopez, F. Articles by McAdam, K. P. Related Content Load related web page information Social Bookmarking CiteULike Connotea Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter What's this? current issue December 2011, volume 49, issue 12 Alert me to new issues of JCM About JCM Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JCM RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • [email protected] Print ISSN: 0095-1137 Online ISSN: 1098-660X Copyright © 2011 by the American Society for Microbiology. For an alternate route to JCM .asm.org, visit: http://intl- JCM .asm.org | More Info»
Monoclonal antibodies to Mokola virus for identification of rabies and rabies-related viruses.Bussereau, F; Vincent, J; Coudrier, D; Sureau, P
doi: N/Apmid: 3068246
Rabies and rabies-related virus strains were studied by using a panel of monoclonal antibodies directed against either nucleocapsid proteins or cell surface antigens of Mokola virus (Mok-3). Each strain was used in parallel to infect cultured cells and mice. Then, the patterns of reactivity of the different monoclonal antibodies were determined by the immunofluorescent-antibody staining procedure. On cells, the monoclonal antibodies differentiated fixed rabies virus strains (serotype 1) from rabies-related virus strains. The seven fixed strains (CVS, PV4, PM, Flury LEP and HEP, ERA, and SAD) reacted identically. The previous serotype groupings (serotype 2, Lagos-bat virus; serotype 3, Mokola virus; serotype 4, Duvenhage virus) established with anti-rabies monoclonal antibodies were confirmed, except for that of Lagos-bat Kindia, which appeared to be related to the African subtype of the Duvenhage serotype (Duv-2). Within the Mokola (Mok-1, -2, -3, and -5 and Umhlanga) and the Lagos-bat (Lag-1 and -2, Zimbabwe, Pinetown, and Dakar) serotypes, each strain appeared to be distinct. The African subtype of the Duvenhage serotype reacted differently from the European subtype. Within the Duvenhage serotype, subtypes Duv-4, -5, and -6 and Denmark reacted identically, while subtypes Duv-1, -2, and -3 and German Democratic Republic appeared to be distinct. The monoclonal antibodies specific for the cell surface antigens were also used in neutralization tests with all the strains. Two of them neutralized the infectivity of Mokola virus. J Clin Microbiol. 1988 December; 26(12): 2489-2494
Monoclonal antibodies to Mokola virus for identification of rabies and rabies-related viruses.Bussereau, F; Vincent, J; Coudrier, D; Sureau, P
doi: N/Apmid: 3068246
Monoclonal antibodies to Mokola virus for identification of rabies and rabies-related viruses. F Bussereau , J Vincent , D Coudrier and P Sureau Unité Rage, Institut Pasteur, Paris, France. ABSTRACT Rabies and rabies-related virus strains were studied by using a panel of monoclonal antibodies directed against either nucleocapsid proteins or cell surface antigens of Mokola virus (Mok-3). Each strain was used in parallel to infect cultured cells and mice. Then, the patterns of reactivity of the different monoclonal antibodies were determined by the immunofluorescent-antibody staining procedure. On cells, the monoclonal antibodies differentiated fixed rabies virus strains (serotype 1) from rabies-related virus strains. The seven fixed strains (CVS, PV4, PM, Flury LEP and HEP, ERA, and SAD) reacted identically. The previous serotype groupings (serotype 2, Lagos-bat virus; serotype 3, Mokola virus; serotype 4, Duvenhage virus) established with anti-rabies monoclonal antibodies were confirmed, except for that of Lagos-bat Kindia, which appeared to be related to the African subtype of the Duvenhage serotype (Duv-2). Within the Mokola (Mok-1, -2, -3, and -5 and Umhlanga) and the Lagos-bat (Lag-1 and -2, Zimbabwe, Pinetown, and Dakar) serotypes, each strain appeared to be distinct. The African subtype of the Duvenhage serotype reacted differently from the European subtype. Within the Duvenhage serotype, subtypes Duv-4, -5, and -6 and Denmark reacted identically, while subtypes Duv-1, -2, and -3 and German Democratic Republic appeared to be distinct. The monoclonal antibodies specific for the cell surface antigens were also used in neutralization tests with all the strains. Two of them neutralized the infectivity of Mokola virus. CiteULike Connotea Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter What's this? « Previous | Next Article » Table of Contents This Article J. Clin. Microbiol. December 1988 vol. 26 no. 12 2489-2494 » Abstract PDF Classifications Research Article Services Email this article to a colleague Similar articles in ASM journals Alert me when this article is cited Alert me if a correction is posted Similar articles in this journal Similar articles in Web of Science Similar articles in PubMed Alert me to new issues of JCM Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Load citing article information Citing articles via Web of Science Citing articles via Google Scholar Google Scholar Articles by Bussereau, F. Articles by Sureau, P. Search for related content PubMed PubMed citation Articles by Bussereau, F. Articles by Sureau, P. Related Content Load related web page information Social Bookmarking CiteULike Connotea Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter What's this? current issue December 2011, volume 49, issue 12 Alert me to new issues of JCM About JCM Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JCM RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • [email protected] Print ISSN: 0095-1137 Online ISSN: 1098-660X Copyright © 2011 by the American Society for Microbiology. For an alternate route to JCM .asm.org, visit: http://intl- JCM .asm.org | More Info»
Improved Syva MicroTrak Chlamydia trachomatis direct test method.Judson, B A; Lambert, P P
doi: N/Apmid: 3230139
Improved Syva MicroTrak Chlamydia trachomatis direct test method. B A Judson and P P Lambert Infectious Diseases Division, Syva Company, Palo Alto, California 94304. ABSTRACT Recent changes in the MicroTrak Chlamydia trachomatis Direct Specimen Test (Syva Company, Palo Alto, Calif.) have led to improved product performance. The use of the recommended cervical cytology brush can significantly increase the number of endocervical cells collected, and fixation with methanol increases the intensity of elementary-body staining in many specimens. CiteULike Connotea Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter What's this? « Previous | Next Article » Table of Contents This Article J. Clin. Microbiol. December 1988 vol. 26 no. 12 2657-2658 » Abstract PDF Classifications Research Article Services Email this article to a colleague Similar articles in ASM journals Alert me when this article is cited Alert me if a correction is posted Similar articles in this journal Similar articles in Web of Science Similar articles in PubMed Alert me to new issues of JCM Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Load citing article information Citing articles via Web of Science Citing articles via Google Scholar Google Scholar Articles by Judson, B. A. Articles by Lambert, P. P. Search for related content PubMed PubMed citation Articles by Judson, B. A. Articles by Lambert, P. P. Related Content Load related web page information Social Bookmarking CiteULike Connotea Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter What's this? current issue December 2011, volume 49, issue 12 Alert me to new issues of JCM About JCM Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JCM RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • [email protected] Print ISSN: 0095-1137 Online ISSN: 1098-660X Copyright © 2011 by the American Society for Microbiology. For an alternate route to JCM .asm.org, visit: http://intl- JCM .asm.org | More Info»
Enzyme-linked immunosorbent fluorescence assay and high-pressure liquid chromatography for analysis of humoral immune responses to Coxiella burnetti proteins.Schmeer, N; Muller, H P; Baumgartner, W; Wieda, J; Krauss, H
doi: N/Apmid: 3068247
A microtiter enzyme-linked immunosorbent fluorescence assay based on alkaline phosphatase conjugate and 4-methylumbelliferyl phosphate as fluorogenic substrate was developed and adapted to quantitatively analyze immunoglobulin G subclass 1 (IgG1) and IgG2 responses of vaccinated and infected cattle to proteins of Coxiella burnetii. The enzyme-linked immunosorbent fluorescence assay surpassed the conventional enzyme-linked immunosorbent assay with a 50-fold-higher sensitivity and a broader range of linear dose-response signals. Antigens of C. burnetii were purified by sodium dodecyl sulfate extraction and molecular-sieve high-pressure liquid chromatography. The purified 14-, 27-, and 30-kilodalton proteins were used as antigens without any further treatment. Vaccination with either chloroform-methanol-extracted cell residues of C. burnetii or the 27-kilodalton major surface protein evoked an early IgG2 response to the 27-kilodalton protein (2 weeks after immunization), whereas IgG2 to lipopolysaccharides of C. burnetii was detected only in the late phase (13 weeks after immunization). These results may have implications for the serodiagnosis of acute and chronic Q fever. IgG1 against these antigens was induced solely by naturally occurring C. burnetii infections, indicating that infected cattle can be distinguished from vaccinated cattle by using the enzyme-linked immunosorbent fluorescence assay and SP27 antigen. J Clin Microbiol. 1988 December; 26(12): 2520-2525