Literature DB >> 6160723

An antigen common to a wide range of bacteria. I. The isolation of a 'common antigen' from Pseudomonas aeruginosa.

D Sompolinsky, J B Hertz, N Høiby, K Jensen, B Mansa, Z Samra.   

Abstract

In crude water-soluble extracts of Pseudomonas aeruginosa 64 antigens can be demonstrated by crossed immunoelectrophoresis in agarose with polyvalent Pseudomonas-immunoglobulin. One of these antigens cross-reacts with antigens prepared from bacteria of a wide range of taxonomic groups. Monospecific immunoglobulins to this antigen (Common Antigen) were produced by immunization with the appropriate immunocomplex extracted from agarose. Common Antigen was purified by the combination of two fractionation methods: Precipitation of the crude extract with 18% (w/v) sodium sulfate, followed by gel filtration of the supernatant on a Sephadex G-200 column. By this method, 35% of Common Antigen from the crude extract was recovered, more than half of the fractions electrophoretically pure. Electrophoresis of reduced Common Antigen on a dodecyl sodium sulfate polyacrylamide gel revealed two protein bands with apparent molecular weights of 59-62 000 and 62-65 000, respectively. The untreated antigen, however, passed a column of Sephadex G-200 with the void volumen, indicating a substance of high molecular weight (> 4-600 000).

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Year:  1980        PMID: 6160723     DOI: 10.1111/j.1699-0463.1980.tb02620.x

Source DB:  PubMed          Journal:  Acta Pathol Microbiol Scand B        ISSN: 0105-0656


  23 in total

1.  Molecular cloning and sequence analysis of the Sta58 major antigen gene of Rickettsia tsutsugamushi: sequence homology and antigenic comparison of Sta58 to the 60-kilodalton family of stress proteins.

Authors:  C K Stover; D P Marana; G A Dasch; E V Oaks
Journal:  Infect Immun       Date:  1990-05       Impact factor: 3.441

2.  Purified 60-kilodalton Legionella protein antigen with Legionella-specific and nonspecific epitopes.

Authors:  B B Plikaytis; G M Carlone; C P Pau; H W Wilkinson
Journal:  J Clin Microbiol       Date:  1987-11       Impact factor: 5.948

3.  The Mycobacterium tuberculosis 65-kilodalton antigen is a heat shock protein which corresponds to common antigen and to the Escherichia coli GroEL protein.

Authors:  T M Shinnick; M H Vodkin; J C Williams
Journal:  Infect Immun       Date:  1988-02       Impact factor: 3.441

4.  A heat shock operon in Coxiella burnetti produces a major antigen homologous to a protein in both mycobacteria and Escherichia coli.

Authors:  M H Vodkin; J C Williams
Journal:  J Bacteriol       Date:  1988-03       Impact factor: 3.490

5.  Immunogenicity of some common thermolabile surface antigens of Escherichia coli.

Authors:  F Orskov; J C Larsen; I Orskov
Journal:  Med Microbiol Immunol       Date:  1981       Impact factor: 3.402

6.  Legionella pneumophila htpAB heat shock operon: nucleotide sequence and expression of the 60-kilodalton antigen in L. pneumophila-infected HeLa cells.

Authors:  P S Hoffman; L Houston; C A Butler
Journal:  Infect Immun       Date:  1990-10       Impact factor: 3.441

7.  Cross-reactive antigens shared by Pseudomonas aeruginosa, Helicobacter pylori, Campylobacter jejuni, and Haemophilus influenzae may cause false-positive titers of antibody to H. pylori.

Authors:  H K Johansen; A Nørgaard; L P Andersen; P Jensen; H Nielsen; N Høiby
Journal:  Clin Diagn Lab Immunol       Date:  1995-03

8.  Identification, immunochemical characterization, and purification of a major lipoprotein antigen associated with the inner (cytoplasmic) membrane of Escherichia coli.

Authors:  H Doherty; H Yamada; P Caffrey; P Owen
Journal:  J Bacteriol       Date:  1986-06       Impact factor: 3.490

9.  Crossed immunoelectrophoretic analysis of anti-Salmonella typhi antibodies in sera of typhoid patients and carriers: demonstration of the presence of typhoid-specific antibodies to a non-O, non-H, non-Vi antigen.

Authors:  P Y Chau; K C Wan; R S Tsang
Journal:  Infect Immun       Date:  1984-03       Impact factor: 3.441

10.  Cloning and sequence of the gene for heat shock protein 60 from Chlamydia trachomatis and immunological reactivity of the protein.

Authors:  M C Cerrone; J J Ma; R S Stephens
Journal:  Infect Immun       Date:  1991-01       Impact factor: 3.441

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