Antigenic analysis of Pseudomonas aeruginosa and Pseudomonas cepacia GroEL proteins and demonstration of a lipopolysaccharide-associated GroEL fraction in P. aeruginosa

P Jensen, A Fomsgaard, G Shand, P Hindersson, N Høiby

Abstract

Quantitative crossed immunoelectrophoresis was used to evaluate the antigenic similarity of Pseudomonas aeruginosa and Pseudomonas cepacia GroEL proteins. We found that the two proteins showed 75% identity. By using a panel of monoclonal antibodies against the P. aeruginosa GroEL protein, we identified 10 monoclonal antibodies which cross-reacted with the P. cepacia GroEL protein and 21 monoclonal antibodies which recognized type-specific epitopes on the P. aeruginosa GroEL protein. In crossed immunoelectrophoresis two different fractions of GroEL reactive material could be resolved. These fractions showed a reaction of partial identity. Examination of the two immunoprecipitates by Western blotting, showed that both fractions consisted of anti-60 kDa GroEL reactive protein. One fraction, in addition, contained LPS with a characteristic 'ladder' reaction in modified Western blotting. We therefore conclude that this fraction represents a complex between LPS and GroEL.

Original languageEnglish
JournalAPMIS - Journal of Pathology, Microbiology and Immunology
Volume101
Issue number8
Pages (from-to)621-30
Number of pages10
ISSN0903-4641
DOIs
Publication statusPublished - Aug 1993
Externally publishedYes

Keywords

  • Antibodies, Monoclonal/analysis
  • Antigens, Bacterial/analysis
  • Bacterial Proteins/analysis
  • Blotting, Western
  • Burkholderia cepacia/chemistry
  • Chaperonin 60
  • Cross Reactions
  • Electrophoresis, Polyacrylamide Gel
  • Epitopes/immunology
  • Heat-Shock Proteins/analysis
  • Humans
  • Immunoelectrophoresis
  • Lipopolysaccharides/metabolism
  • Pseudomonas aeruginosa/chemistry

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