Abstract
S. Sawada and co-workers reported that a monoclonal antibody (MAb), E87, interacted with about 80% of Pseudomonas aeruginosa isolates, and they separated a rhamnose-rich polysaccharide as the probable antigen for MAb E87 from P. aeruginosa IFO 3080 (S. Sawada, T. Kawamura, Y. Masuho, and K. Tomibe, J. Infec. Dis. 152:1290-1299, 1985). In the present study, the rhamnose-rich polysaccharide was shown to be structurally and immunologically identical to the D-rhamnan of P. aeruginosa IID 1008 (S. Yokota, S. Kaya, S. Sawada, T. Kawamura, Y. Araki, and E. Ito, Eur. J. Biochem. 167:203-209, 1987). Furthermore, a set of enzymes responsible for the formation of GDP-rhamnose (probably in a D-form) from GDP-D-mannose was found in the 100,000 x g supernatant fractions obtained from all of nine P. aeruginosa strains reactive against MAb E87. The result strongly supports a possibility that lipopolysaccharides having a D-rhamnan chain widely occur as the common antigen among various P. aeruginosa isolates.
MeSH Terms
Antibodies, Monoclonal/immunology
Antigens, Bacterial/analysis
Deoxy Sugars/analysis
Enzyme-Linked Immunosorbent Assay
Magnetic Resonance Spectroscopy
Mannans/analysis
Polysaccharides, Bacterial/analysis,immunology
Pseudomonas aeruginosa/immunology
Chemicals
Antibodies, Monoclonal
Antigens, Bacterial
Deoxy Sugars
Mannans
Polysaccharides, Bacterial
rhamnan
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Yokota S
Department of Chemistry, Faculty of Science, Hokkaido University, Sapporo, Japan.
Kaya S
Araki Y
Ito E
Kawamura T
Sawada S
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