AI Article Synopsis
- OprF, an outer membrane protein of Pseudomonas aeruginosa, was studied to assess variations in its surface antigenic epitopes across different serotypes.
- Only 16 nucleotide changes were found in the gene sequence of a serotype 5 isolate compared to a serotype 12, none affecting the amino acid structure.
- A panel of monoclonal antibodies (mAbs) showed that OprF has conserved antigenic epitopes, which were somewhat obscured by lipopolysaccharide side chains, indicating its potential role in immune response.
Article Abstract
The outer membrane proteins of several prominent bacterial pathogens demonstrate substantial variation in their surface antigenic epitopes. To determine if this was also true for Pseudomonas aeruginosa outer membrane protein OprF, gene sequencing of a serotype 5 isolate was performed to permit comparison with the published serotype 12 oprF gene sequence. Only 16 nucleotide substitutions in the 1053 nucleotide coding region were observed; none of these changed the amino acid sequence. A panel of 10 monoclonal antibodies (mAbs) reacted with each of 46 P. aeruginosa strains representing all 17 serotype strains, 12 clinical isolates, 15 environmental isolates and 2 laboratory isolates. Between two and eight of these mAbs also reacted with proteins from representatives of the rRNA homology group I of the Pseudomonadaceae. Nine of the ten mAbs recognized surface antigenic epitopes as determined by indirect immunofluorescence techniques and their ability to opsonize P. aeruginosa for phagocytosis. These epitopes were partially masked by lipopolysaccharide side chains as revealed using a side chain-deficient mutant. It is concluded that OprF is a highly conserved protein with several conserved surface antigenic epitopes.
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| http://dx.doi.org/10.1111/j.1574-6968.1993.tb06524.x | DOI Listing |
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