| Literature DB >> 10523590 |
S Korbsrisate1, N Suwanasai, A Leelaporn, T Ezaki, Y Kawamura, S Sarasombath.
Abstract
We cloned and characterized a phosphatidylcholine-hydrolyzing phospholipase C (PC-PLC) gene from Burkholderia pseudomallei. DNA sequence analysis of the gene indicated an open reading frame coding for 700 amino acids with a 34-amino-acid signal peptide. When cleaved, this yields a secreted 73-kDa mature protein. The deduced amino acid sequence exhibited 48% similarity to that of a nonhemolytic PLC from Pseudomonas aeruginosa. The expressed PC-PLC was heat stable, nonhemolytic for sheep erythrocytes, and active between pH 2 and 8. Western blot analysis with sera from melioidosis patients indicated that they produced immunoglobulin M antibodies against this PC-PLC protein.Entities:
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Year: 1999 PMID: 10523590 PMCID: PMC85747
Source DB: PubMed Journal: J Clin Microbiol ISSN: 0095-1137 Impact factor: 5.948