Sunee KorbsrisateNuttiga SuwanasaiAmornrut LeelapornTakayuki EzakiYoshiaki KawamuraSuttipant SarasombathFaculty of Medicine, Siriraj Hospital, Mahidol UniversityGifu University School of MedicineMahidol University2018-09-072018-09-071999-11-01Journal of Clinical Microbiology. Vol.37, No.11 (1999), 3742-3745009511372-s2.0-0032867180https://repository.li.mahidol.ac.th/handle/20.500.14594/25569We 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.Mahidol UniversityMedicineArticleSCOPUS