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.
journal_name
J Clin Microbioljournal_title
Journal of clinical microbiologyauthors
Korbsrisate S,Suwanasai N,Leelaporn A,Ezaki T,Kawamura Y,Sarasombath Sdoi
10.1128/JCM.37.11.3742-3745.1999subject
Has Abstractpub_date
1999-11-01 00:00:00pages
3742-5issue
11eissn
0095-1137issn
1098-660Xjournal_volume
37pub_type
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