This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Tso, J Y Articles by Siebel, C Search for Related Content PubMed PubMed Citation Articles by Tso, J Y Articles by Siebel, C

 Previous Article  |  Next Article 

Infect Immun. 1989 February; 57(2): 468-476

Cloning and expression of the phospholipase C gene from Clostridium perfringens and Clostridium bifermentans.

Protein Design Labs, Inc., Palo Alto, California 94304.

ABSTRACT

The phospholipase C gene from Clostridium perfringens was isolated, and its sequence was determined. It was found that the structural gene codes for a protein of 399 amino acid residues. The NH2-terminal residues have the typical features of a signal peptide and are probably cleaved after secretion. Escherichia coli cells harboring the phospholipase C gene-containing plasmid expressed high levels of this protein in the periplasmic space. Phospholipase C purified from E. coli transformants was enzymatically active, hemolytic to erythrocytes, and toxic to animals when injected intravenously. The phospholipase C gene from a related organism, Clostridium bifermentans, was also isolated. The two phospholipase C genes were found to be 64% homologous in coding sequence. The C. bifermentans protein, however, was 50-fold less active enzymatically than the C. perfringens enzyme.

This article has been cited by other articles:

• Sakurai, J., Nagahama, M., Oda, M. (2004). Clostridium perfringens Alpha-Toxin: Characterization and Mode of Action. J Biochem 136: 569-574 [Abstract] [Full Text]  
• Vulevic, J., McCartney, A. L., Gee, J. M., Johnson, I. T., Gibson, G. R. (2004). Microbial Species Involved in Production of 1,2-sn-Diacylglycerol and Effects of Phosphatidylcholine on Human Fecal Microbiota. Appl. Environ. Microbiol. 70: 5659-5666 [Abstract] [Full Text]  
• Karasawa, T., Wang, X., Maegawa, T., Michiwa, Y., Kita, H., Miwa, K., Nakamura, S. (2003). Clostridium sordellii Phospholipase C: Gene Cloning and Comparison of Enzymatic and Biological Activities with Those of Clostridium perfringens and Clostridium bifermentans Phospholipase C. Infect. Immun. 71: 641-646 [Abstract] [Full Text]  
• AUGUSTYNOWICZ, E., GZYL, A., SLUSARCZYK, J. (2002). Detection of enterotoxigenic Clostridium perfringens with a duplex PCR. J Med Microbiol 51: 169-172 [Abstract] [Full Text]  
• Schoepe, H., Pache, C., Neubauer, A., Potschka, H., Schlapp, T., Wieler, L. H., Baljer, G. (2001). Naturally Occurring Clostridium perfringens Nontoxic Alpha-Toxin Variant as a Potential Vaccine Candidate against Alpha-Toxin-Associated Diseases. Infect. Immun. 69: 7194-7196 [Abstract] [Full Text]  
• Ghannoum, M. A. (2000). Potential Role of Phospholipases in Virulence and Fungal Pathogenesis. Clin. Microbiol. Rev. 13: 122-143 [Abstract] [Full Text]  
• Jepson, M., Howells, A., Bullifent, H. L., Bolgiano, B., Crane, D., Miller, J., Holley, J., Jayasekera, P., Titball, R. W. (1999). Differences in the Carboxy-Terminal (Putative Phospholipid Binding) Domains of Clostridium perfringens and Clostridium bifermentans Phospholipases C Influence the Hemolytic and Lethal Properties of These Enzymes. Infect. Immun. 67: 3297-3301 [Abstract] [Full Text]  
• Flores-Diaz, M., Alape-Giron, A., Titball, R. W., Moos, M., Guillouard, I., Cole, S., Howells, A. M., von Eichel-Streiber, C., Florin, I., Thelestam, M. (1998). UDP-glucose Deficiency Causes Hypersensitivity to the Cytotoxic Effect of Clostridium perfringens Phospholipase C. J. Biol. Chem. 273: 24433-24438 [Abstract] [Full Text]