Phospholipid metabolism induced by Clostridium perfringens alpha-toxin elicits a hot-cold type of hemolysis in rabbit erythrocytes.

Abstract

GTP and AIF4- significantly stimulated the late phosphatidic acid (PA) formation induced by Clostridium perfringens alpha-toxin in rabbit erythrocyte lysates. Pertussis toxin blocked the PA production. AIF4- markedly enhanced phosphatidylethanol production induced by alpha-toxin in the presence of ethanol. GTP[gamma S] stimulated the PA formation and hemolysis induced by alpha-toxin, and GDP[beta S] inhibited them. An H-to-G mutation at position 126 (H126G) induced the PA formation and hemolysis in a Co2+ concentration-dependent manner. H148G induced neither the PA formation nor hemolysis. These results suggest that the toxin-induced hemolysis is due to activation of phospholipid metabolism systems through GTP-binding protein.

• Authors: S Ochi, K Hashimoto, M Nagahama, J Sakurai
• Journal: Infection and immunity (Infect Immun) Vol. 64 Issue 9 Pg. 3930-3 (Sep 1996) ISSN: 0019-9567 [Print] United States
• PMID: 8751953 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Aluminum Compounds
• Bacterial Toxins
• Calcium-Binding Proteins
• Guanine Nucleotides
• Phospholipids
• Cobalt
• Type C Phospholipases
• alpha toxin, Clostridium perfringens
• GTP-Binding Proteins
• Fluorides
• aluminum fluoride

Topics

• Aluminum Compounds (pharmacology)
• Animals
• Bacterial Toxins (chemistry, toxicity)
• Calcium-Binding Proteins
• Clostridium perfringens (pathogenicity)
• Cobalt (pharmacology)
• Cold Temperature
• Erythrocyte Membrane (physiology)
• Fluorides (pharmacology)
• GTP-Binding Proteins (metabolism)
• Guanine Nucleotides (metabolism)
• Hemolysis (drug effects)
• Hot Temperature
• Phospholipids (blood)
• Rabbits
• Structure-Activity Relationship
• Type C Phospholipases