Author:
Lycke E,Carlberg K,Norrby R
Abstract
A protein with a molecular weight of 70,000 to 150,000 which was extracted from merozoites of Toxoplasma gondii enhanced the host cell penetration of the merozoites. The optimal pH and temperature for penetration of merozoites coincided with those favoring the action of the penetration-enhancing protein. In addition, a dependence on Ca and Mg existed for penetration of merozoites, either in the presence or absence of this protein. No evidence was found that indicated that the enhancing effect on penetration elicited by the protein was due to increased phagocytic capacity of host cells (HeLa) or improved motility of the merozoites. Electron microscopy demonstrated that the protein, in high concentration, caused disruption of cytoplasmic membranes. In a 100-fold-lower concentration, which still caused a marked enhancement of penetration, no such effect was observed. However, the vacuoles surrounding the penetrated parasites seemed smaller than for merozoites penetrating in cultures to which no penetration-enhancing factor was given, and the membranes limiting the vacuoles demonstrated discontinuities more often. The penetration-enchancing effect of some known enzymes was studies. However, none of these enzymes seemed to correspond to the penetration-enhancing protein of toxoplasma. The mode of entry of toxoplasma merozoites into host cells is discussed. It is concluded that phagocytosis must play a less important role and that merozoites actively penetrate the cytoplasmic membranes of the host cells. The penetration is proposed to be a result of combined mechanical and chemical actions. It is suggested that an enzymatic function of the penetration-enhancing factor released by the merozoites is of importance. The membrane limiting the vacuole of a penetrated merozoite seems to be newly formed in the cell after penetration is completed.
Publisher
American Society for Microbiology
Subject
Infectious Diseases,Immunology,Microbiology,Parasitology
Reference41 articles.
1. Ultramicroscopic studies on the localization of adenosine triphosphatase activity and H3-glucose transport in Toxoplasma gondii;Akao S.;Jpn. J. Parasitol.,1969
2. Toxoplasma gondii: aspartate aminotransferase in cell membrane;Akao S.;Exp. Parasitol.,1971
3. Studies on the localization of peroxidase activity in Toxoplasma gondii;Akao S.;Exp. Parasitol.,1971
4. Effect of normal and activated human macrophages on Toxoplasma gondii;Anderson S. E.;J. Exp. Med.,1974
5. Quantitative nitroblue tetrazolium test in chronic granulomatous disease;Baehner R. L.;N. Engl. J. Med.,1968
Cited by
87 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献