Rearrangements of actin cytoskeleton during infection with Escherichia coli O157 in macrophages.
The lamina propria of the large intestine is rich in macrophages, and they might be one of the first lines of the host defense in enterohemorrhagic Escherichia coli (EHEC) O157:H7 infection. Although macrophages were infected with them, they can survive the EHEC O157 infection. We examined the structural rearrangements of the actin cytoskeleton during the microbial infection process. Macrophage actin filaments were rearranged in the following sequence; 1) disappearance of the actin filament bundles in the cytoplasm, 2) accumulation of actin filaments under the cell surface, and 3) construction of actin networks underlying the endosome membrane. Before infection, actin filaments were distributed under the cell surface and in bundles located in the macrophage cytoplasm. Within 2 min, infection caused a rapid and marked loss of the actin filament bundles that had run parallel to the long axis of the cell. Concomitant with the loss, actin filaments became more markedly distributed under the cell surface. In the formation of the endosome, new networks of actin filaments were constructed below the phagosome membrane. The networks contained a large amount of actin as well as a fodrin-like immunoreactivity. The thickness of the networks reached about 400 nm under the phagosome membrane. The actin networks disappeared again after the bacterial digestion. The results of this study showed that actin filaments undergo three major rearrangements of the actin filaments during the infection in macrophages, and suggested that the third rearrangement is mediated by actin-binding proteins, such as a fodrin-like molecules. These morphological changes in macrophages were not clear after infection with other strains of Escherichia coli.
Shimada
O
O
Department of Anatomy, Yamanashi Medical University, School of Medicine, Tamaho, Yamanashi 409-3821, Japan. oshimada@swallow.res.yamanashi-med.ac.jp
Ishikawa
H
H
Tosaka-Shimada
H
H
Atsumi
S
S
D000135:Acid Phosphatase / Q000032:analysis; D000199:Actins / Q000378:metabolism*; D000818:Animals; D015153:Blotting, Western; D002352:Carrier Proteins / Q000378:metabolism; D003599:Cytoskeleton / Q000378:metabolism*; D019453:Escherichia coli O157 / Q000737:chemistry / Q000254:growth & development*; D005260:Female; D007150:Immunohistochemistry; D008247:Lysosomes / Q000201:enzymology; D017737:Macrophages, Peritoneal / Q000166:cytology / Q000378:metabolism* / Q000382:microbiology; D008840:Microfilament Proteins / Q000378:metabolism; D018613:Microscopy, Confocal; D016253:Microscopy, Immunoelectron; D019081:O Antigens / Q000032:analysis; D010587:Phagocytosis / Q000502:physiology; D010588:Phagosomes / Q000382:microbiology / Q000648:ultrastructure; D010590:Phalloidine / Q000737:chemistry; D051381:Rats; D017208:Rats, Wistar; D022622:Shiga Toxin 1 / Q000032:analysis; D022641:Shiga Toxin 2 / Q000032:analysis; D013049:Spectrin
D000135:Acid Phosphatase; D000199:Actins; D002352:Carrier Proteins; D008840:Microfilament Proteins; D019081:O Antigens; D010590:Phalloidine; D022622:Shiga Toxin 1; D022641:Shiga Toxin 2; D013049:Spectrin