Harricane M C, Caron E, Porte F, Liautard J P
INSERM U-249, CRBM du CNRS, Université Montpellier I, France.
Cell Biol Int. 1996 Mar;20(3):193-203. doi: 10.1006/cbir.1996.0024.
Annexin I is an abundant protein in U937 cells differentiated towards a macrophagic phenotype. These cells become able to kill Escherichia coli, however, the intracellular pathogen Brucella suis, known to interfere with phagosome maturation, multiply in these differentiated cells. We have analysed by confocal and electron microscopy the cellular localization of annexin I during phagocytosis of yeast, non-pathogenic E. coli and the intracellular pathogen B. suis. Using immunocytochemical detections annexin I was found mainly as patches in the cytoplasm of uninfected cells. Upon phagocytosis of yeast or E. coli organisms, annexin I rapidly translocated and concentrated around phagosomes. On the other hand, annexin I was never detected around live B. suis-containing phagosomes. However, when dead brucellae were used, annexin I did translocate to the periphagosomal region. Our results suggest that annexin I could play a role in the molecular mechanism of phagosome maturation, which is impaired by some intracellular pathogens.
膜联蛋白I是U937细胞向巨噬细胞表型分化过程中一种丰富的蛋白质。这些细胞能够杀死大肠杆菌,然而,已知会干扰吞噬体成熟的细胞内病原体猪布鲁氏菌在这些分化细胞中会繁殖。我们通过共聚焦显微镜和电子显微镜分析了在吞噬酵母、非致病性大肠杆菌和细胞内病原体猪布鲁氏菌过程中膜联蛋白I的细胞定位。使用免疫细胞化学检测发现,膜联蛋白I在未感染细胞的细胞质中主要呈斑块状分布。在吞噬酵母或大肠杆菌后,膜联蛋白I迅速转移并集中在吞噬体周围。另一方面,在含有活猪布鲁氏菌的吞噬体周围从未检测到膜联蛋白I。然而,当使用死布鲁氏菌时,膜联蛋白I确实会转移到吞噬体周围区域。我们的结果表明,膜联蛋白I可能在吞噬体成熟的分子机制中发挥作用,而某些细胞内病原体损害了这一机制。