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J Biol Chem, Vol. 274, Issue 17, 11459-11462, April 23, 1999
From the Department of Cell Biology and Physiology, Washington
University School of Medicine, St. Louis, Missouri 63110
Previous studies have shown that Listeria
monocytogenes (LM) modulates phagocytic membrane traffic. Here we
explore whether Rab5a, a GTPase associated with phagosome-endosome
fusion, is related to phagosome maturation and to the intracellular
survival of LM. Stable transfection of Rab5a cDNA into macrophages
accelerates intracellular degradation of LM. Morphological studies
confirmed that phagosome maturation and phagosome-lysosome fusion is
enhanced by overexpression of Rab5a.
Down-regulation experiments using antisense oligonucleotides targeted
to the Rab5a mRNA efficiently reduced Rab5a synthesis, reduced
phagosome-endosome traffic, blocked phagosome-lysosome fusion, and
extended intraphagosomal survival of LM. Down-regulation of Rab5a had
no effect on LM internalization. Down-regulation of Rab5c had no effect
on phagosome maturation and phagosome-lysosome fusion. The results
indicate that Rab5a controls early phagosome-endosome interactions and
governs the maturation of the early phagosome leading to
phagosome-lysosome fusion.
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