LAMP-3 (Lysosome-Associated Membrane Protein 3) Promotes the Intracellular Proliferation of Salmonella typhimurium
In: Molecules and Cells, Jg. 39 (2016-06-21), S. 566-572
Online
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Zugriff:
Lysosomes are cellular organelles containing diverse classes of catabolic enzymes that are implicated in diverse cellular processes including phagocytosis, autophagy, lipid transport, and aging. Lysosome-associated membrane proteins (LAMP-1 and LAMP-2) are major glycoproteins important for maintaining lysosomal integrity, pH, and catabolism. LAMP-1 and LAMP-2 are constitutively expressed in Salmonella-infected cells and are recruited to Salmonella-containing vacuoles (SCVs) as well as Salmonella-induced filaments (Sifs) that promote the survival and proliferation of the Salmonella. LAMP-3, also known as DC-LAMP/CD208, is a member of the LAMP family of proteins, but its role during Salmonella infection remains unclear. DNA microarray analysis identified LAMP-3 as one of the genes responding to LPS stimulation in THP-1 macrophage cells. Subsequent analyses reveal that LPS and Salmonella induced the expression of LAMP-3 at both the transcriptional and translational levels. Confocal Super resolution N-SIM imaging revealed that LAMP-3, like LAMP-2, shifts its localization from the cell surface to alongside Salmonella. Knockdown of LAMP-3 by specific siRNAs decreased the number of Salmonella recovered from the infected cells. Therefore, we conclude that LAMP-3 is induced by Salmonella infection and recruited to the Salmonella pathogen for intracellular proliferation.
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LAMP-3 (Lysosome-Associated Membrane Protein 3) Promotes the Intracellular Proliferation of Salmonella typhimurium
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Autor/in / Beteiligte Person: | Park, Kwan-Sik ; Lee, Sang-Jeon ; Lee, Hak-Kyo ; Song, Ki-Duk ; Choy, Hyun E. ; Choi, Jae-Woon ; Jeon, In-Sook ; Choi, Joong-Kook ; Lee, Eun-Ju |
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Zeitschrift: | Molecules and Cells, Jg. 39 (2016-06-21), S. 566-572 |
Veröffentlichung: | Korean Society for Molecular and Cellular Biology, 2016 |
Medientyp: | unknown |
ISSN: | 0219-1032 (print) ; 1016-8478 (print) |
DOI: | 10.14348/molcells.2016.0112 |
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