Open AccessExpression of adipose differentiation‐related protein (ADRP) and perilipin in macrophages infected with Mycobacterium leprae
Author(s) -
Tanigawa Kazunari,
Suzuki Koichi,
Nakamura Kazuaki,
Akama Takeshi,
Kawashima Akira,
Wu Huhehasi,
Hayashi Moyuru,
Takahashi ShinIchiro,
Ikuyama Shoichiro,
Ito Tetsuhide,
Ishii Norihisa
Publication year - 2008
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2008.01369.x
Subject(s) - phagosome , perilipin , mycobacterium leprae , biology , microbiology and biotechnology , lipid droplet , macrophage , phagocytosis , adipose tissue , immunology , adipocyte , biochemistry , leprosy , in vitro
Mycobacterium leprae survives and replicates within a lipid droplet stored in the enlarged phagosome of histiocytes, a typical feature of lepromatous leprosy that is thought to be an important nutrient source for the bacillus. However, the underlying mechanisms by which lipids accumulate within phagosomes remain unclear. Recently, it was revealed that the lipid droplet‐associated proteins, including ADRP and perilipin, play essential roles in lipid accumulation in adipocytes or macrophages. Therefore, we attempted to examine the role of these proteins in leprosy pathogenesis. ADRP and perilipin localized to the phagosomal membrane, which contains M. leprae in skin biopsy specimens of lepromatous leprosy. ADRP expression was transiently increased after phagocytosis in THP‐1 cells. However, high levels of ADRP expression persisted only when live M. leprae , but not dead bacilli or latex beads, was added. Furthermore, although peptidoglycan, a Toll‐like receptor 2 ligand, suppressed the expression levels of ADRP and perilipin, M. leprae infection inhibited this suppression. These results suggest that live M. leprae has the ability to actively induce and support ADRP/perilipin expression to facilitate the accumulation of lipids within the phagosome and to further maintain a suitable environment for the intracellular survival within the macrophage.