Lysosomal integral membrane protein 2 (LIMP-2) restricts the invasion of Trypanosoma cruzi extracellular amastigotes through the activity of the lysosomal enzyme 尾-glucocerebrosidase

详细信息    查看全文

• 作者：Viviane Martinelli Gonç ; alves^a ; Vâ ; nia D'Almeida^b ; Karen Barbosa Mü ; ller^c ; Fernando Real^a ; ^{fernando.real@unifesp.br" class="auth_mail} ; Renato Arruda Mortara^a
• 关键词：LIMP-2 ; 尾-Glucocerebrosidase ; Trypanosoma cruzi ; Extracellular amastigotes
• 刊名：Microbes and Infection
• 出版年：March, 2014
• 年：2014
• 卷：16
• 期：3
• 页码：253-260
• 全文大小：1378 K

文摘

Lysosomal integral membrane protein 2 (LIMP-2, SCARB2) is directly linked to 尾-glucocerebrosidase enzyme (尾GC) and mediates the transport of this enzyme from the Golgi complex to lysosomes. Active 尾GC cleaves the 尾-glycosidic linkages of glucosylceramide, an intermediate in the metabolism of sphingoglycolipids, generating ceramide. In this study we used mouse embryonic fibroblasts (MEFs) deficient for LIMP-2 and observed that these cells were more susceptible to infection by extracellular amastigotes of the protozoan parasite Trypanosoma cruzi when compared to wild-type (WT) fibroblasts. The absence of LIMP-2 decreases the activity of 尾GC measured in fibroblast extracts. Replacement of 尾GC enzyme in LIMP-2 deficient fibroblasts restores the infectivity indices to those of WT cells in T. cruzi invasion assays. Considering the participation of 尾GC in the production of host cell ceramide, we propose that T. cruzi extracellular amastigotes are more invasive to cells deficient in this membrane component. These results contribute to our understanding of the role of host cell lysosomal components in T. cruzi invasion.