Murray Rebecca, Derré Isabelle
Department of Microbiology, Immunology, and Cancer Biology, University of Virginia, Charlottesville, VA, USA.
Contact (Thousand Oaks). 2018 May 17;1:2515256418775512. doi: 10.1177/2515256418775512. eCollection 2018 Jan-Dec.
In naïve cells, the endoplasmic reticulum (ER) and the ER-resident esicle-associated membrane protein-ssociated roteins (VAP) are common components of sites of membrane contacts that mediate the nonvesicular transfer of lipids between organelles. There is increasing recognition that the hijacking of VAP by intracellular pathogens is a novel mechanism of host-pathogen interaction. Here, we summarize our recent findings showing that the inclusion membrane protein IncV tethers the ER to the inclusion membrane by binding to VAP via the molecular mimicry of two eukaryotic FFAT motifs. We extend the discussion to other microorganisms that have evolved similar mechanisms.
在未致敏细胞中,内质网(ER)和内质网驻留囊泡相关膜蛋白相关蛋白(VAP)是膜接触位点的常见组成部分,介导细胞器之间脂质的非囊泡转运。越来越多的人认识到,细胞内病原体劫持VAP是宿主-病原体相互作用的一种新机制。在这里,我们总结了我们最近的发现,即包涵体膜蛋白IncV通过两个真核FFAT基序的分子模拟与VAP结合,将内质网与包涵体膜相连。我们将讨论扩展到其他进化出类似机制的微生物。