Abstract
The cytoplasm in mammalian cells is a battlefield between the host and invading microbes. Both the living organisms have evolved unique strategies for their survival. The host utilizes a specialized autophagy system, xenophagy, for the clearance of invading pathogens, whereas bacteria secrete proteins to defend and escape from the host xenophagy. Several molecules have been identified and their structural investigation has enabled the comprehension of these mechanisms at the molecular level. In this review, we focus on one example of host autophagy and the other of bacterial defense: the autophagy receptor, NDP52, in conjunction with the sugar receptor, galectin-8, plays a critical role in targeting the autophagy machinery against Salmonella; and the cysteine protease, RavZ secreted by Legionella pneumophila cleaves the LC3-PE on the phagophore membrane. The structure-function relationships of these two examples and the directions of future research will be discussed.
| Original language | English |
|---|---|
| Pages (from-to) | 27-34 |
| Number of pages | 8 |
| Journal | Molecules and cells |
| Volume | 41 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - 2018 |
Bibliographical note
Funding Information:We apologize to the researchers who were not referenced because of space limitations or unintentional omissions. This work was supported by the National Research Foundation of Korea (NRF) grants from the Korean government (BRL grant: No. 2015041919 and International Cooperation Program: No. 2015K2A2A6002008) and supported by a grant from the Samsung Science & Technology Foundation (SSTF-BA 1701-14).
Publisher Copyright:
© The Korean Society for Molecular and Cellular Biology. All rights reserved.
Keywords
- Galectin-8
- Legionella
- NDP52
- RavZ
- Salmonella
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology