Eukaryotic cells can selectively target and degrade intracellular pathogens using autophagy, a process referred to as xenophagy. This selectivity is controlled by proteins called autophagy receptors, which can recognise pathogens and address them to the autophagy machinery. Among them, NDP52 can recognise Salmonella Typhimurium on the one hand and the ATG8 family member LC3C on the other hand, thus allowing the docking of the bacteria to a growing autophagosome. Additionally, we recently reported that NDP52 is involved in the maturation of the bacteria-containing autophagosome and hence necessary for the ultimate degradation of the bacteria. These two functions of NDP52 are independent as they rely on distinct binding domains and protein partners. Therefore, NDP52 plays a dual role during xenophagy, first by targeting the bacteria to the autophagy machinery and then by regulating its degradation.