Phagocytosis is a fundamental cellular process through which phagocytic immune cells internalize foreign particles such as microorganisms, leading to the creation of the phagosome. Once formed, the phagosome acquires its functional properties through a series of fission and fusion events with endomembranes plus modification of phosphoinositides in the phagosomal membrane, which ultimately culminates in formation of the phagolysosome in which the foreign content is destroyed in a robust environment. A wide variety of pathogens have developed and implemented multiple mechanisms to circumvent the immune system and alter phagosome maturation to escape destruction. Studies of our lab have revealed the presence of SNARE ER-ERGIC Sec22b protein, well-known to be involved in membrane fusion, at the membrane contact sites (MCS) between the endoplasmic reticulum and the phagosomes which raised a question of whether Sec22b could be regulating the phagosome maturation by a role in tethering ER-Phagosomes MCS. Here, we show that the knockdown of the ER-ERGIC SNARE protein Sec22b in mouse embryonic fibroblasts leads to increased lysosome fusion with phagosomes, and the overexpression of an artificial MCS in cells deficient in Sec22b rescued the phagolysosome fusion, which verify that membrane contact sites are involved in the phagolysosome regulation. Furthermore, we showed that Sec22b modulates the phagolysosome fusion by recruiting lipid transfer protein ORP8 which eventually mediate non-vesicular transfer of the phosphatidylinositol-4-phosphate across MCS. Identifying the molecular players involved in the regulation of the phagosome maturation could provide novel targets for future therapeutic interventions.