Large lipid transfer proteins are involved in lipid transportation and diverse other molecular processes. These serum proteins include vitellogenins that are egg-yolk precursors and pathogen pattern recognition receptors, and apolipoprotein B that is an anti-inflammatory cholesterol carrier. In the honey bee, vitellogenin acts as an antioxidant, and elevated vitellogenin titer is linked to prolonged lifespan in this animal. Here, we show that vitellogenin has cell and membrane binding activity, and that it binds preferentially to dead and damaged cells. Vitellogenin binds directly to phosphatidylcholine liposomes, and with higher affinity to liposomes containing phosphatidylserine - a lipid of the inner-leaflet of cell membranes that is exposed in damaged cells. Vitellogenin binding to live cells, furthermore, improves cell oxidative stress tolerance. This study can shed more light on why large lipid transfer proteins have a well-conserved α-helical domain, as we locate the lipid bilayer-binding ability of vitellogenin largely to this region. We suggest that recognition of cell damage and oxidation shield properties are two mechanisms that allow vitellogenin to extend honey bee lifespan.