Our understanding of the function of vitellogenin (Vg) in reproduction has undergone a transformation over the past decade in parallel with new insights into the role of Vg in immunity. Initially, Vg was regarded as a female-specific reproductive protein, which is cleaved into yolk proteins such as phosvitin (Pv) and lipovitellin (Lv), stored in egg, providing the nutrients for developing embryos. Recently, Vg is shown to be an immune-relevant molecule involved in the defense of the host against the microbes including bacterium and virus. Furthermore, Pv and Lv, that both are proteolytically cleaved products of Vg, play a defense role in developing embryos. Importantly, yolk protein-derived small peptides also display antimicrobial activity. These data together indicate that Vg, in addition to being involved in yolk protein formation, plays a non-reproductive role via functioning as an immune-relevant molecule in both parent fishes and their offspring. It also shows that yolk proteins and their degraded peptides are novel players in maternal immunity, opening a new avenue to study the functions of reproductive proteins.
Keywords: Lipovitellin; Phosvitin; Vg-derived peptide; Vitellogenin.
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