The apple buprestid beetle, Agrilus mali Matsumura (Coleoptera: Buprestidae), can respond to various volatiles, but the underlying mechanism of odorant perception for this insect is poorly understood. Here, we cloned A. mali's odorant-binding proteins 3 (AmalOBP3) and 8 (AmalOBP8) and characterized their expression patterns and binding profiles. Sequence and phylogenetic analyses showed that AmalOBP3 and AmalOBP8 were distributed in the classic and minus-C OBP subfamily, respectively. AmalOBP3 was specifically and abundantly expressed in antennae of both sexes. AmalOBP8 displayed high transcript levels in antennae of both sexes, abdomens of males, and wings of both sexes. Both AmalOBPs exhibited much higher expression in male antennae than in female antennae, suggesting that they could be important in perception of male-specific olfactory cues (e.g., some sex pheromones). Out of the 40 odorant ligands tested, AmalOBP3 and AmalOBP8 bound to 15 and 21 different odorants, respectively, indicating a distinct and selective binding profile for them. Both AmalOBPs seemed to have very strong binding affinity to aliphatic alcohols and aldehydes with 12 to 15 carbon atoms. Alcohols, esters, and terpenoids were more likely to be good ligands for both AmalOBPs than aldehydes and alkanes. Together with its broad expression in different tissues, strong binding with higher numbers of putative ligands for AmalOPB8 means that this protein can have more extensive functional roles in chemosensation of A. mali. Our results provide insights into the molecular basis of chemosensation in A. mali, as well as a basis for developing detection, monitoring, and management tools for this serious pest.