In common with all segmented negative-sense RNA viruses, bunyavirus transcripts contain heterologous sequences at their 5′ termini originating from capped host cell RNAs. These heterologous sequences are acquired by a socalled cap-snatching mechanism. Whereas for nuclear replicating influenza virus the source of capped primers as well as the cap-binding and endonuclease activities of the viral polymerase needed for cap snatching have been functionally and structurally well characterized, our knowledge on the expected counterparts of cytoplasmic replicating bunyaviruses is still limited and controversial. This review focuses on the cap-snatching mechanism of bunyaviruses in the light of recent structural and functional data. Bunyavirus Transcription and Genome Replication The order of Bunyavirales, which was established in 2018, accommodates a diverse group of viruses formerly separated into the Arenaviridae and Bunyaviridae families [1]. The Bunyavirales order contains important human pathogens such as Lassa virus (LASV; family Arenaviridae), Crimean-Congo hemorrhagic fever virus (family Nairoviridae), Rift Valley fever virus (RVFV, family Phenuiviridae), Hantaan virus (family Hantaviridae), and La Crosse virus (family Peribunyaviridae). Highlights Endonuclease domains have been located in many different bunyavirus L proteins and can be classified as His+ or His-metal-dependent endonucleases. An active cap-binding domain (CBD) has been identified in the C-terminal region of bunyavirus L protein. Despite very low sequence identity, this domain is very similar to influenza virus PB2 CBD on the structural level. Atomic structures of bunyavirus N protein do not provide evidence for the hypothesized N protein cap-binding site. It remains unclear whether a functionally relevant cap-specific binding site exists in any bunyavirus N protein. The comparably low affinity of bunyavirus CBD for cap-structures indicates the necessity for further regions of the L protein or other viral or cellular proteins to be involved in cap binding.