ArticleFEBS open bio2025
Comparative study of adenosine 3'-pyrophosphokinase domains of MuF polymorphic toxins.
Article in FEBS open bio, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Polymorphic toxins (PT) are multidomain proteins used for interbacterial competition and pathogenesis. The N-terminal domain of PT specifies the mode of transport and names the family, while the variable C-terminal domain carries the toxic activity, which can be counteracted by immunity proteins that protect the PT-producing bacterium. The MuF family of polymorphic toxins is specifically associated with temperate phages, and our recent work showed that the C-terminal domain of a MuF toxin encoded by a Streptococcus pneumoniae prophage carries adenosine 3'-pyrophosphokinase activity. This type of toxin, which combines a MuF N-terminal domain and an adenosine 3'-pyrophosphokinase C-terminal domain, is called Apk2 for adenosine 3'-pyrophosphokinase family 2. Here, we extend the characterization of this novel family of toxins by providing information on two new members encoded by prophages of Mannheimia haemolytica and Pasteurella multocida. Production of their adenosine 3'-pyrophosphokinase domains (Apk2
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