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Abstract A contractile sheath and rigid tube assembly is a widespread apparatus used by bacteriophages, tailocins, and the bacterial type VI secretion system to penetrate cell membranes. In this mechanism, contraction of an external sheath powers the motion of an inner tube through the membrane. The structure, energetics, and mechanism of the machinery imply rigidity and straightness. The contractile tail ofAgrobacterium tumefaciensbacteriophage Milano is flexible and bent to varying degrees, which sets it apart from other contractile tail-like systems. Here, we report structures of the Milano tail including the sheath-tube complex, baseplate, and putative receptor-binding proteins. The flexible-to-rigid transformation of the Milano tail upon contraction can be explained by unique electrostatic properties of the tail tube and sheath. All components of the Milano tail, including sheath subunits, are crosslinked by disulfides, some of which must be reduced for contraction to occur. The putative receptor-binding complex of Milano contains a tailspike, a tail fiber, and at least two small proteins that form a garland around the distal ends of the tailspikes and tail fibers. Despite being flagellotropic, Milano lacks thread-like tail filaments that can wrap around the flagellum, and is thus likely to employ a different binding mechanism. 

Abstract TheJ= 5.5 → 4.5 andJ= 5 → 4 transitions of PO and PN, respectively, have been imaged in the envelope of hypergiant star VY Canis Majoris (VY CMa) using the Atacama Large Millimeter/submillimeter Array with angular resolutions of 0.″2 and 1.″5 and data from the Submillimeter Telescope of the Arizona Radio Observatory. These maps are the first high-fidelity images of PO and PN in a circumstellar envelope. Both molecules are primarily present in a spherical, star-centered region with a radius ∼60R_*(0.″5), indicating formation by LTE chemistry and then condensation into grains. PN, however, shows additional, fan-shaped emission 2″ southwest of the star, coincident with dust features resolved by Hubble Space Telescope (HST), as well as four newly identified distinct structures 1″–2″ toward the north, east, and west (Cloudlets I–IV), not visible in HST images. The “SW Fan” and the cloudlets are also prominent in theJ= 5.5 → 4.5 transition of NS. The correlation of PN with NS, SiO, and dust knots in the SW Fan suggests a formation in shocked gas enhanced with nitrogen. Excess nitrogen is predicted to favor PN synthesis over PO. Abundances for PN and PO in the spherical source aref∼ 4.4 × 10⁻⁸and 1.4 × 10⁻⁷, respectively, relative to H₂. Given a cosmic abundance of phosphorus, an unusually high fraction (∼35%) is contained in PO and PN. Alternatively, the stellar winds may be enriched in P (and N) by dredge-up from the interior of VY CMa. 

Abstract Large gaps exist in our understanding of how bacteriophages, the most abundant biological entities on Earth, assemble and function. The structure of the “neck” region, where the DNA-filled capsid is connected to the host-recognizing tail remains poorly understood. We describe cryo-EM structures of the neck, the neck-capsid and neck-tail junctions, and capsid of theAgrobacteriumphage Milano. The Milano neck 1 protein connects the 12-fold symmetrical neck to a 5-fold vertex of the icosahedral capsid. Comparison of Milano neck 1 homologs leads to four proposed classes, likely evolved from the simplest one in siphophages to more complex ones in myo- and podophages. Milano neck is surrounded by the atypical collar, which covalently crosslinks the tail sheath to neck 1. The Milano capsid is decorated with three types of proteins, a minor capsid protein (mCP) and two linking proteins crosslinking the mCP to the major capsid protein. The extensive network of disulfide bonds within and between neck, collar, capsid and tail provides an exceptional structural stability to Milano.