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The Myoviridae cyanophage A-1(L) specifically infects the model cyanobacteria Anabaena sp. PCC 7120. Here, authors present the high-resolution cryo-EM structure of its intact tail machine, and identify multiple hydrolytic and binding modules.
Orthoreovirus σNS, essential for forming viral replication factories, has RNA chaperone activity that requires the association of σNS dimers into filamentous structures stabilized by domain-swapping interactions of the flexible N-terminal arms.
Here, Li et al. provide the cryo-EM structures of Banna virus (BAV) in four configurations. VP10 functions as a unique cementing protein to stabilize the capsid shells and spikes in the full particles and during cell entry. Structural transition from BAV virions to cores is a stepwise process of dissociation of receptor binding protein VP9 and membrane penetration protein VP4.
A study reports cryogenic electron microscopy structures of the respiratory syncytial virus polymerase bound to its genomic and antigenomic viral RNA promoters.
Single-particle cryo-electron microscopy structures of HIV-1 envelope (Env) trimers bound to one or two CD4 receptors identify intermediate Env conformations that precede host–virus fusion and inform the design of therapeutics to prevent HIV-1 infection.
To read and transcribe the viral genome, the polymerase complex of human metapneumovirus (HMPV) needs to attach to the nucleocapsid. Here, the authors define the dynamic basis of how the polymerase cofactor P facilitates this attachment.
This study reveals that a cross-neutralizing antibody targets a conserved site on betacoronavirus spike proteins and confers protection against SARS-CoV-2 infection.
This study provides ultrastructural evidence that the HIV-1 capsid can enter the nucleus of an infected T cell line through the nuclear pore complex and fragments in the nucleoplasm to release the viral genome.