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Baculoviruses are large DNA virus widely used as biotechnological tools. Here, authors present the complete cryoEM structure of a circulating nucleocapsid, including the DNA packaging and exiting hub termed the apical cap.
Sialoglycan receptor binding promotes the D2 ___domain up conformation in the HKU1 coronavirus spike protein. Here the authors show that this conformational change is driven fundamentally by the full structuring of the canonical embecovirus binding site.
Cryo-EM structures of measles virus polymerase complexes reveal their architecture and show how the C protein remodels the polymerase to regulate RNA synthesis, offering new insights into replication mechanisms and potential antiviral targets.
Here, the authors have mapped the antibody response of the adeno-associated virus 9 (AAV9) gene therapy vector Zolgensma. AAV9 capsid variants were designed to escape this response while preserving manufacturing and biodistribution properties.
The cryo-EM structure of phage φTE is presented, revealing a distinct neck topology, tail sheath baseplate organization and oligomeric state of the tape measure protein. These features suggest a mechanism linking base plate conformational changes to sheath contraction and genome ejection.
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.
