Vaccination induces maturation in a mouse model of diverse unmutated VRC01-class precursors to HIV-n
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SARS-CoV-2 is a betacoronavirus virus responsible for the COVID-19 pandemic. Here, we determine the X-ray crystal structure of a potent neutralizing monoclonal antibody, CV30, isolated from a patient infected with SARS-CoV-2, in complex with the receptor binding domain. The structure reveals that CV30 binds to an epitope that overlaps with the human ACE2 receptor binding motif providing a structural basis for its neutralization. CV30 also induces shedding of the S1 subunit, indicating an additional mechanism of neutralization. A germline reversion of CV30 results in a substantial reduction in both binding affinity and neutralization potential indicating the minimal somatic mutation is needed for potently neutralizing antibodies against SARS-CoV-2.
Upon binding of NifW, a subtle conformation change occurs in NifD 2 K 2 , decreasing the distance between the two [4Fe:4S] clusters precursors of the P-cluster in nitrogenase.
Potential to capture 70% of feedstock carbon while >50% of feedstock lower heating value is converted to biofuel and coproducts.
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