An outbreak of coronavirus disease 2019 (COVID-19) 1-3 , caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) 4 , has spread globally. Countermeasures are needed to treat and prevent further dissemination of the virus. Here we report the isolation of two specific human monoclonal antibodies (termed CA1 and CB6) from a patient convalescing from COVID-19. CA1 and CB6 demonstrated potent SARS-CoV-2-specific neutralization activity in vitro. In addition, CB6 inhibited infection with SARS-CoV-2 in rhesus monkeys in both prophylactic and treatment settings. We also performed structural studies, which revealed that CB6 recognizes an epitope that overlaps with angiotensin-converting enzyme 2 (ACE2)-binding sites in the SARS-CoV-2 receptor-binding domain, and thereby interferes with virus-receptor interactions by both steric hindrance and direct competition for interface residues. Our results suggest that CB6 deserves further study as a candidate for translation to the clinic.

Named Data Networking (NDN) is one of five projects funded by the U.S. National Science Foundation under its Future Internet Architecture Program. NDN has its roots in an earlier project, Content-Centric Networking (CCN), which Van Jacobson first publicly presented in 2006. The NDN project investigates Jacobson's proposed evolution from today's host-centric network architecture (IP) to a data-centric network architecture (NDN). This conceptually simple shift has far-reaching implications for how we design, develop, deploy, and use networks and applications. We describe the motivation and vision of this new architecture, and its basic components and operations. We also provide a snapshot of its current design, development status, and research challenges. More information about the project, including prototype implementations, publications, and annual reports, is available on named-data.net.

The transthyretin amyloidoses (ATTR) are invariably fatal diseases characterized by progressive neuropathy and/or cardiomyopathy. ATTR are caused by aggregation of transthyretin (TTR), a natively tetrameric protein involved in the transport of thyroxine and the vitamin A–retinol-binding protein complex. Mutations within TTR that cause autosomal dominant forms of disease facilitate tetramer dissociation, monomer misfolding, and aggregation, although wild-type TTR can also form amyloid fibrils in elderly patients. Because tetramer dissociation is the rate-limiting step in TTR amyloidogenesis, targeted therapies have focused on small molecules that kinetically stabilize the tetramer, inhibiting TTR amyloid fibril formation. One such compound, tafamidis meglumine (Fx-1006A), has recently completed Phase II/III trials for the treatment of Transthyretin Type Familial Amyloid Polyneuropathy (TTR-FAP) and demonstrated a slowing of disease progression in patients heterozygous for the V30M TTR mutation. Herein we describe the molecular and structural basis of TTR tetramer stabilization by tafamidis. Tafamidis binds selectively and with negative cooperativity (K d s ∼2 nM and ∼200 nM) to the two normally unoccupied thyroxine-binding sites of the tetramer, and kinetically stabilizes TTR. Patient-derived amyloidogenic variants of TTR, including kinetically and thermodynamically less stable mutants, are also stabilized by tafamidis binding. The crystal structure of tafamidis-bound TTR suggests that binding stabilizes the weaker dimer-dimer interface against dissociation, the rate-limiting step of amyloidogenesis.

Trifluorophenyl‐functionalized multi‐walled‐carbon‐nanotube/poly(vinylidene fluoride) (TFP‐MWNT/PVDF) nanocomposites are fabricated by employing a wet‐chemistry route. The modified MWNTs are observed to form a well‐dispersed, structurally random nanophase within the polymer matrix (see figure). The TFP‐MWNT/PVDF nanocomposite exhibits enhanced dielectric permittivity when the content of TFP‐MWNT is close to the percolation threshold.

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