Radio-transparent dipole antenna based on a metasurface cloak.

Antenna technology is at the basis of ubiquitous wireless communication systems and sensors. Radiation is typically sustained by conduction currents flowing around resonant metallic objects that are optimized to enhance efficiency and bandwidth. However, resonant conductors are prone to large scattering of impinging waves, leading to challenges in crowded antenna environments due to blockage and distortion. Metasurface cloaks have been explored in the quest of addressing this challenge by reducing antenna scattering. However, metasurface-based designs have so far shown limited performance in terms of bandwidth, footprint and overall scattering reduction. Here we introduce a different route towards radio-transparent antennas, in which the cloak itself acts as the radiating element, drastically reducing the overall footprint while enhancing scattering suppression and bandwidth, without sacrificing other relevant radiation metrics compared to conventional antennas. This technique opens opportunities for cloaking technology, with promising features for crowded wireless communication platforms and noninvasive sensing.

Analysis of the role of tripeptidyl peptidase II in MHC class I antigen presentation in vivo.

Previous experiments using enzyme inhibitors and RNA interference in cell lysates and cultured cells have suggested that tripeptidyl peptidase II (TPPII) plays a role in creating and destroying MHC class I-presented peptides. However, its precise contribution to these processes has been controversial. To elucidate the importance of TPPII in MHC class I Ag presentation, we analyzed TPPII-deficient gene-trapped mice and cell lines from these animals. In these mice, the expression level of TPPII was reduced by >90% compared with wild-type mice. Thymocytes from TPPII gene-trapped mice displayed more MHC class I on the cell surface, suggesting that TPPII normally limits Ag presentation by destroying peptides overall. TPPII gene-trapped mice responded as well as did wild-type mice to four epitopes from lymphocytic choriomeningitis virus. The processing and presentation of peptide precursors with long N-terminal extensions in TPPII gene-trapped embryonic fibroblasts was modestly reduced, but in vivo immunization with recombinant lentiviral or vaccinia virus vectors revealed that such peptide precursors induced an equivalent CD8 T cell response in wild-type and TPPII-deficient mice. These data indicate that while TPPII contributes to the trimming of peptides with very long N-terminal extensions, TPPII is not essential for generating most MHC class I-presented peptides or for stimulating CTL responses to several Ags in vivo.