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The Einstein Telescope (ET) is a third generation gravitational wave detector that includes a room-temperature high-frequency (ET-HF) and a cryogenic low-frequency laser interferometer (ET-LF). The cryogenic ET-LF is crucial for exploiting the full scientific potential of ET. We present a new baseline design for the cryogenic payload that is thermally and mechanically consistent and compatible with the design sensitivity curve of ET. The design includes two options for the heat extraction from the marionette, based on a monocrystalline high-conductivity marionette suspension fiber and a thin-wall titanium tube filled with static He-II, respectively. Following a detailed description of the design options and the suspension thermal noise (STN) modelling, we present the sensitivity curves of the two baseline designs, discuss the influence of various design parameters on the sensitivity of ET-LF and conclude with an outlook to future R&D activities.

The human complement system is an important part of the immune system responsible for lysis and elimination of invading microorganisms and apoptotic body cells. Improper activation of the system due to deficiency, mutations, or autoantibodies of complement regulators, mainly factor H (FH) and FH-related proteins (FHRs), causes severe kidney and eye diseases. However, there is no recombinant FH therapeutic available on the market. The first successful recombinant production of FH was accomplished with the moss bioreactor, . Recently, a synthetic regulator, MFHR1, was designed to generate a multitarget complement inhibitor that combines the activities of FH and the FH-related protein 1 (FHR1). The potential of MFHR1 was demonstrated in a proof-of-concept study with transiently transfected insect cells. Here, we present the stable production of recombinant glyco-engineered MFHR1 in the moss bioreactor. The key features of this system are precise genome engineering homologous recombination, Good Manufacturing Practice-compliant production in photobioreactors, high batch-to-batch reproducibility, and product stability. Several potential biopharmaceuticals are being produced in this system. In some cases, these are even biobetters, i.e., the recombinant proteins produced in moss have a superior quality compared to their counterparts from mammalian systems as for example moss-made aGal, which successfully passed phase I clinical trials. mass spectrometry-based analysis of moss-produced MFHR1, we now prove the correct synthesis and modification of this glycoprotein with predominantly complex-type N-glycan attachment. Moss-produced MFHR1 exhibits cofactor and decay acceleration activities comparable to FH, and its mechanism of action on multiple levels within the alternative pathway of complement activation led to a strong inhibitory activity on the whole alternative pathway, which was higher than with the physiological regulator FH.