Specific antiviral activities of the human α interferons are determined at the level of receptor (IFNAR) structure

AbstractDifferences in activity among the family of human IFNs α are much reduced if these ligands are assayed on bovine cells. In particular, the activity of IFN αD is much higher on bovine than on human cells. To examine these differences, the bovine counterpart of the human IFNAR has been cloned and expressed in a human cell line. The transfected cell line now recognizes the human IFN αD as a high-specific-activity IFN subtype, indicating that the differences in sensitivity between the bovine and human cells to the human IFN α lie in the structure of the IFNAR chain rather than in the other components of the functional receptor

Low-complexity BCH codes with optimized interleavers for DQPSK systems with laser phase noise

The presence of high phase noise in addition to additive white Gaussian noise in coherent optical systems affects the performance of forward error correction (FEC) schemes. In this paper, we propose a simple scheme for such systems, using block interleavers and binary Bose–Chaudhuri–Hocquenghem (BCH) codes. The block interleavers are specifically optimized for differential quadrature phase shift keying modulation. We propose a method for selecting BCH codes that, together with the interleavers, achieve a target post-FEC bit error rate (BER). This combination of interleavers and BCH codes has very low implementation complexity. In addition, our approach is straightforward, requiring only short pre-FEC simulations to parameterize a model, based on which we select codes analytically. We aim to correct a pre-FEC BER of around (Formula presented.). We evaluate the accuracy of our approach using numerical simulations. For a target post-FEC BER of (Formula presented.), codes selected using our method result in BERs around 3(Formula presented.) target and achieve the target with around 0.2 dB extra signal-to-noise ratio

Distinct domains of the protein tyrosine kinase tyk2 required for binding of interferon-a/b and for signal transduction

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The Two Groups of Zebrafish Virus-Induced Interferons Signal via Distinct Receptors with Specific and Shared Chains

International audienceBecause the availability of fish genomic data, the number of reported sequences for fish type II helical cytokines is rapidly growing, featuring different IFNs including virus-induced IFNs (IFN_) and IFN-_, and IL-10 with its related cytokines (IL-20, IL-22, and IL-26). Many candidate receptors exist for these cytokines and various authors have postulated which receptor chain would be involved in which functional receptor in fish. To date, only the receptor for zebrafish IFN_1 has been identified functionally. Three genes encoding virus-induced IFN_s have been reported in zebrafish. In addition to these genes clustered on chromosome 3, we have identified a fourth IFN_ gene on chromosome 12. All these genes possess the intron-exon organization of mammalian _ IFNs. In the zebrafish larva, all induce the expression of reporter antiviral genes; protection in a viral challenge assay was observed for IFN_1 and IFN_2. Using a combination of gain- and loss-of-function experiments, we also show that all zebrafish IFN_s do not bind to the same receptor. Two subgroups of fish virus-induced IFNs have been defined based on conserved cysteines, and we find that this subdivision correlates with receptor usage. Both receptor complexes include a common short chain receptor (CRFB5) and a specific long chain receptor (CRFB1 or CRFB2)

Insecticide resistance in mosquito vectors

Resistance to insecticides among mosquitoes that act as vectors for malaria (Anopheles gambiae) and West Nile virus (Culex pipiens) emerged more than 25 years ago in Africa, America and Europe; this resistance is frequently due to a loss of sensitivity of the insect's acetylcholinesterase enzyme to organophosphates and carbamates1. Here we show that this insensitivity results from a single amino-acid substitution in the enzyme, which we found in ten highly resistant strains of C. pipiens from tropical (Africa and Caribbean) and temperate (Europe) areas, as well as in one resistant African strain of A. gambiae. Our identification of this mutation may pave the way for designing new insecticides