Chicken Ig-like receptor B2, a member of a multigene family, is mainly expressed on B lymphocytes, recruits both Src homology 2 domain containing protein tyrosine phosphatase (SHP)-1 and SHP-2, and inhibits proliferation

Ig-like inhibitory receptors have been the focus of intensive research particularly in mouse and human. We report the cloning and characterization of three novel inhibitory chicken Ig-like receptors (CHIR) that display a two Ig-domain extracellular structure, a transmembrane region lacking charged residues and a cytoplasmic domain containing two ITIM. The localization of all receptors to a small genomic region and the hybridization pattern indicated that they belong to a multigene family. The genomic structure of the extracellular domain with two exons encoding the signal peptide and single exons for each Ig domain resembled that of all human leukocyte Ig-like receptors and killer cell Ig-like receptors, whereas the exons encoding the C terminus displayed a structure closely resembling killer cell Ig-like receptor genes. A mAb generated against one receptor designated CHIR-132 reacted with all B cells and a small T cell subset, but not with monocytes, thrombocytes, or various leukocyte-derived cell lines. The mAb immunoprecipitated a 46-kDa protein from bursal cells and transfected cells. The Src homology 2 domain containing protein tyrosine phosphatase (SHP)-2 bound to CHIR-132 even in unstimulated cells, whereas pervanadate treatment induced the tyrosine phosphorylation and recruitment of several CHIR-B2-associated proteins including SHP-1 and increased levels of SHP-2. Moreover, mAb cross-linking of CHIR-132 reduced the proliferation of a stable transfected cell line. Together, we have identified a multigene family containing multiple CHIR including one receptor designated CHIR-132 that is mainly expressed on B lymphocytes and inhibits cellular proliferation by recruitment of SHP-1 and SHP-2

Production of structured soy-based meat analogues using simple shear and heat in a Couette Cell

A Couette Cell device was employed to provide proof of concept for the production of structured meat analogues by application of simple shear flow and heat to a 31 wt% Soy Protein Isolate (SPI)–Wheat Gluten (WG) dispersion. Three relevant process parameters (temperature, time and rotation rate) were varied over a range of realistic values (90–110 °C, 5–25 min and 5–50 RPM, respectively). Layer- or fibre-structured products with high stress and strain anisotropy indices have been demonstrated. Fibrousness is favoured at temperatures over 90 °C and under 100 °C, whereas the role of process time and rotation rate is not critical. Simultaneous application of simple shear and heat is the key to obtaining structured plant protein-based products. The Couette Cell concept is scalable and can enable continuous operation. On this ground, it appears as a realistic option for production of meat analogues at commercial scale

Production of structured soy-based meat analogues using simple shear and heat in a Couette Cell

A Couette Cell device was employed to provide proof of concept for the production of structured meat analogues by application of simple shear flow and heat to a 31 wt% Soy Protein Isolate (SPI)–Wheat Gluten (WG) dispersion. Three relevant process parameters (temperature, time and rotation rate) were varied over a range of realistic values (90–110 °C, 5–25 min and 5–50 RPM, respectively). Layer- or fibre-structured products with high stress and strain anisotropy indices have been demonstrated. Fibrousness is favoured at temperatures over 90 °C and under 100 °C, whereas the role of process time and rotation rate is not critical. Simultaneous application of simple shear and heat is the key to obtaining structured plant protein-based products. The Couette Cell concept is scalable and can enable continuous operation. On this ground, it appears as a realistic option for production of meat analogues at commercial scale

A novel activating chicken IgY FcR is related to leukocyte receptor complex (LRC)

FcRs have multifaceted roles in the immune system. Chicken FcRs were demonstrated on macrophages decades ago; however, only recently the chicken Ig-like receptor AB1, encoded in the leukocyte receptor complex, was molecularly identified as a high-affinity FcR. The present study was initiated to identify additional receptors with the capability to bind chicken immunoglobulins. Based on database searches, we cloned a novel chicken FcR, designated gallus gallus FcR (ggFcR), which was shown to bind selectively chicken IgY. The receptor consists of four extracellular C2-set Ig domains, followed by a transmembrane region containing arginine as a positively charged amino acid and a short cytoplasmic tail. ggFcR associates with the common -chain, indicative for an activating receptor, and real-time RT-PCR revealed high expression on PBMC, thrombocytes, and macrophages. The genomic organization is similar to most Ig-like receptor genes, where each Ig domain is encoded by a separate exon. Additionally, the ggFcR signal peptide is encoded by two exons, the second of which is 36 bp, a hallmark for genes encoded in the leukocyte receptor complex. Phylogenetic analysis also showed a relationship to genes encoded in the leukocyte receptor complex. Surprisingly, ggFcR is not encoded in the leukocyte receptor complex, but it is located as a single isolated gene at the extremity of chicken chromosome 2