IgCaller is a python program designed to fully characterize the immunoglobulin gene rearrangements and oncogenic translocations in lymphoid neoplasms. It was originally developed to work with WGS data but it has been extended to work with WES and high-coverage, capture-based NGS data.

The avian immune system exhibits a unique immunoglobulin (Ig) system characterized by distinct features absent in other vertebrates. Birds possess a specialized IgY, which serves as the functional equivalent to mammalian IgG and IgE, but with significant structural and functional differences. Unlike mammalian systems, birds utilize a limited number of germline gene segments and rely on gene conversion within the bursa of Fabricius to generate antibody diversity. This mechanism allows for a rapid and diverse immune response, showcasing the evolutionary adaptation of birds to their ecological niches and pathogen challenges.

The 12/23 rule is fundamental in the V(D)J recombination process, which assembles the variable (V), diversity (D), and joining (J) gene segments in the immune system to create diverse antibodies and T cell receptors. The rule stipulates that recombination can only occur between a gene segment flanked by a recombination signal sequence (RSS) with a 12-base pair (bp) spacer and one with a 23-bp spacer. This ensures proper alignment and prevents inappropriate recombination, thereby maintaining the integrity and functionality of the immune response​.

MGT®, the international ImMunoGeneTics information system®, is a comprehensive resource for immunogenetics and immunoinformatics. It was created and has been developed since 1989 by Professor Marie-Paule Lefranc at the Université de Montpellier, France. IMGT® is recognized as the global reference in immunogenetics and immunoinformatics due to its high-quality, integrated knowledge and its standardized nomenclature.

The flu NA (neuraminidase) protein is crucial because it plays a key role in the influenza virus's ability to infect host cells and spread within the body. It helps the virus to release newly formed viral particles from infected cells, facilitating the spread of the infection. As such, it's a key target for antiviral drugs and vaccine development, helping in controlling and preventing flu outbreaks.

This post provides a detailed exploration of the CR9114 antibody, focusing on its binding properties and effectiveness against various influenza A virus strains. It covers the specific gene segments from which CR9114 is derived, explaining its broad reactivity to both group 1 and group 2 influenza A viruses. The article highlights the significance of the HA stem region in the virus and how CR9114's binding to this region blocks the necessary conformational changes for viral entry into host cells. Additionally, it compares CR9114 to other antibodies like CR6261 and FI6v3, discussing their different binding modes and effectiveness. The content is technical and geared towards readers with a background in biology and immunology.

In the evolving realm of biotechnology, antibodies and phage display stand as two pillars of immense significance. This article delves into the structural intricacies of antibodies, emphasizing their heavy and light chains, along with the pivotal Complementarity-Determining Regions (CDRs). Furthermore, the article illuminates the concept of phage display, a groundbreaking technique that bridges genotypic information with phenotypic expression, offering a high-throughput approach to study protein interactions. Illustrated with detailed visuals, the piece offers readers an in-depth understanding of these subjects, underscoring their paramount importance in modern medicine and research.

Integrins Form an Expanding Diffusional Barrier that Coordinates Phagocytosis