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Videos de Conceptos Relacionados

Diversity of Antigen Receptors01:28

Diversity of Antigen Receptors

Antigen receptors are essential components of the immune system crucial in defending the body against foreign invaders. These receptors are present on the surface of B and T cells, enabling them to recognize antigens and mount an appropriate immune response.
Before encountering any antigen, lymphocytes express these receptors. On B cells, the antigen receptor is a membrane-bound antibody molecule called BCR; on T cells, it is a T cell receptor or TCR. B and T cell receptors are composed of two...
Antibody Structure01:10

Antibody Structure

Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
Antibody Structure01:10

Antibody Structure

Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
Hybridoma Technology01:31

Hybridoma Technology

Hybridoma technology is used for the large-scale production of monoclonal antibodies. Monoclonal antibodies bind to only a single antigenic determinant or epitope. Such antibodies are used in research, diagnostics, and disease therapy. The hybridoma technology established in 1975 by Georges Köhler and Cesar Milstein was awarded the Nobel Prize in Medicine in 1984 for revolutionizing research and therapy.
Hybridoma Selection
Commonly used fusion techniques — electroporation, polyethylene glycol...
Antibody Structure and Classes01:25

Antibody Structure and Classes

Antibodies, also known as immunoglobulins, are produced by B cells in response to foreign substances, such as bacteria and viruses. These proteins are critical for recognizing and neutralizing these substances, protecting the body from potential harm.
The basic structure of an antibody consists of four protein chains: two identical heavy chains and two identical light chains. These chains are held together by disulfide bonds and other non-covalent interactions, forming a Y-shaped structure.

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Identification of Mouse and Human Antibody Repertoires by Next-Generation Sequencing
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Published on: March 15, 2019

La remodelación de la diversidad de anticuerpos.

Feng Wang1, Damian C Ekiert, Insha Ahmad

  • 1Department of Chemistry, The Scripps Research Institute, La Jolla, CA 92037, USA.

Cell
|June 11, 2013
PubMed
Resumen
Este resumen es generado por máquina.

Las vacas poseen anticuerpos únicos con bucles H3 CDR ultralargos que forman minidomaines enlazados con disulfuro. Esta diversidad estructural, generada por la hipermutación somática, mejora el repertorio de anticuerpos bovinos y el reconocimiento de antígenos.

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Área de la Ciencia:

  • Inmunología Inmunología.
  • Biología Estructural Biología estructural.
  • Biología Molecular Biología Molecular

Sus antecedentes:

  • Algunas especies exhiben fuertes respuestas de anticuerpos a pesar de su limitada diversidad genética.
  • El ganado bovino (Bos taurus) tiene un sistema de anticuerpos único caracterizado por largos bucles CDR H3 y pocas regiones V, con un mecanismo de generación de diversidad desconocido.

Objetivo del estudio:

  • Investigar el mecanismo detrás de la generación de diversidad de anticuerpos en el ganado, centrándose en las características únicas de sus bucles CDR H3.
  • Aclarar las bases estructurales y las implicaciones funcionales de las CDR H3 ultralargas en los anticuerpos bovinos.

Principales métodos:

  • Secuenciación profunda de los repertorios de anticuerpos bovinos.
  • Determinación de la estructura cristalina de los anticuerpos bovinos.
  • Análisis de los patrones de hipermutación somática y el sesgo del codón.

Principales resultados:

  • Los bucles H3 de CDR ultralongos en los anticuerpos de ganado bovino contienen numerosas cisteínas, lo que sugiere la formación de minidomaines enlazados con disulfuro.
  • Las estructuras cristalinas revelaron una arquitectura con un "talón" de hebra beta que soporta un dominio diverso de "granula" enlazado con disulfuro.
  • La hipermutación somática de segmentos DH ultralargos, con un sesgo hacia la cisteína, impulsa la generación de diversidad.

Conclusiones:

  • El sistema inmunológico bovino genera diversidad de anticuerpos a través de CDR H3 ultralargos que se pliegan en minidomaines a través de disulfuros generados somáticamente.
  • Estas estructuras únicas de anticuerpos, en particular el dominio de la perilla, se pueden obtener para reconocer antígenos específicos.
  • Los anticuerpos bovinos poseen un mecanismo estructural y generador de diversidad distinto en comparación con otras especies.