Name: antibody heavy and light chains
Uploaded: 2020-11-23T11:47:34.000Z
Duration: 1 min 10 s
Channel: JoVE

K12 Standards

Tennessee Academic Standards

High School

Biology

from-molecules-to-organisms-structures-and-processes

From Molecules to Organisms: Structures and Processes

BIO1.LS1.3

Antibody Structure

Des anticorps, aussi connus sous le nom d'immunoglobulines,sont des acteurs clés de la réponse immunitaire humoralecontre les antigènes étrangers. 
Ce sont des protéines constituées de quatre polypeptidesdans une structure en forme de Y,avec deux chaînes lourdes identiqueset deux chaînes légères identiques,liées entre elles par une combinaisonde liaisons non-covalenteset de liaisons disulfure covalentes. 
Aux extrémités mêmes de chaque chaîne polypeptidiqueil y a des domaines variables uniquesqui se lient sélectivement aux antigènes. 
Bien que certaines parties de cette régionpeuvent interagir directement,d'autres parties assurent un soutien structurelpour ces sites de fixation. 
En revanche, la région de la tige de l'anticorps,connue sous le nom de région constante,détermine le mécanisme d'action immunologique spécifique,en fonction de la classe. 
Par exemple, un type, l'immunoglobuline E,est sécrétée dans l'organisme en réponse à un allergènecomme les phanères de chat et servent de médiateurà la réaction allergique.

Silverton, E. W., M. A. Navia et D. R. Davies. « Structure tridimensionnelle d’une immunoglobuline humaine intacte. » Actes de l’Académie nationale des sciences 74, n° 11 (1er novembre 1977) : 5140-44. [<a href="https://doi.org/10.1073/pnas.74.11.5140 » target="__blank">Source</a>]

structure des anticorps

<h4>Aperçu</h4>
 
 Les anticorps, également connus sous le nom d’immunoglobulines (Ig), sont des acteurs essentiels du système immunitaire adaptatif. Ces protéines liant les antigènes sont produites par les cellules B et représentent 20 pour cent du plasma sanguin total en poids. Chez les mammifères, les anticorps se divisent en cinq classes différentes, qui provoquent toutes une réponse biologique différente avec la fixation de l’antigène.
 
 <h4>La structure en forme de Y des anticorps se compose de quatre chaînes polypeptidiques</h4>
 
 Les anticorps se composent de quatre chaînes de polypeptides : deux chaînes lourdes identiques d’environ 440 acides aminés chacune, et deux chaînes légères identiques composées d’environ 220 acides aminés chacune. Ces chaînes sont disposées dans une structure en forme de Y qui est maintenue par une combinaison de liaisons disulfure covalentes et de liaisons non covalentes. En outre, la plupart des anticorps transportent des résidus de sucre. Le processus d’addition des chaînes latérales de sucre à une protéine s’appelle la glycosylation.
 
 <h4>Les sous-unités d’un anticorps ont des fonctions différentes</h4>
 
 La chaîne légère et la chaîne lourde contribuent toutes deux au site de fixation de l’antigène à chacune des extrémités de la structure en Y. Ces 110-130 acides aminés sont très variables pour permettre la reconnaissance d’un nombre presque illimité d’antigènes. Cette région est également appelée la région variable et fait partie du fragment de fixation de l’antigène.
 
 Chaque bras de l’unité en forme de Y porte un site identique de fixation de l’antigène. Les anticorps peuvent réticuler les antigènes : lorsqu’un bras se lie à un antigène et que l’autre bras se lie à un deuxième antigène structuralement identique. La réticulation est facilité par la région de charnière flexible qui relie les bras de l’anticorps à la tige et permet des distances variables entre les sites de fixation de l’antigène. Les grands réseaux d’antigènes réticulés sont ensuite engloutis plus rapidement et plus facilement par les macrophages, éliminant ainsi de plus grandes quantités de l’antigène à la fois.
 
 La région de la tige de l’anticorps est également appelée la région du fragment cristallisable (Fc) et détermine la fonction effectrice de l’anticorps. Par le biais du domaine Fc, l’anticorps peut interagir avec les récepteurs Fc sur d’autres cellules immunitaires, telles que les cellules B, les macrophages et les mastocytes. La région Fc est souvent glycosylée, ce qui entrave ou permet l’accès aux récepteurs Fc. La modification de l’état de glycosylation de l’anticorps permet donc une modulation rapide de la fonction des anticorps.
 
 <h4>Les mammifères ont cinq catégories d’anticorps</h4>
 
 Les anticorps sont classés selon leur nombre de structures en forme de Y et leur type de chaînes lourdes. Les anticorps de la classe IgD, IgE et IgG ont une structure unique en forme de Y, fournissant deux sites identiques de fixation d’antigènes au bout de leurs bras. En termes plus scientifiques : ils ont une valence de deux. Les IgD, IgE et IgG diffèrent toutefois dans la composition des liaisons disulfure et non covalentes entre leurs deux chaînes lourdes. L‘IgA peut exister en tant que monomère ou en tant que dimère, ressemblant à deux Y qui se joignent à leur base. En tant que dimère, l’IgA a quatre sites identiques de fixation de l’antigène : une valence de quatre. L‘IgM peut exister en tant que monomère, mais on la rencontre plus souvent en tant que pentamère, ce qui lui donne une valence de 10. 
 
 <h4>Les cinq classes d’anticorps déclenchent différentes fonctions immunitaires</h4>
 
 Les anticorps IgG sont les molécules d’anticorps les plus abondantes dans le sang et sont sécrétés en grands volumes lorsqu’un agent pathogène spécifique est rencontré pour la deuxième fois. Les IgG contribuent à l’élimination des agents pathogènes de plusieurs façons. Elles opsonisent les agents pathogènes pour déclencher leur phagocytose par les macrophages ou les neutrophiles. L’activité de ces cellules phagocytaires est renforcée par le système du complément, une cascade de protéines enzymatiques. Le système du complément est lui-même déclenché par les IgG. En outre, les IgG sont les seuls anticorps qui peuvent traverser le placenta de la mère au fœtus. Elles sont également sécrétées dans le lait de la mère, offrant ainsi une immunité passive qui protège le nourrisson contre les infections.
 
 L’IgA protège les surfaces muqueuses telles que les voies gastro-intestinales, respiratoires et urogénitales. Elle neutralise avant tout les bactéries, empêchant leur mouvement à travers l’épithélium. L’IgA est également sécrétée dans le mucus, les larmes, la salive et le colostrum (la sécrétion riche en anticorps du sein d’une mère pendant les premiers jours après l’accouchement). L’IgA existe en tant que dimère lorsqu’elle est sécrétée et en tant que monomère dans les fluides corporels.
 
 Les monomères de la classe IgM sont les premiers à apparaître sur les cellules B naïves. Les IgM sont la principale classe d’anticorps sécrétés par les cellules B en réponse à la première exposition à un antigène, la réponse primaire des anticorps. Lorsqu’un antigène se lie à une molécule d’IgM, il active le système du complément et neutralise les agents pathogènes.
 
 Les fonctions des anticorps IgD ne sont pas bien comprises mais semblent ressembler à des celles de l’IgM.
 
 Les IgE sont difficiles à étudier en raison de leurs niveaux faibles dans les fluides corporels et sont surtout connues pour leur impact négatif sur le bien-être humain : les allergies. Lors d’une réaction allergique, l’IgE se lie à son antigène apparenté. Par la suite, la région Fc de l’IgE se lie aux mastocytes et aux basophiles, un type de globule blanc. L’interaction de l’IgE et du récepteur Fc sur la surface cellulaire provoque la libération d’histamines et d’interleukines, ce qui provoque à son tour des symptômes allergiques tels que des éternuements et des démangeaisons.
 
 <h4>Les anticorps pour la recherche, le diagnostic et les thérapies sont produits dans les animaux</h4>
 
 Les anticorps sont un outil important dans de nombreuses disciplines de recherche ainsi que dans le diagnostic, et parfois le traitement de la maladie. Pour produire des anticorps, un antigène est injecté dans un animal de ferme ou de laboratoire, souvent des lapins, des poulets, des hamsters ou des chèvres, et il est plus tard isolé à partir du sang de l’animal.

Structure des anticorps

Aperçu
Les anticorps, également appelés immunoglobulines (Ig), sont des acteurs essentiels du système immunitaire adaptatif. Ces protéines de liaison à l’antigène sont produites ...

Education

Enseignement

JoVE Core

Molecular Biology

Biologie moléculaire

Unit 1

Unité 1

Protein Structure

Structure des protéines

KEY TERMS AND CONCEPTS

TERMES ET CONCEPTS CLÉS

antibody heavy and light chains

Antibodies are built from heavy and light chains that work together to form a Y-shaped molecule. These chains give the antibody its basic structure and help it bind to specific targets.

The two upper arms of the Y contain the variable regions, which differ from one antibody to another. These variable regions help determine which antigen, or foreign molecule, the antibody can recognize.

The lower part of the antibody is the constant region. This region is more similar across antibodies and helps define the antibody class. The structure of the chains also supports the antibody’s overall shape and function.

Antibody Heavy and Light Chains

what are proteins?

Proteins, Amino Acids, and Polypeptides

Proteins are built from amino acids and form polypeptides. Amino acids are the small building blocks, and a polypeptide is a chain of amino acids joined together. This basic relationship explains how proteins are made and why their structure matters. Proteins have several important roles in living things. Some proteins help build body structures, while others carry out work inside cells. The transcript also connects proteins to enzymes, which are proteins that speed up chemical reactions.

protein organization

Protein Organization and Folding Levels

Protein organization describes how a protein is arranged at several levels. These levels help explain how a chain of amino acids becomes a working molecule. The main stages are primary, secondary, tertiary, and quaternary structure. Primary structure is the linear order of amino acids in the protein chain. Secondary structure is the first step of folding. In this stage, the chain can form patterns such as helices and sheets. Tertiary structure is the overall three-dimensional shape of one...

protein folding

Protein Folding and Structure

Protein folding is the process that gives a protein its final three-dimensional shape. That shape is essential because a protein’s structure helps determine how it works in the cell. A folded protein is stabilized by several interactions. These include hydrogen bonds, van der Waals interactions, and disulfide bridges. Each one helps hold the protein in the correct form. When a protein does not fold properly, its structure can change. That can affect its function and can interfere with normal...

conservation of protein domains over different proteins

conservation-of-protein-domains-over-different-proteins

Argonaute Protein Domains Across Species

Argonaute proteins have conserved domains that help small RNAs guide gene silencing. These proteins are found across organisms, but the number of Argonaute family members can differ from one species to another. Protein domains are small, structurally independent parts of a single amino acid chain. They can keep their shape on their own, but they may still work together with other parts of the protein. During evolution, domains can duplicate, recombine, and form new combinations. This process,...

globular and fibrous proteins

Protein Shapes: Globular vs Fibrous

Proteins can be grouped by shape into globular proteins and fibrous proteins. These two subtypes also differ in how they dissolve in water and in the jobs they do in cells and tissues. Globular proteins, also called spheroproteins, are usually round in shape. They contain a mix of amino acid types and varied primary sequences. Their shapes support many functions, including enzymes, cellular messengers, and molecular transporters. These roles often need the proteins to stay soluble in the...

intrinsically disordered proteins

Flexible Protein Regions and Binding

Intrinsically disordered proteins are proteins that do not fold into one fixed three-dimensional shape. Their flexible structure helps them work with ordered proteins to do jobs that rigid proteins cannot easily do. They are found more often in eukaryotes than in prokaryotes, and they can be fully disordered or made of both ordered and disordered regions. This lack of a rigid shape is linked to amino acid makeup. These proteins usually have many polar and charged amino acids and fewer...

protein complex assembly

How Proteins Self-Assemble in Cells

Proteins can self-assemble into working complexes inside cells. Some complexes are homomeric, which means they contain more than one copy of the same protein. Others are heteromeric, which means they are built from different protein types. Most protein complexes form through ordered self-assembly. In some cases, assembly factors help guide the proteins into the correct structure. Even in the crowded space inside a cell, proteins usually find the right partners and form functional complexes. <br...

conjugated proteins

Conjugated Proteins and Their Roles

Conjugated proteins are proteins that bond with a non-protein part. Unlike simple proteins, which contain only amino acids, these protein complexes include another chemical moiety attached covalently. That extra part can change how the protein works in the body. Nucleoproteins are conjugated proteins that contain nucleic acids. They are grouped as deoxyribonucleoproteins (DNPs) or ribonucleoproteins (RNPs). A nucleosome is a common DNP example, where nuclear DNA is associated with histone...

amyloid fibrils

Amyloid Fibrils in Brain Disease

Amyloid fibrils are clumps of misfolded proteins linked to brain disease and other disorders. In normal cells, misfolded proteins are usually refolded by chaperone proteins or broken down by the proteasome. But in some mutations or diseases, these proteins can build up into large clusters and then assemble into long fibers called fibrils. Amyloid deposits were seen as early as 1639 in the liver and spleen. In 1854, Rudolph Virchow used iodine staining, a method normally used to identify...

antibody structure

Antibodies are built from heavy and light chains that work together to form a Y-shaped molecule. These chains give the antibody its basic structure and help it bind to specific targets. The two upper arms of the Y contain the variable regions, which differ from one antibody to another. These variable regions help determine which antigen, or foreign molecule, the antibody can recognize. The lower part of the antibody is the constant region. This region is more similar across antibodies and...

protein families

Protein Families and Superfamilies

Protein families are groups of homologous proteins with similar amino acid sequences and three-dimensional shapes. They often appear after gene duplication, when an extra copy of a gene is added to an organism’s genome. Mutations can then change the amino acids, as long as the protein can still be made correctly. If the new proteins keep similar amino acids in key places, their domains and overall three-dimensional structure can stay similar too. Members of the same family can share as little...

key terms and concepts

Explore how antibody heavy and light chains form a Y-shaped molecule, with variable regions for target binding and a constant region that helps define class.

Antibody Heavy and Light Chains | JoVE K12

molecular biology

JoVE Core Biologie Moléculaire illustre les processus moléculaires au sein de la cellule grâce à des leçons vidéos claires et concises. Les applications de ces concepts sont ensuite démontrées grâce à des expériences concrètes en laboratoire.

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Life Science

HS+B.L1

HS+B.L1U1.5

myJoVE Corporation

Characteristics of Life

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The Tree of Life - Bacteria, Archaea, and Eukaryotes

Prokaryotic Cells

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Size and Structure of Viral Genomes

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Compare and contrast existing models, identify patterns, and use structural and functional evidence to analyze the characteristics of life. Engage in argument about the designation of viruses as non-living based on these characteristics.
EXPLANATION: Students begin to develop patterns of living and non-living organisms in kindergarten and build on detailed characteristics of different classifications of living organisms throughout elementary and middle school. Biology 1 discussions introduce viral particles and viral cycles, building on student understanding of living organisms to engage in an argument regarding the classification of a viral particle as either living or non-living.

BIO1.LS1.1

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Evaluate comparative models of various cell types with a focus on organic molecules that make up cellular structures.
EXPLANATION: Students explicitly discuss the structure and function of major cellular organelles in seventh grade. Building on this understanding, Biology I students should shift their focus to the different types of cells found in organisms and how the role of each cell type relates to its composition and the prevalence of different organelles within that cell. An example might include the absence (or enucleation) of the nucleus in red blood cells in mammals providing for increased levels of oxygen transport in organisms or the lack of centrioles in most neurons. Varying cell types can include both prokaryotic and eukaryotic cell types.

BIO1.LS1.2

Nucleic Acids

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DNA Base Pairing

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The Central Dogma

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DNA Packaging

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Organization of Genes

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Karyotyping

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Replication in Prokaryotes

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Replication in Eukaryotes

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Mutations

Overview

Mutations are changes in the sequence of DNA. These changes can occur spontaneously or they can be induced by exposure to environmental factors. ...

Transcription

Overview
Transcription is the process of synthesizing RNA from a DNA sequence by RNA polymerase. It is the first step in producing a protein from a gene ...

Translation

Lesson: Translation
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RNA Structure

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RNA Stability

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pre-mRNA Processing

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Types of RNA

Overview
Three main types of RNA are involved in protein synthesis: messenger RNA (mRNA), transfer RNA (tRNA), and ribosomal RNA (rRNA). These RNAs ...

MicroRNAs

siRNA - Small Interfering RNAs

Small interfering RNAs, or siRNAs, are short regulatory RNA molecules that can silence genes post-transcriptionally, as well as the transcriptional ...

piRNA - Piwi-interacting RNAs

PIWI-interacting RNAs, or piRNAs, are the most abundant short non-coding RNAs. More than 20,000 genes have been found in humans that code for piRNAs while ...

CRISPR and crRNAs

Bacteria and archaea are susceptible to viral infections just like eukaryotes; therefore, they have developed a unique adaptive immune system to protect ...

lncRNA - Long Non-coding RNAs

In humans, more than 80% of the genome gets transcribed. However, only around 2% of the genome codes for proteins. The remaining part produces non-coding ...

What are Proteins?

Protein Organization

Protein Folding

Protein Families

Protein families are groups of homologous proteins; that is, they have similarities in amino acid sequences and three-dimensional structures. Protein ...

Conservation of Protein Domains Over Different Proteins

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Globular and Fibrous Proteins

Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
Globular ...

Intrinsically Disordered Proteins

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Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.&#160; Most protein complexes ...

Conjugated Proteins

Simple proteins and protein complexes contain only amino acids. In contrast, many other proteins, called conjugated proteins, covalently bond with ...

Allosteric Proteins-ATCase

Binding sites linkages can regulate a protein&#39;s function.&#160; For example, enzyme activity is often regulated through a feedback mechanism where the ...

Amyloid Fibrils

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Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand ...

Phosphorylation

Ligand Binding Sites

Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their ...

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, ...

Protein-protein Interfaces

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GTPases and their Regulation

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Conserved Binding Sites

Many proteins&#8217; biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein ...

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an ...

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The Equilibrium Binding Constant and Binding Strength

The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at ...

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Protein Complexes with Interchangeable Parts

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Cofactors and Coenzymes

Mechanical Protein Functions

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Allosteric Regulation

Structural Protein Function

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Ligand Binding and Linkage

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Protein Networks

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Integrate evidence to develop a structural model of a DNA molecule. Using the model, develop and communicate an explanation for how DNA serves as a template for self-replication and encodes biological information.
EXPLANATION: Discussions of DNA in earlier grades have been limited to discussions of genes and the role of genes in the appearance and activities of an organism. Biology 1 represents a student's introduction to a molecular model of a DNA as well as the organization of DNA into genes and genes subsequently into chromosomes. Students should address interactions between genes in proteins which regulate both the shape and reproduction of DNA molecules. It is important to note that not all segments of DNA are transcribed for proteins. Portions of DNA are involved in regulating the expression of genes or affect the structure of the chromosomes (replication origin, centromeres, and telomeres).

What is the Cell Cycle?

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Interphase

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The Cell Cycle Control System

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S-Cdk Initiates DNA Replication

M-Cdk Drives Transition Into Mitosis

Mitogens and the Cell Cycle

Replicative Cell Senescence

Abnormal Proliferation

cells-coordinate-growth-and-proliferation

Cells Coordinate Growth and Proliferation

Create a model for the major events of the eukaryotic cell cycle, including mitosis. Compare and contrast the rates of cell division in various eukaryotic cell types in multicellular organisms.
EXPLANATION: Students first discuss mitosis in seventh grade, specifically focusing on the role of mitosis in creating genetically identical daughter cells. Biology 1 discussions should connect a student's understanding of gene expression and protein function with the process of mitosis to explore the differentiation of cell types from otherwise identical daughter cells. Discussions should also include varying rates of mitotic division and the relationship between these rates of division and the function of specific cell types within eukaryotic organisms. Examples may include the extremely limited use of mitosis by neurons due to their interconnectedness within neural networks or the rapid rates of mitosis with growing root tips.

BIO1.LS1.6

Antibody Heavy and Light Chains

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