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

- [Instructeur] Antilichamen, ook bekend als immunoglobulinen, zijn belangrijke spelers in de humorale immuunreactie tegen vreemde antigenen. Het zijn eiwitten die bestaan uit vier polypeptiden in een Y-vormig structuur met twee identieke zware en twee identieke lichte ketens met elkaar verbonden door een combinatie van niet-covalente bindingen en covalente disulfidebindingen. Aan de uiteinden van elke polypeptideketen zijn unieke variabele domeinen, die selectief antigenen binden.

Hoewel sommige delen van dit gebied direct op elkaar inwerken, bieden andere delen structurele ondersteuning voor deze bindingsplaatsen. Daarentegen bepaald het stamgebied van het antilichaam, bekend als het constante gebied, het specifieke immunologische werkingsmechanisme van actie afhankelijk van de klasse. Bijvoorbeeld, één type, Immunoglobuline E, wordt als reactie in het lichaam uitgescheiden als een allergeen-achtige kattenhuidschilfers en bemiddelt de allergische reactie.

antibody structure

Overzicht

Antilichamen, ook bekend als immunoglobulinen (Ig), zijn essentiële spelers in het adaptieve immuunsysteem. Deze antigeenbindende eiwitten worden geproduceerd door B-cellen en vormen qua gewicht 20 procent van het totale bloedplasma. Bij zoogdieren vallen antilichamen onder vijf verschillende klassen, die elk een andere biologische reactie op antigeenbinding uitlokken.

De Y-vormige structuur van antilichamen bestaat uit vier polypeptideketens

Antilichamen bestaan uit vier polypeptideketens: twee identieke zware ketens van elk ongeveer 440 aminozuren, en twee identieke lichte ketens van elk ongeveer 220 aminozuren. Deze ketens zijn gerangschikt in een Y-vormige structuur die bij elkaar wordt gehouden door een combinatie van covalente disulfidebindingen en niet-covalente bindingen. Bovendien dragen de meeste antilichamen suikerresiduen. Het proces waarbij suikerzijketens aan een eiwit worden toegevoegd, wordt glycosylatie genoemd.

De subeenheden van een antilichaam hebben verschillende functies

Zowel de lichte keten als de zware keten dragen bij aan de antigeenbindingsplaats aan elk van de uiteinden van de Y-structuur. Deze 110-130 aminozuren zijn zeer variabel, waardoor herkenning van een vrijwel onbeperkt aantal antigenen mogelijk is. Dit gebied wordt ook wel het variabele gebied genoemd en maakt deel uit van het antigeenbindende fragment.

Elke arm van de Y-vormige eenheid draagt een identieke antigeenbindingsplaats. Antilichamen kunnen antigenen verknopen: wanneer de ene arm zich aan het ene antigeen bindt en de andere arm aan een tweede, structureel identiek antigeen. Crosslinking wordt vergemakkelijkt door het flexibele scharniergebied dat de armen van het antilichaam met de stengel verbindt en variabele afstanden tussen antigeenbindingsplaatsen mogelijk maakt. Grote roosters van verknoopte antigenen worden vervolgens sneller en gemakkelijker door macrofagen overspoeld, waardoor grotere hoeveelheden van het antigeen in één keer worden verwijderd.

Het stamgebied van het antilichaam wordt ook wel het fragmentkristalliseerbare (Fc) gebied genoemd en bepaalt de effectorfunctie van het antilichaam. Via het Fc-domein kan het antilichaam interageren met Fc-receptoren op andere immuuncellen, zoals B-cellen, macrofagen en mestcellen. Het Fc-gebied is vaak geglycosyleerd, waardoor toegang tot de Fc-receptor wordt belemmerd of mogelijk wordt gemaakt. Het veranderen van de glycosyleringstoestand van het antilichaam maakt daarom een snelle modulatie van de antilichaamfunctie mogelijk.

Zoogdieren hebben vijf klassen antilichamen

Antilichamen worden geclassificeerd op basis van het aantal Y-vormige structuren en het type zware ketens. Antilichamen van de klasse IgD, IgE en IgG hebben een enkele Y-vormige structuur, die twee identieke antigeenbindingsplaatsen aan de uiteinden van hun armen verschaft. In meer wetenschappelijke termen: ze hebben een valentie van twee. IgD, IgE en IgG verschillen echter in de samenstelling van disulfide- en niet-covalente bindingen tussen hun twee zware ketens. IgA kan voorkomen als monomeer of als dimeer, vergelijkbaar met twee Y's die aan hun basis met elkaar zijn verbonden. Als dimeer heeft IgA vier identieke antigeenbindingsplaatsen – een valentie van vier. IgM kan voorkomen als monomeer, maar wordt vaker aangetroffen als pentameer, waardoor het een valentie van 10 heeft.

De vijf klassen antilichamen activeren verschillende immuunfuncties

IgG-antilichamen zijn de meest voorkomende antilichaammoleculen in het bloed en worden in grote hoeveelheden uitgescheiden wanneer een specifiek pathogeen voor de tweede keer wordt aangetroffen. IgG's dragen op verschillende manieren bij aan de eliminatie van pathogenen. Ze opsoniseren pathogenen om fagocytose door macrofagen of neutrofielen te veroorzaken. De activiteit van deze fagocytische cellen wordt versterkt door het complementsysteem, een cascade van enzymatische eiwitten. Het complementsysteem wordt zelf geactiveerd door IgG. Bovendien zijn IgG's de enige antilichamen die de placenta van de moeder naar de foetus kunnen passeren. Ze worden ook uitgescheiden in de moedermelk en bieden daardoor een passieve immuniteit die het kind tegen infecties beschermt.

IgA beschermt slijmvliesoppervlakken zoals het maagdarmkanaal, de luchtwegen en urogenitale kanalen. Het neutraliseert vooral bacteriën en verhindert hun beweging door het epitheel. IgA wordt ook uitgescheiden in slijm, tranen, speeksel en colostrum (de antilichaamrijke afscheiding van de borst van een moeder gedurende de eerste dagen na de bevalling). IgA komt voor als dimeer wanneer het wordt uitgescheiden en als monomeer in lichaamsvloeistoffen.

Monomeren van de IgM-klasse verschijnen als eerste op naïeve B-cellen. IgM's vormen de belangrijkste klasse antilichamen die door B-cellen worden uitgescheiden als reactie op de eerste blootstelling aan een antigeen: de primaire antilichaamreactie. Wanneer een antigeen zich aan een IgM-molecuul bindt, activeert het het complementsysteem en neutraliseert het ziekteverwekkers.

De functies van IgD-antilichamen zijn niet goed begrepen, maar lijken op die van IgM.

IgE is een uitdaging om te bestuderen vanwege hun lage niveaus in lichaamsvloeistoffen en staat vooral bekend om hun negatieve invloed op het menselijk welzijn: allergieën. Tijdens een allergische reactie bindt IgE zich aan zijn verwante antigeen. Vervolgens bindt het Fc-gebied van IgE zich aan mestcellen en basofielen, een soort witte bloedcellen. De interactie van IgE en de Fc-receptor op het celoppervlak veroorzaakt de afgifte van histaminen en interleukines, die op hun beurt allergische reacties veroorzaken.

Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced ...

Education

JoVE Core

Molecular Biology

Moleculaire biologie

Unit 1

Protein Structure

Eiwitstructuur

KEY TERMS AND CONCEPTS

BELANGRIJKE TERMEN EN CONCEPTEN

Antilichaamstructuur

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...

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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

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Arizona Science Standards

Life Science

HS+B.L1

HS+B.L1U1.5

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BIO1.LS1.6

Antibody Heavy and Light Chains

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