Antibodies Flashcards

1
Q

Define antibody

A

an antibody is a protein that is produced in response to a foreign molecule (antigen), and has the property of binding specifically to that antigen

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2
Q

What type of luekocytes produce antibodies?

A

antibodies are produced by B lymphocytes

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3
Q

Antibodies constitute the class of proteins known as ……………….

A

immunoglobulins

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4
Q

What are the secondary effector functions after an antibody has binded onto a antigen?

A

complement activation

opsonisation (promotion of phagocytosis)

cell activation via specific antibody-binding receptors (Fc receptors)

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5
Q

Identify the antigen binding site (Fab) and Fc portions of the molecule?

A

add pic

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6
Q

Are antibody molecules flexiable

A

yes

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7
Q

Both light chains and heavy chains can be divided into ………… regions and ………….. regions Hint: it has to do with the flexability of antibodies

A

variable and constant add pic

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8
Q

How many hypervariable regions make up the antigen binding site?

A

3

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9
Q

What region that is made up of 3 hypervariable regions within V domains forms the antigen binding site?

A

complementary determining region (CDRs)

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10
Q

Define Antibody Affinity?

A

Is a measure of the strength of binding between a single binding site of an antibody and its antigen

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11
Q

Define Antibody Avidity?

A

Defined as the overall strength of multiple interactions between an antibody with multiple binding sites and a complex antigen with multiple epitopes: add pic

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12
Q

define epitopes

A

the part of an antigen molecule to which an antibody attaches itself.

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13
Q

Briefly explain Antibody Cross-Reactivity?

A

Antibody elicited in response to one antigen can sometimes recognise a different antigen of similar structure: 1. Vaccination with cowpox induces antibodies which are able to recognise smallpox 2. ABO blood-group antigens (glycoproteins on r.b.c.) Antibodies made against microbial antigens on common intestinal bacteria may cross-react with carbohydrates on r.b.c.

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14
Q

What part of the antibody differs between different antibody classes?

A

Different classes of antibodies differ in the constant regions of their heavy chains: add image

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15
Q

List the immunoglobulin classes

A

IgG IgA IgM IgE IgD GAMED

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16
Q

What is the function of IgG?

A

Ig nuetralises toxins and viruses Major activator of classical complement pathway (mainly IgG1 and IgG3)

17
Q

How does IgG structure help with its function?

A

When IgG binds to a bacterium or other infectious agent, macrophages or nuetrophils recognise their Fc (they posses Fc receptors) and this leads to phagocytosis (opsonisation)

18
Q

Name the 4 sub classes of IgG?

A

IgG1 IgG2 IgG3 IgG4 I

Actively transported across the placenta

19
Q

Name the function of IgA?

A

Protects mucosal surfaces from bacteria, viruses and protozoa

Nuetralise toxins- by binding ontp infectious agents it can block their infectivity- often by preventing adherence of the agents to the epithelial cells

20
Q

Where does IgA occur as a mononmer and where does it occur as a dimer

A

Occurs as a monomer (blood) and as a dimer (secretions)

21
Q

Where does the SC (secretory component) get added to the IgA and what role does it play?

A

add Pic of IgA The SC is added to the IgA when it passes through the epithelial cells it helps protect IgA from degradative enzymes

22
Q

How does IgM structure helps with its function?

A

Its 5 Fab pairs allow it to bind strongly to the surface of bacteria causing agglutination

23
Q

What is the function of IgD?

A

involved in B cell development and activation

24
Q

What is IgE function and how does its structure help it carry out it function?

A

Mast cells and basophils have a high affinity for the Fc of IgE When IgE that is bound in this way is cross-linked by antigen, degranulation of the cells occurs with release of inflammatory mediators such as histamine. This can give rise to allergic reactions.

25
Q

Lable the diagram below

A