Anti Bodies Flashcards

1
Q

General structure of antibodies what stabilises it

A

Quaternary structure, 2 light chains and two heavy chains stabilised by disulphides bridges bridges between shapes forming the characteristic Y shape

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2
Q

Two main regions of antibodies, which one is used for antigenic recognition of pathogens

A

We have a constant fraction, where sequence is identical for each antibody of a specific isotope (A,G,E,M…) and variable fraction, which is responsible for specificity towards specific antigen of specific pathogen

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3
Q

What the constant region used for? And the variable region?

A

Variable region is responsible for the antibodies specificity constant region is important for effector functions, and joining with surface cell receptors

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4
Q

what is the Fc region of the antibody

A

The Fc region is the crystalize able fraction of the antibody, also known as the constant fraction. Only varies between different isotypes and its used for interactions with surface receptors and determining effector functions

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5
Q

What is the Fab region

A

The antigen binding fraction which also contains the variable regions that give antibodies their unique specificity

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6
Q

Name the two regions that make up an antibody

A

Constant regions and variable region

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7
Q

Who determines the specificity of an antibody

A

The variable regions, or the Fabs of the antibodies containing the CDR loops (3 on heavy and and 3 on light). Thanks to somatic recombination

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8
Q

Name two proteolytic enzymes used in antibody modification

A

Papain and pepsin, Used to generate fragments with a modified function (from antibodies)

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9
Q

What does PaPain cause

A

proteolytic Cleavage of antibodies removing Fab regions, generating 2 Fab fragments and 1 Fc fragment

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10
Q

Pepsins mechanism of action

A

Proteolytic cleavage of generating a fragment composed of only two Fab regions, this cleavage also breaks down the Fc portion of the antibody into peptides, generating peptides and and F(ab)2 fragment

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11
Q

Nomenclature of fragment generated by Pepsin

A

F’(ab)2

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12
Q

Is the hypervariable region on what terminal of polypeptide

A

N terminal of polypep chain

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13
Q

what are antibodies classified by

A

Classified by constant fractions of both light and heavy chains. Heavy chain FC–IgM, A, E, D, G, and light chain FC- Kappa and landa where landa is more common due to isotypic exclusion

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14
Q

what antibodies team up forming dimers or pentamers how do the join to each other, and which ones have an extra constant region

A

IgA’s forming dimers and IgM’s forming pentamers ( big and slow one of reasons IgM is not a gent opsonizer) IgM and IgE have extra CH region

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15
Q

Isotypes of light chain constant regions, are they both produced in a particular b cell?

A

Kappa and landa, NO thanks to isotypic exclusion (allelic exclusion) in a particular b cell only one isotype is being produced.

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16
Q

What are the effector functions for antibodies

A

Neutralization (with agglutination), complement activation, Opsonization, ADCC

17
Q

what antibody has 4 subclasses

A

IgG, subclasses 1,2,3,4

18
Q

main antibody in acute immune response

A

IgM

19
Q

most abundant serum isotype

A

IgG 70-89% and M is 5-10%

20
Q

Epitope

A

Region of antigen that binds to paratope on antigen, also called the antigenic determinant, Two type linear and conformational determinants. Tip; there can be different epitopes on one antigen—relate to monoclonal antibody screening process

21
Q

antigenicity

A

the ability of an antigen to bind to a specific antibody or t cell receptor,

22
Q

immunogenicity

A

The ability of an antigen to generate and immune response, specifically through the activation of lymphatic cells, antigens that can do this are also called IMMUNOGENS

23
Q

Haptens

A

antigen that are not immunogenic on their own, need to associate with molecules called “carriers” in order to create an immunogenic response

24
Q

Paratope

A

Region on Fab the binds to epitope of antigen

25
Q

IgD, how common is it in serum

A

Not common, mainly found bound to b cells as BCR’s

26
Q

what are IgEs mainly involved in

A

IgE are mainly involve in the allergic response and helminth immune responses

27
Q

What are IgM’s functions

A

IgM’s are the main antibodies in an accute immune response, mainly for pentamers joined by J chains

28
Q

Types of epitopes or determinants

A

Linear determinants and conformational determinants

29
Q

what’s responsible for the high variability of the antigen binding regions, when does it occur

A

somatic recombination occurs during maturation of b cells, we see recombination’s between D J sequences and D V sequences on heavy chains and DV sequences on Light chains, combines generate billions of possible antigens for any pathogenic antigen the body can encounter

30
Q

what’s the difference between Light chain and heavy chain somatic recombination

A

The variability, heavy chains have up to 9,000 possible recombination’s while the kappa and alpha have 200 and 270 respectively. A lot more variability can be achieved on the heavy chain thanks to the fact that they have the joining regions which are also involved in the recombination

31
Q

What are CDR`s…What do they determine

A

The determine the antigen specificity of an an antibody (the paratope of the antibody) also known as complementary determining regions.

32
Q

Structure of CDR`s , where on the antibody are they

A

On Fab, forming part of variable regions, The form loops at the tips, 3 from light chains and 3 from heavy chains

33
Q

Immunogen

A

An antigen that is immunogenic, no all antigens are immunogenic

34
Q

What types of molecules are the best immunogens

A

carbohydrates and glycoproteins ( peptides most, those are the one incorporated in HlA)

35
Q

Antibody maturation

A

Occurs in already differentiated b cells and we see somatic hypermutation in which we see improvements to paratope specificity and overall function, and isotype recombination in which IgM’s are converted to IgG,A,or E