Antibody Structure and Function Flashcards

1
Q

what are antibodies

A

specifically induced serum glycoproteins which recognize antigens

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2
Q

where are antibody molecules found

A
  • circulate in the blood
  • present in body secretions
  • found on the surface of B cells (act as antigen-spec receptors)
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3
Q

how can antibodies inactivate pathogens

A

-directly inactivate pathogens following interaction w/ relevant antigenic determinants that they express

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4
Q

what can antibodies stimulate

A

non-specific host effector mechanisms such as complement proteisn and cytotoxic cells
-can also act as opsonins

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5
Q

which end of antibodies recognize antigenic determinants (epitopes) on the antigen

A

amino terminal end of the molec contains the antigen binding site which recognizes epitopes

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6
Q

which end of ab binds various effector cells and molecules

A

carboxy terminal portion

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7
Q

what were the major bands that were revealed when serum proteins were separated into fractions

A

albumin
alpha
beta
gamma globulins

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8
Q

which fraction is the only one capable of passively transferring humoral immunity from an immunized donor to a naive recipient

A

gamma globulin fraction

known as passive immunization or vaccination

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9
Q

how are gamma globulin and albumin different

A

gamma is not a homogenous protein, it consists of many diff molec having the same basic structural features but diff aa sequences

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10
Q

what is the molecular weight of a typical gamma globulin

A

150,000 daltons

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11
Q

what make up the basic immunologic structure

A

2 identical heavy chains of 50,000

2 light chains of 25,000 daltons

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12
Q

what is papain

A

an enzyme that produces fragments of approx equal molec weight but of diff molec composition when digested with immunoglobulin

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13
Q

what are fab fragments

A

fragments that retain their ability to bind antigen after being liberated by papain digestion
“fragments w/ antigen binding activity)

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14
Q

what is an fc fragment

A

crystallizable fragment

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15
Q

what is pepsin

A

an enzyme when digusted liberates a single fragment of approx 100,000 daltons which exhibi antigen binding capability

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16
Q

why is f(ab)2 referred to as being bivalent

A

it can bind antigen at 2 sites

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17
Q

what is f(ab)2 held together by

A

disulfide bond

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18
Q

what do multiple myeloma tumor cells produce

A

a single homogeneous innunoglobulin w/ one aa sequence (confirming clonal selection theory)

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19
Q

patients with multiple myeloma secrete what

A

prodigious amounts homogeneous antibody, which facilitate the sequencing of the molec

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20
Q

what are immunogloblulin molec held together by

A

interchain disulfide bonds within each of the protein chains
non-covalent, ionic, and hydrophobic bonds

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21
Q

what are the 2 classes of light chaisn in humans

A

kappa and lambda

-each antibody molec has either kappa or lambda chains, not both

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22
Q

how many classes of heavy chains are there in humans

A

10

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23
Q

what part of the light and heavy chain is responsible for antigen recognition (fab portion)

A

amino terminal half of the light chain

amino terminal quarter of the heavy chain

24
Q

where are the variable (V) regions located at

A

the end of the chain

-in the amino terminal

25
where are the C regions located at
close to the hinge
26
what are the hypervariable regions
-highly divergent stretched w/in the V regions
27
what form the antigen-binding cleft
hypervariable regions of apposed heavy and light chains of each Fab fragment
28
where is the hinged region, what does it do
in the heavy chains affects the flexibility of movement of Fab portions -in some it can allow both fab portions to bind antigen, rather than just 1, which increases the strength of ab attachment
29
where are the constant regions of immunoglobulin on the heavy and light chains
3/4 of the heavy chains from the carboxy end and similar half of the light chains
30
where are complx carbs located on the chains
heavy chains in the Fc region
31
what involves the rearrangement of the germinline DNA endocding the heavy chain
first steps in B cell development
32
what are the major classes of antibody isotypes
igG, A, M, E, D "Gamed"
33
which isotypes can be subdivded into closely related subclasses "subtypes"
igA and igG
34
what creates the different isotpes
sequence of aa in the heavy chain make the difference
35
which is the first isotype that is released by plasma cells
igM
36
which is the most effective complement-activating antibody isotype, why
igM | =secreted form found in serum is a pentamer (consits of 5 igM monomers => 10 antigen binding sites
37
which isotypes are found on virgin B cells (havent seen antigen yet)
igM and igD
38
how do you form secreted igM
monomers are polymerized in the cell by a process requiring the production of a separate protein called the J chain, which links and stabilizes them
39
which is the first immunoglobulin produced during the immune response
igM
40
what is the primary functino of igD
rare found in serum | to act as a second antigen receptor
41
what is the major immunoglobulin class found in serum
igG
42
what is the role of igG
activates complement | act as B cell surface antigen-receptors on memory B cells (cells that are produced after initial antigen stimulation)
43
where is igA found
relatively low concentrations in the serum but is abundant in body fluids like intestinal and mucous secretions, saliva, tears, and colostrum
44
what ist he only isotype that can be transported across epithelial cell boundaries
igA
45
which isotype is critical for host defense againt organisms that cn invade the body
igA
46
which isotype binds to polymeric immunoglobulin receptors on the basolateral membranes of lacrimal acinar cells
igA
47
what does the secretory componene tsreve as
to protect igA from degradation by microbial proteases produced ex ocular surface bacteria
48
what is immune repertoire
the established pool of immunoglobulin V regions that is present in an indiv
49
what are the 3 mech by which the immune system generates an enormous variety of diff V regions on immuno heavy and light chains
1. multiple genes: large # of separte genes which encodes one V region domain 2. somatic (genetic) mutation: V region mutates during B cell devleopment to produce diff genes in diff B cell clones 3. somatic recombination: # of gene segments recombine to join the main part of the V regino gene. results in protein containing elements coded for by diff gene segments
50
what are the antimicrobial functions of secretory igA
1. agglutination (clumps) 2. preventino of microbial attachment 3. inactivation of bacterial enzymes and toxins 4. antibody-dependent cell mediated cytotoxicity 5. opsinization (igA acts as opsonin)
51
which isotype are good at complement activation | which is not
igG and igM | igA is not good
52
how can antigens enter the body
- from the gut through M cells (delivers antigen directly to underlying immune cells) - through more common enterocytes (ep cells taht line the gut)
53
who described monoclonal ab
georges kohler | cesar milstein
54
what are hybridomas
immortilized cells produced with monoclonal antibodies of pre-determined specificity
55
what are the applications of monoclonal antibody tech
1. identificatino of phenotypic markers of cell types 2. purified isolation of cell types with unique markers 3. purification of antigens 4. immunodiagnosis 5. functional analysis of cell-surface and secreted molec 6. immunotherapy and immunosuppresion