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Immunology > 2nd test > Flashcards

2nd test Flashcards

1
Q

What must the shapes of the HVR be

A

complementary to the antigen

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2
Q

Why must the HVR be complementary

A

in order for bonds to form between

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3
Q

What types of bonds form between

A

ionic bonds, hydrogen bonds, hydrophobic bonds

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4
Q

What kinds of bonds are the bonds that form

A

non covalent

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5
Q

Since the bonds are non covalent what can occur

A

they can be reversible

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6
Q

How does a better fitting antibody to antigen affect reversibility

A

more bonds form with a stronger attraction between the antibody and antigen resulting in the bonds being harder to break and slowly reversible

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7
Q

How does a poorer fitting shape affect reversibility

A

poorer shape forms fewer bonds that cause a weak attractiion making them quickly reversible

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8
Q

What three things is the antibody antigen binding region

A

relatively specific
more or less tight
variable reversible

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9
Q

What 5 things is antigen antibody binding useful

A 
disease recovery
disease prevention
disease diagnosis
disease treatment
research
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10
Q

How does the antigen antibody help disease diagnosis

A

detect a specific antigen through using specific “store bought” antibodies or the presence of antibody implies the presence of the complementary antigen

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11
Q

How does the antigen antibody region help research

A

identifies a specific protein in a complex mixture

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12
Q

What is agglutination

A

the clumping of antigen containing particles by antibodies

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13
Q

How does agglutination help

A

for diagnostics—agglutination can indicate a positive

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14
Q

What is direct agglutination for

A

to find out if a specific bacterial antigen is present

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15
Q

What is the method for direct agglutination

A

(in a tube) mix stock cells with known antigens on their surfaces and presumed or unknown source of Ab (patient serum)

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16
Q

What is the interpretation of direct agglutination for when Abs are present

A

the antibodies and antigens cross link the cells and neutralize the natural negative charge on their surfaces, clumping or agglutinating them into visible clumps that precipitate to the bottom of the tube

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17
Q

If agglutination occurs what conclusions can be drawn

A

antibodies are present,

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18
Q

If no antibodies are present what will occur

A

the cells will not agglutinate and will repel each other

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19
Q

What conclusions can be drawn if agglutination does not occur

A

patient has bot been exposed to that antigen

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20
Q

What is a quantitation of antibodies

A

titer

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21
Q

What is a titer

A

mix a constant number of bacteria in a series of tubes and different dilutions of antibody and serum

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22
Q

What occurs in a titer

A

at some point and dilution there is not enough antibodies to cause agglutination of the cells

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23
Q

What does the highest dilution that causes agglutination indicate

A

the titer of that serum for the antigen on those cells

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24
Q

What does a high titer indicate

A

high concentration of antibodies in the original sample of serum

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25
Q

Titer is what

A

relative, not absolute, concentration

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26
Q

What is passive agglutination for

A

antigens not found on the surface of cells (viral antigens)

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27
Q

Where are antigens that are not on the surface of cells

A

can be chemically attached to RBCs or microscopic inert particles

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28
Q

What is the method for passive agglutination

A

mix antigen coated particles and presumed source of Ab

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29
Q

What conclusions can be drawn from passive agglutination

A

particles will agglutinate if Abs to that Ag are present

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30
Q

What is agglutination inhibition for

A

soluble antigens (hormone hCG)

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31
Q

What does hCG indicate

A

pregnancy

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32
Q

What is the method for agglutination inhibition

A

purchase latex particles with hCG chemically bound to their surface, add stock hCG to be able to agglutinate the latex, add urine

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33
Q

What are the results of agglutination inhibition

A

if hCG is present it inhibits agglutination by preoccupying the hCG antibodies

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34
Q

What does agglutination imply

A

no hCG in the urine

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35
Q

What is RIA

A

radio immuno assay

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36
Q

What is radio immuno assay

A

a test for the presence of small soluble antigen molecules in a patient sample

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37
Q

What is the method for radio immuno assay

A

mix a known solution of antibody+ presumed source of the antigen and a known solution of a small amount of radioactive labeled antigen

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38
Q

Where does the known solution of antibody come from for the RIA

A

made by immunizing an animal with a hapten carrier conjugate

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39
Q

Where does the antigen come from for the RIA

A

the patient serum

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40
Q

What is the principle for RIA

A

labeled antigen and unlabled antigen compete for binding to the Ab in forming immune complexes of Ag+Ab

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41
Q

What occurs after immune complexes form

A

they are separated from uncomplexed and unbound antigens, antibodies, Ag* by precipitating all large proteins (antibodies) not small antigens

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42
Q

What is the last principle step of RIA

A

the amount of radioactivity in the supernatant is measured

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43
Q

What is the interpretation of RIA

A

if lots of unlabeled Ag was present in the patient serum it will out compete Ag* for binding to the Ab and radioactivity will be found in the supernatant

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44
Q

What is the conclusion drawn if lots of radioactivity is found in the supernatant

A

lots of unlabeled Ag is present in the patients serum

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45
Q

If there was no Ag in the patient serum what will occur

A

nothing will stop the Ag* from binding and no radioactivity will be found in the supernatant

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46
Q

If there was some Ag in the serum what will occur

A

the amount of Ag* in the supernatant will be quantitatively proportional to the amount of unlabeled Ag in the patient serum

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47
Q

What are FAT tests

A

Fluorescent antibody tests

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48
Q

What are fluorescent antibody tests

A

an antibody covalently attached to a small fluorescent molecule is used to detect and locate an antigen on cells or tissues on a microscope slide

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49
Q

What does the FAT test indicate

A

presence or absence of antigen, relative amount of antigen and the distibution and location of antigen in cells or organ

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50
Q

What is the direct FAT for antigen

A

the presumed unknown source of antigen is placed on a slide, stock labeled Ab is allowed to bind to its antigen, unbound Ab is washed away

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51
Q

What is a slide viewed in for FAT test

A

fluorescence microscope

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52
Q

If Ag is present what will occur in the FAT test

A

presence and location of fluorescence will occur

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53
Q

How is an indirect FAT for antigen performed

A

presumed source of Ag from patient is placed on slide, stock labeled Ab is allowed to bind to the antigen, unbound Ab is washed away, labeled fluorescent antigolubul will attach to the Ab if its Ag is present

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54
Q

What is an antiglobulin

A

antibody for the antibody

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55
Q

What is the result of the indirect FAT test

A

fluorescence means antigen is present

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56
Q

What is an indirect FAT for antibody test for

A

if presence of antibody is the unknown

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57
Q

How is an indirect FAT for antibody performed

A

known source of stock antigen is placed on slide, presumed source of Ab (patient) is added, unbound Ab is washed away, fluorescent antiglobulin is added to located the Ab

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58
Q

What is the result of indirect FAT test for antibody

A

if no fluorescence is on slide then no antibody is in the unknown

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59
Q

What should be included in all serological tests

A

positive and negative controls along with the test of the presumed molecule

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60
Q

Why are positive and negative controls needed

A

to rule out false negative and false positive results

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61
Q

How many slides does an indirect FAT for Ab require

A

3

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62
Q

What are the 3 slides for indirect FAT for Ab

A

Ag+Ab+AG= positive control
Ag ?Ab +AG= unknown
Ag –Ab +AG*= negative control

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63
Q

If Ag ? Ab +AG* was positive, what would be assumed

A

it was because Ab present

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64
Q

What could have resulted in the previous test that may have made it positive

A

AG may have bound directly to some antigen in the cell or tissue

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65
Q

What would the AG binding produce

A

false positive bc Ab is not present in the unknown

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66
Q

If Ag ?Ab +AG* was negative, what would be assumed

A

Ab was absent from the unknown solution

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67
Q

What could have resulted in the previous test that may have made it negative

A

Antigens being denatured, AG was not at an adequate concentration, the AG was not active

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68
Q

What is ELISA

A

enzyme linked immuno sorbent assay

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69
Q

What is an enzyme linked immuno sorbent assay

A

atibody or AG is labeled with an enzyme whose reaction is detectable

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70
Q

Why are ELISAs useful

A

for Ags or Abs which are not naturally found on cell surfaces but can be adsorbed onto the bottome of pastic wells in dishes or tubes

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71
Q

What is the method for ELISA

A

Ag is adsorbed non covalently onto well bottoms, the resumed source of Ab is added and allowed to bind, unbound Ab is washed away, AG-E is added and allowed to bind, unbound AG-E is washed away, the enzymes substrate is added

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72
Q

What is the interpretation of ELISA

A

if Ag, Ab, and AG-E are present and active, the enzyme will convert the colorless substrate into a colored product

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73
Q

What is the intensity of the color amount to

A

proportional to the amount of antigen antibody antiglobulin enzyme and time

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74
Q

What is the application of ELISA

A

screen patients and donated blood for the presence of Abs to HIV

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75
Q

Is HIV easy or hard to detect and why

A

hard, and HIV in the blood is not an entirely reliable indicator of HIV infection since it may be hiding elsewhere

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76
Q

What of HIV is adsorbed

A

HIV proteins-prospective antigens unavoidably contaminated by proteins from the cultured cells in which HIV was replicated

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77
Q

What is the presumptive source of antibodies for ELISA

A

patient serum

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78
Q

What could a positive ELISA mean

A

patient was exposed to HIV (true positive)
patient has antibodies to something else that cross reacted with an HIV epitope (false positive)
patient has antibodies to a contaminant in the HIV antigen preparation (false positive)

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79
Q

How is a false negative result possible for ELISA

A

patient has antibodies to a new strain of HIV which do not cross react with the test strain

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80
Q

What can ELISA not tell you

A

which Ags are being detected or exactly how many

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81
Q

What can the Western blot tell you

A

which antigens and how many are being detected

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82
Q

What is the method of the Western blot

A

antigens in a mixture are separated by size through electrophoresis, the patterns of bands are transfered to or “blotted” onto nitrocellulose or nylon paper, the whole piece of paper is exposed to the presumed source of HIV antibodies, labeled AG* is added to locate where Abs have bound

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83
Q

What does each Ab bind to

A

only its Ag band

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84
Q

What occurs when an AG* binds to where Abs have bound

A

an enzyme label produces a colored product on the otherwise invisible protein band, radioactive label exposes

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85
Q

What is the interpretation of the Western blot

A

Abs to several known HIV proteins is strong evidence for HIV exposure

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86
Q

What does a single Ab band indicate

A

cross reactivity by an Ab produced against another Ag

87
Q

Abs to non HIV proteins are

A

easy to see and indicate HIV non exposure

88
Q

What are Western blots used for

A

to check ELISA positive results and rule out false negatives

89
Q

Most ELISA positive results are

A

negative when checked by western blot

90
Q

What could produce a weak positive result for ELISA

A

low titer of HIV antibody

91
Q

What is the basic mechanism for antibody diversity

A

combination

92
Q

What is the variable region of heavy or light chain constructed from

A

a few separate segments

93
Q

For each variable region segment there are many what

A

genes on a chromosome

94
Q

What do the genes on a chromosome ultimately provide

A

one supplies the information for that segment in a particular B cell

95
Q

How can many possible antibody V regions be made

A

through combinations of variable regions in both light and heavy chains

96
Q

How is combining gene segments possible

A

chromsome is not bumper to bumper genes

97
Q

What allows the chromosome to not be bumper to bumper

A

non coding spacers between genes

non coding introns within genes

98
Q

What do non coding regions provide

A

ideal locations for splicing genes or gene segments together

99
Q

How are immunoglobulins organized

A

into families

100
Q

How many sets of gene segments for Ig molecules

A

3

101
Q

How are the members of families aligned on a chromosome

A

adjacent to each other with spacers and introns between the members of each family

102
Q

Where are all the gene segments for all heavy chains

A

on chromosome #14

103
Q

Where are all the gene segments for kappa light chains

A

on chromosome #2

104
Q

Where are all the gene segments for lambda L chains

A

on chromosome #22

105
Q

How many chromosomes involve light chains

A

4 (maternal and paternal)

106
Q

What is it called when only one of the chromosomes is expressed in an individual B cell

A

allelic exclusion

107
Q

How many chromosomes involve heavy chains

A

2

108
Q

How many chromosomes are used for heavy chains

A

1 for each B cell

109
Q

How are the families separated

A

on different chromosomes

110
Q

How do light chains and heavy chains come together

A

light and heavy chain genes are transcribed separately and translated separately and then are later bonded together to form complete Ig molecules

111
Q

Where are light and heavy chains translated

A

on ribosomes attached to the ER

112
Q

Where do light and heavy chains bind together

A

inside the ER

113
Q

Once molecules are bonded to form Ig what happens

A

they are packaged into transport vesicles and secreted from the cell or retained in the plasma membrane as mIg

114
Q

How are light chain genes organized

A

in order with introns or spacers between them on chromosome #2 and #22

115
Q

What is TIP

A

translocation initiation peptide

116
Q

What is function of TIP

A

to ensure attachment of the ribosome to the ER and eventual Ig secretion or insertion

117
Q

How many different gene segments for most of the variable region

A

80

118
Q

What is the variable region combined by

A

one of the J gene segments

119
Q

how many different J gene segments

A

5

120
Q

What is the V and J regions combined with

A

C constant region

121
Q

How many constant regions are there

A

1

122
Q

How is splicing accomplished

A

the selected J and V regions come together forming a loop of the unnecessary DNA in which the loop is cut and ligate occurs to bond the J and V region together along with the C

123
Q

Where is splicing done

A

in the primary lymphoid organ (bone marrow)

124
Q

Why is splicing done in the primary lymphoid organ

A

absence of antigen so it is not a response to antigen that causes the formation of antibodies

125
Q

When does most splicing occur in ones life

A

before birth

126
Q

WHy is splicing done before birth

A

so you are not vulnerable completely at birth

127
Q

How does splicing occur

A

randomly by recombinase enzymes

128
Q

Where is the actual splice made along the DNA

A

somewhere in the introns

129
Q

What happens to the rest of the DNA when the loop is cut

A

it is lost forever from the cell

130
Q

What is the result of cutting the DNA

A

the cell cannot change the antibody it makes and can only recognize one epitope

131
Q

When in the duplication process of DNA does splicing occur

A

before transcription

132
Q

When is the splicing of the leader to its V gene segment and of the V-J combination to the C region gene done

A

after transcription during the process of the primary transcript into mRNA

133
Q

What stage of the IS cell does this occur

A

during the maturation to the antigen sensitive lymphocyte stage

134
Q

What 3 ways does light chain diversity occur

A

which V gene segment is combined
which J gene segment is combined
variation in the exact splice point between V and J

135
Q

What can cause variation in the exact splice point between V and J

A

how much intron is removed
how many filler nucleotides are added
what amino acids those nucleotides code for

136
Q

Where is the splice point on the finished light chain

A

the HVR3 near the C region

137
Q

What occurs when rearrangements are non productive

A

they produce internal stop codons and truncate L or H chains

138
Q

What does the cell do if an internal stop codon is produced

A

to try another allele or die

139
Q

What is the order of the variation process

A

splice first then exclude alleles

140
Q

What is RNA editing

A

deamination of certain bases creates different bases amino acids, shapes, contacts

141
Q

How is heavy chain diversity created

A

similarly to the light chain

142
Q

Where is heavy chain diversity done

A

on one of the two chromosomes #14

143
Q

How many V regions are there

A

300

144
Q

How many D regions are there

A

5

145
Q

How many J regions are there

A

9

146
Q

Where does impricise splicing occur

A

between V and D introns and between D and J

147
Q

What does the imprecise splicing between D and J create

A

HVR3 on the H chain

148
Q

some splices create internal stop codons which creates what

A

a non productive rearrangement

149
Q

What must occur for the non productive rearrangment

A

forced to try another allele or kill itself

150
Q

How can L and H chain mRNAs be edited

A

deamination of certain bases altering the corresponding amino acids and shape of the V region

151
Q

What is affinity selection

A

even more variability is introduced by point mutations occurring at an accelerated rate within the other two HVRs in both L and H chains

152
Q

after B cell selection what occurs

A

it begins proliferation cloned all cells of the heavy chain combination

153
Q

What may occur during each round of DNA synthesis during proliferation

A

DNA plymerase introduces some errors into the DNA copy in the specific areas corresponding to HVR1 and HVR2

154
Q

How is a B cell selected

A

the one with the best available fir with the epitope on the antigen

155
Q

by introducing mutations in the HVR1 and HVR2 regions

A

some produce a better fit while some have a not so good fit

156
Q

What institutes a better fit

A

one with more bonds between the antibody and the epitope

157
Q

One with more bonds is said to have a

A

higher affinity and attraction

158
Q

Those that have poorer fits are subject to

A

suicide

159
Q

What is the process of selecting a B cell for fit

A

affinity selection or somatic hypermutation

160
Q

When does the fine tuning of the shape of the antibody to match the antigen occur

A

following infection or vaccination

161
Q

How can diversity in the H chain constant region occur

A

heavy chain constant region is splice together combination of gene segments

162
Q

What is the constant region segments made up of

A

one exon which is a particular domain of 110 amino acids

163
Q

after transcription pre mRNA processing splices what

A

L onto VDJ, C regions together and the parts are combined to form a mature mRNA

164
Q

What is the mature mRNA translated into

A

a single contiguous amino acid chain

165
Q

What is the purpose for the apparently wasteful RNA splicing

A

allows the cell to splice its VDJ combination onto any C region and to switch classes

166
Q

How can VDJ be spliced onto any C region

A

because we have not spliced DNA for constant regions, we are splicing RNA

167
Q

What is the final element of diversity

A

a certain H chain protein is paired with a L chain

168
Q

When is an immune system response evoked

A

when the antibody binds to the antigen

169
Q

What different IS effectors are evoked

A

phagocytosis, ADCC by NK cells, initiation of C’ cascade

170
Q

Why doesn’t a free Ab induce these responses

A

the free Ab has the Fc regions covered by the Fab regions

171
Q

What happens when an Ab and Ag bind to each other

A

the Ab changes shape at its hinge region exposing the Fc region that then can bind

172
Q

How must the proteins react in the complementary cascade

A

in a specific order

173
Q

What are the proteins involved in the C’ pathway

A

proteases, helpers, form membrane attack complex, regulatory proteins

174
Q

What is the function of the proteases

A

can act on several of the next members is a series, cutting, activating it, enabling it to act on the next one

175
Q

What happens when the proteases continue the pathway

A

it amplifies the response forming a cascade

176
Q

What do the helper proteins do

A

hold proteins in a position so the protease can attack them

177
Q

What is MAC

A

membrane attack complex

178
Q

What is the function of the membrane attack complex

A

attaches to the nearest membrane and forms a hole in it to lyse the cell

179
Q

What do regulatory proteins do

A

govern, control each protein in the series, aborting, or shutting off the chain reaction

180
Q

What are the two different sets of proteins that can form in the first half of the cascade

A

classical C’ pathway

alternative C’ pathway

181
Q

What is the classical C’ pathway

A

antibody dependent

182
Q

What is the alternative C’ pathway

A

antibody independent

183
Q

What do the two different sets converge into

A

a common MAC

184
Q

What is the purpose of the alternative C’ pathway

A

no antibodies are required and it is faster

185
Q

Why is the alternative pathway faster

A

because no B cells need to be selected, proliferate and synthesize antibodies

186
Q

Where are C’ proteins synthesized

A

by the liver

187
Q

When are C’ proteins synthesized

A

continually so always available

188
Q

What does the alternative pathway provide

A

immediate, innate defense while the IR is getting ready

189
Q

What are the cons to the alternative pathway

A

less specific meaning lower affinity which is less effective

has no memory

190
Q

How are some C3b formed

A

slow, spontaneous breakdown of C3 into C3b and C3a

191
Q

What initiates the second half of the pathway

A

C3b

192
Q

What binds to C3b

A

C5b, C6, C7

193
Q

What does C5b, C6, C7 bind to

A

the nearest cell membrane

194
Q

If no cell membrane is present what happens

A

they aggregate to become inactive

195
Q

What does C5b, C6, C7 attract

A

C8 and up to 18 C9 proteins

196
Q

What do the C8 and C9 proteins assemble themselves into

A

a tube in the PM

197
Q

What does the tube do

A

leads to osmotic lysis of the cell

198
Q

What does this tube make up

A

MAC

199
Q

Why is regulation of the complementary pathway critical

A

can lead to C’ diseases

200
Q

What are three ways C’ is regulated

A

C’ proteins present in limited amounts preventing an over reaction
C’ proteins have very short half lives that naturally break apart within a few minutes
C’ proteins are inhibited by special regulatory proteins that regulate concentration of C3b

201
Q

What is the final effect of C’ activation

A

lysis

202
Q

What does C3b also activate

A

opsonizes foreign cells for phagocytic cells

203
Q

C3a and C5a are what

A

chemotactic

204
Q

What do C3a and C5a attract

A

neutrophils and monocytes/macrophages

205
Q

What do C3a and C5a contribute to

A

inflammation by causing mast cells and plateltes to release histamine

206
Q

C3a and C5a are what

A

vasoactive

207
Q

How are immune complexes removed

A

from the bloodstream by attaching C3b and its receptors on RBCs which are removed by liver and spleen

208
Q

Where are most imune complexes

A

in ISS not in bloodstream

209
Q

Deficiency of any C’ protein can lead to

A

increased susceptibility to infection as no alternative pathway and no MACs

210
Q

Inadequate C3b production can lead to

A

non removal of immune complexes

211
Q

Non removal of immune complexes results in

A

deposition in joint and blood filtering organs

212
Q

What can deficiency of C’ regulatory proteins lead to

A

uncontrolled activation of C’

213
Q

What does uncontrolled activation of C’ lead to

A

constant lysis of nearby RBCs and anemia

Immunology (4 decks)

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