Chapter 4 Flashcards
antibodies are also called
immunoglobulins
antibodies are made by
plasma cells
what plasma makes antibodies
plasma of blood, lymph, and mucosal surfaces
most common antigens that it recognizes is
proteins and carbohydrates
vaccine protection relies on
Ab
how does vaccine protection relie on Ab through what
phagocytosis and neutralization
1 antigen or small number of structurally similar antigens is called
Ab specficity
what binds 2 places on one microbe or 1 place on each of 2 microbes
Ab specificity
what is all the individual things Ab recognize called
Ab repertoire
all specificities of Ab about 10 to the 9th
Ab repertoire
what is clonal expansioin
massive proliferation of a B cell with infection relevant specificity
3 steps of clonal expansion
- resting B cell
(small number of B cell w/ specificity) - encounter with antigen
( recognize infection) - stimulated B cell gives rise to antibody-secreting plasma cell
(B cell proliferate and diff into plasma cell)
best/ most abundant/ most versatile antibody isotype
IgG
what antobody isotypes act as B cell receptors
IgM and IgD
what antibody isotype helps with parasitic infection and allergies
IgE
a lot of antigen binding is mediated by interaction with what?
the host cell
hinge region has what type of bonds
disulfide bonds
what region actually binds antigen
variable region
Fab region consists of
heavy and light chains and does the binding
the constant region of the antibody structure interacts with
host cells
the base of the antibody structure consists of heavy or light
heavy chain
the hinge region provides
flexibility
each Ab has how many arms
2
do each arm recognize the same thing on an Ab
yes
the hinge region allows flexibility of where the antibody can bind the the distance between
Ag
Ig means
immunoglobulin
the antigen binding sites are what so that we can bind all the things
hypervariable
hypervariable region has what kind of loops
CDR
Loops bind to what
Ag
how many loops in each heavy and light chain
3
what is something antibodies can bind
antigen
what are epitopes
amino acids that the antibody binds
can an antigen have more than one epitopes
yes
can one antibody type bind multiple of the same epitopes
yes
antigen and antibody match
shapes for binding
bind to amino acid next to each other is called
linear epitope
what is a more common type of antigen binding and the amino acids are not next to each other in sequence but are in a folded protein
discontinuous epitope
what type of antibody does not exist in the wild
monoclonal
how are antibodies normally found
in polyclonal form
all ab are identical and all bind one thing
monoclonal
bunch of different antibodies with different specifities
polyclonal
antiserum- inoculate animal- isolate serum (pool of antibodies to a specific Ag) is what type of antibody
polyclonal
pool of antibodies that are all specific to an epitope of an Ag
monoclonal antibody
what is great for therapies
monoclonal
mouse is
full mouse
chimeric
human constant region
humanized
mostly human some mouse in variable region
fully human
fully human
monoclonal antibody treatments were all made in what
mice
how would monoclonal antibody treatments be recognized in our bodies
as foreign
lambda light chain locus is on what chromosome
chromosome 22
kappa light chain locus is on what chromosome
chromosome 2
heavy chain locus is on what chromosome
chromosome 14
variable region is composed of how many segments
3
is diversity in heavy or light chains
heavy
what side would RSS be on
3 prime end of V
what side is V on
5 prime
RSS stands for
recombination signal sequence
what always touches the segment
heptamers
heptamers always have
1 12 and 1 23 spacers
for heavy chain V and J always have the same
spacers
can we delete the diversity segment
no
what segment has the same spacer on 5 prime and 3 prime
D segment
what does all the recombination
RAG1/2
RAG1/2 is only expressed in developing
B and T cells
enzyme conformation requires a
12 and 23 spacer
RAG1/2 cleaves between
segment and heptamer
the coding joint is where
V and J come together
what happens in the signaling joint
DNA in the middle-> dont want-> degraded
germline DNA has all
possibilities
VJ-joined rearranges DNA
within individual B cell
IgM and IgD are expressed on the surface of a
B cell
alternative splicing dictates
IgM (normal)
IgD (alternative)
B cell receptor heterodimer=
signaling domain
short tails->
no signaling on its own
somatic hypermutation is unique to
BCRs
somatic hypermutation is only in B cells that have
seen antigens
somatic hypermutation is mediated by
AID enzymes
C-> U conversions get repair with random nucleotide is an example of
NHEJ complex
process of selecting BCR that binds the best is called
affinity maturation
one week after primary immunization what antibody is made
IgM
two weeks after primary immunization what antibodies are made
IgM/ IgG
TMD means
transmembrane domain
what determines BCR vx antibody for IgM and IgD only
alternative splicing
secretion domain lack what
TMD
TMD binds
BCR
J chain allows for
oligomerization of 5 IgMs
isotype switching=
class switching
isotype switching goes from IgM to
IgG/A/E
once isotype switching happens the B cell can no longer make
IgM or IgD
switch regions are roughly equivalent to
RSSs
class swithes also use
AID
once something is X out can u undergo futher class switching
yes to something not X out
what mediates removal or intervening sequence
loop AID
is VDJ recomincation variable of heavy and light chain alt splicing or recombination
recombinatioin
class switching make IgG/A/E is alt or recombination
recombination
IgM BCR to IgD BCR is alt or recombination
alt
make secreted IgM ot IgD is alt or recomb
alt
Dimeric IgA with j chain helps with
clumping
IgG is
flexible
IgG1, IgG2, IgG3 is neutralization or complement
complement
IgG4 is complement or neutralization
neutralization
is IgG4 monomeric
yes
in the curculation of IgG4 molecules become functionally
monovalent
IgG4 is unnatural and only happens in
circulation
IgG4 recgonize different things with
each arm
