Clonal selectional theory Flashcards

1
Q

What are the major features of clonal selection?

A

1.The immune system is comprised of a heterogeneous population of
billions of different lymphocytes.

  1. Each individual lymphocyte is specific for a single epitope of an antigen.
  2. This antigen-specificity is by virtue of each lymphocyte’s unique surface
    receptor.
  3. Only a small number of lymphocytes will recognize a specific antigen.
  4. Recognition of an antigen (i.e. interaction of the antigen with the
    lymphocyte receptor) signals the cell to undergo proliferation. This
    results in a clone of cells all expressing receptors with the same antigen-
    specificity.
  5. Proliferating lymphocytes will eventually differentiate into either effector
    cells or memory cells.
  6. Self-reactive lymphocytes are deleted at an early stage in lymphoid cell
    development.
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2
Q

the antigen-specific receptors in the case of B cells are membrane-bound _______

A

Immunoglobulins

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3
Q

What reaction would the B and C cells have if there is an antigen exposure subsequent to the initial exposure?

A

-memory
cells are more easily “triggered” than so-called naïve lymphocytes.

-this means that the immune system is able to respond in a shorter
period of time upon subsequent infection.

-Memory cells also produce an immune response larger in magnitude than naïve lymphocytes.

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4
Q

What are antibodies? (Ab or Ig)

A

glycoproteins found in SERUM, extracellular fluid, and mucosal secretions.

-SECRETED by EFFECTOR B cells in response to foreign substances called antigens (Ag)

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5
Q

Antibodies are antigenic _____

A

specific

-they only bind to ONE SPECIFIC ANTIGEN

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6
Q

What major fractions can be obtained when separating serum? and which one can you find immunoglobulin?

A

albumin, alpha-globulin, beta-globulin, and y-
globulin

y-globulin

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7
Q

What chains do antibody molecule MONOMER consist of? and what is their confirmation?

A

TWO heavy H chains

TWO light L chains

**Each H chain is linked COVALENTLY to an L CHAIN by a disulfide bond formed between cystine residues

** The two H chains are also linked to each other by s-s bonds, producing a flexible region that is referred to as a HINGE REGION

EVERYTHING FORMS Y SHAPE

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8
Q

what is a hinge region?

A

the flexible region produced by The two H chains linked to each other by s-s bonds

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9
Q

How can an antibody monomer be split to become functional units? and what are each of the functional units functions?

A

the antibody molecules are cleaved into various parts by using PAPAIN (enzyme)

Fab- include one light chain and part of a heavy chain. contains ONE BINDING site for an antigen. (TWO fabs per monomer—- two binding sites for an antigen)
*EACH FAB DINIGN SITE IS IDENTICAL!! bind to the same antigen

Fc- made up of two parts s of heavy chains. Determines SPECIFIC EFFECTOR FUNCTIONS that the immune system will take on the antigen-antibody complex

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10
Q

What is a domain?

A

tightly folded regions of about 100 amino acids on each Immunoglobulin chain of a monomer

light chain has 2 domains

heavy chain has 4 domains

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11
Q

What are the variable regions (Vh and Vl) and the constant regions (Ch and Cl) in an immunoglobulin?

A

Variable regions- domains at N-terminus in both heavy and light chains, where ANTIGEN- SPECIFICITY of a particular antibody resides.
Vh and Vl combine together to FORM a SHAPE that recognizes and BINDS antigens together (antigen binding site)

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12
Q

What are hypervariable regions? (or CDRS)

A

-three segments of extreme high variability in both Variable regions for H and l chains. (Three hyper variable regions in EACH DOMAIN)

-when the Vh and Vl variable regions bind (uniting a total of six variable regions or 6 CDRS), they create a binding site for a specific epitope.

**HYPERVARIABLE regions for Vh DIFFER from the hypervariable regions of VL

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13
Q

what are the five CLASSES of immunoglobulin (Isotypes) in mammals, their H CHAIN DESIGNATION, and their number of CDRS on each variable region?

A
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14
Q

Which class of immunoglobulin is the most prominant?

A

IgG

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15
Q

Where are the hinges present on each type of immunoglobulin?

A

IgG, IgA, IgD - between Ch1 and cH2 (HAVE 3 CDR’S)

IgM, IgE- between ch2-ch3 ( HAVE 4 CDR’S)

*** the constant region of each class is THE SAME to the others OF THEIR CLASS

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16
Q

Which Ig’s are classified as polymeric Ig’s and why?

A

IgM and IgA

IgM is found in the SERUM (circulation only– not tissue due to size) as a PENTAMER.
it is held together by a J CHAIN
has 10 binding sites (due to 2 binding sites per monomer attached)

IgA found in serum as monomers and dimers.
-ONLY found as DIMERS in SECRETIONS (secretory IgA)
-regular DIMERS have a J CHAIN only
-Secretory IgA have J chain and a SECRETORY COMPONENT

17
Q

what is multiple myeloma? and how can it be found?

A

-cancer of a SINGLE plasma cell (effector B cells)

-caused by a single plasma cell becoming neoplastic (growing out of control) and crowding the bone marrow

-produce large amounts of myeloma protein

-found by VERY large y-globulin peak in serum

-IgG spike goes up and and calcium levels go up

18
Q

Antibodies are found in ______

A

bODY FLUIDS

19
Q

ALBUMIN IS THE MOST PRESENT IN SERUM

A
20
Q

Fc are easily _____

A

crystallizable

21
Q

though one antibody has two different binding regions they can only _____ to one epitope, why?

A

bind

  • h chains are equal all throughout
    -L chains are equal all throughout
    *due to variable regions
22
Q

hypervariable regions allow for _____

A

each antibody to bind to different epitopes

23
Q

What are the types of light chain isotypes?

A
24
Q

chickens only have ______ light chains

A

Lambda

25
Q

What are the Ig classes in chickens?

A

ONLY THREE
-IgY
-IgA
-IgM

26
Q

what Ig isotope classes do camelids have?

A

**Only have two IgG sublclasses

-Have Vh region (called VHH) that forms binding site WITHOUT A LIGHT CHAIN

27
Q

True or false: one antibody molecule can have a kappa light chain and a lambda light chain?

A

FALSE

28
Q

true or false: VH domains of the two heavy chains in an antibody molecule are identical in their amino acid sequence

A

TRUE