Recognition of extracellular pathogens Flashcards

1
Q

What are TLRs

A

Toll-like receptors

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2
Q

What do TLR’s do

A

Recognize variety of PAMPS

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3
Q

What receptors do macrophages have

A
  • MAnnose
  • CD14
  • scavanger receptor
  • c reactive protein
  • Mannan binding lectin
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4
Q

How are immunoglobulins made

A
  • MIcrobe infects body
  • MIcrobe has antigen
  • B cell binds to it
  • B cells releases antibody which is specific to antigen
  • Antibodies also known as immunoglobulins
  • Antigen combining site on antibody bind to the antigen
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5
Q

What part of the microbe binds to the antibody

A

Antigenic determinant/EPITPOPE part of antigen binds to antigen binding site

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6
Q

How does an antibody bind to an antigen

A
  • Non covalent interactions only effective on short distances
  • For there to be strong non-covalent interactions to occur between antibody and antigen, the shape must fit snugly (complementary)
  • strong binding = specific interaction; high affinity
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7
Q

What are the different immunoglobulins that a B lymphocyte has

A
  • membrane bound immunoglobin (B cell surface immunoglobulin)
  • immunoglobins released by B lymphocyte
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8
Q

How are plasma cells formed

A

Membrane bound immunoglobulin binding to antigen activates B cells and so these can mature to plasma cells.

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9
Q

What do plasma cells do

A

Release antibodies that bind to the same antigen that the B cell was bound to

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10
Q

What is clonal selection

A

Each B cell can recognize a single epitome (each has only 1 specific antigen binding site)

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11
Q

How are memory cells and clonal selection linked

A

Primary response;

  • Antigen binds to clones (groups) of B cell which binds to it most strongly (highest affinity)
  • THe activated B cell clones itself and loads of that clone of B cell are made
  • Some rest in body (memory cells) and some turn into plasma cells
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12
Q

How many polypeptide chains does an antibody have

A

4

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13
Q

What does each polypeptide chain have on an antibody

A

Globular regions made of domains

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14
Q

What is the hinge region

A

Halfway down heavy chain where there is no domain

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15
Q

Where are the disulfide bridges in an antibody

A

Between cysteine residues

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16
Q

Why do classes and isotopes of immunoglobulins exist

A

Because different types of gene which code for the constant domain

17
Q

What do all newly formed B cells have

A

IgM constant region (natural form of immunoglobulin)

18
Q

What happens when immunoglobulin is activated by antogen

A

Class switching - stops using 1 of the 9 genes and uses another so there’s a change in the constant region in heavy chain

19
Q

What remains the same after class-switching

A

Variable domain same in IgE and IgM structure

20
Q

which isotopes are monomers

A
IgG1 
IgG3
IgG3
IgD
IgE
21
Q

Which structure is a dimer? What are the monomers held by

A

IgA

-held together by J chain

22
Q

Which isotope is a pentamer? What are the monomers held by?

A

IgM

-held together by J chain

23
Q

Where is IgM found

A

BLood

24
Q

Where is IgG found

A

Blood, tissues and placental transfer

25
Q

Where is IgA found

A

Blood/tissues (monomers) and mucosal secretions (dimers)

26
Q

Where is IgE found

A

Tissues (bound to mast cells)

27
Q

Where is IgD found

A

MUsosa of upper aerodigestive tract