Antibodies (Abs) or Immunoglobulins (Igs) Flashcards
What kind of proteins are antibodies? What produces them?
They are plasma glycoproteins produced by plasma cells (Ab-producing cells of B cell lineage) in response to antigens.
In which phases do antibodies bind to their specific antigens?
In both the recognition phase (as membrane Igs [BCRs]) and the effector phase (as secreted Abs) of HUMORAL IMMUNITY.
What percentage of total plasma protein is secreted Abs?
~20% of total plasma protein.
In addition to plasma, secreted Abs are also found where?
In mucosal secretions and the interstitial fluid of tissues.
T or F?
Antibodies are beta-globulins.
FALSE.
Antibodies are gamma-globulins.
What percentage of IgG is carbohydrate?
3-4%
What percentage of IgA, IgM, IgD, and IgE is carbohydrate.
10-18%
T or F?
The oligosaccharide side chains of Igs are usually attached to the CH2 or CH3 domains of the Ig light chain.
FALSE.
The oligosaccharide side chains of Igs are usually attached to the CH2 or CH3 domains of the Ig HEAVY chain.
These structures possess subterminal galactose and terminal neuraminic acid…
The oligosaccharide side chains of Igs.
What does the half-life of Igs in the circulation depend on?
The half-life of Igs in the circulation depends on the status of the oligosaccharide side chains.
For example, When ABs in the circulation have the neuraminic acid removed by the enzyme neuraminidase, the now terminal galactose binds to a receptor on liver cells, triggering endocytosis of the Ig –> the Ig is then degraded by the proteolytic enzymes in the lysosomes of the cell.
How many polypeptide chains do Ig molecules consist of? How many are light and how many are heavy?
4: two identical light (L) chains and two identical heavy (H) chains.
What are the polypeptide chains of the Ig molecules held together by?
They are held together by noncovalent AND covalent inter/intrachain disulfide bonds.
T or F?
Each chain of the Ig molecule consists of a variable (V) and a constant (C) region.
TRUE
What is a “domain” in the Ig context?
It is a 3-dimensionally folded repeating segment - a loop of about 60 AAs around an intrachain S-S bond.
T or F?
An L chain consists of one variable (VL) and one constant (CL) domain.
TRUE.
T or F?
Most H chains consist of one variable (VH) and one constant (CH) domain.
FALSE.
Most H chains consist of one variable (VH) and 3-4 constant (CH) domains.
IgA, IgG, and IgD possess how many CH domains? What are they called?
3 CH domains: CH1, CH2 and CH3.
IgE and IgM possess how many CH domains? What are they called?
4 CH domains: CH1, CH2, CH3, and CH4.
What is a hinge region?
It is a proline-rich region between the CH1 and CH2 domains.
What does the hinge region do to the structure of the Ig molecule?
The hinge region confers segmental flexibility on the Ig molecule, which allows the two antigen combining sites (Fabs) to simultaneously bind 2 epitopes separated by varying distances.
T or F?
All Igs have hinge regions.
FALSE.
IgE and IgM do not possess hinge regions.
What does it mean that Ig molecules are ‘bifunctional’ in nature?
To say that Ig molecules are bifunctional is to say that: the antigen recognition functions AND the effector functions of Ig molecules are spatially separated from each other.
What two enzymes did scientists use to determine that Ig molecules are bifunctional in nature? What do these enzymes do?
Papain and pepsin…
Papain: cleaves IgG ABOVE the S-S bond at the hinge region, which produces 2 antigen-binding fragments (bivalent); The Fab region, which stands for fragment antigen binding; Fc, which stands for fragment crystallizable.
Pepsin: Cleaves IgG BELOW the S-S bond at the hinge region.
T or F?
The hinge region and interchain disulfide bonds are retained in a F(ab’)2 molecule, but the Fc fragment is degraded after pepsin acts upon an IgG.
If so, why? If not, why?
This is TRUE because pepsin will cleave BELOW the S-S bond at the hinge region.