Laboratory Activity 3a – Basic Concepts of Antigen, Antibody, and Complement Flashcards

1
Q

A substance with the ability to combine with an antibody

A

ANTIGEN

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2
Q

• The ability of the antigen to react specifically with the antibodies or cells it provoked

A

Specific Reactivity

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3
Q

• The ability to provoke an immune response by stimulating the production of antibodies, proliferation of specific T cells, or both

A

Immunogenicity

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4
Q

• Substance that is capable of inducing an immune response

A

Immunogen

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5
Q

• No immunogenicity but has reactivity

A

Hapten

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6
Q

Two (2) kinds of haptens :

A

o Simple or nonprecipitating
o Complex or precipitating

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7
Q

Can combine with antibody; cannot produce precipitates

A

o Simple or nonprecipitating

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8
Q

Can combine with the antibody; produces precipitates

A

o Complex or precipitating

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9
Q

• Larger molecules attached to haptens that confer new antigenic specificities

A

Carrier/ Schlepper Molecules

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10
Q

o Capable of stimulating antibody synthesis in the host and can also react with homologous antibodies

A

Complete antigen

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11
Q

o Bacterial cells and proteins

A

Complete antigen

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12
Q

o Cannot by themselves stimulate an immune response

A

Hapten/Incomplete Antigen

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13
Q

o Can react specifically with homologous antibodies

A

Hapten/Incomplete Antigen

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14
Q

• Substance produced in response to antigenic stimulation that is capable of specific interaction with provoking immunogen

A

ANTIBODY or IMMUNOGLOBULIN (Ig)

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15
Q

ANTIBODY or IMMUNOGLOBULIN (Ig) General functions:
o Neutralize (?)
o Facilitate (?) and kill microbes
o Combine with antigens on cellular surfaces and cause the destruction of these cells either (?) (outside of the blood vessels within the mononuclear-phagocyte system) or (?) (within the blood vessels through the action of the complement)

A

toxic substances
phagocytosis
extravascularly; intravascularly

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16
Q

o A four-chain polypeptide unit that consists of two (2) heavy chains and two (2) light chains held together by disulfide bonds

A

Basic structure

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17
Q

4 polypeptide chain:
• 2 heavy chains: each consists of about _____ amino acids
• 2 light chains: each consists of about _____ amino acids

A

450
220

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18
Q

are always of the same type

A

The two (2) heavy chains

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19
Q

o They determine the immunoglobulin class: α, γ, δ, ε, µ

A

Heavy chains

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20
Q

o κ or λ

A

Light chains

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21
Q

o Both (?) are found in all classes of immunoglobulins, but only one type is present in a given molecule

A

κ or λ

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22
Q

o Holds each light chain to a heavy chain

A

Disulfide bonds

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23
Q

o Link the mid-region of the two heavy chains

A

Disulfide bonds

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24
Q

o Fragment antigen-binding

A

Fab fragment

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25
Q

o Consists of one (1) light chain and one-half (½) of a heavy chain

A

Fab fragment

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26
Q

o The intact immunoglobulin has (?), each representing one (1) antigen binding site

A

two (2) Fab fragments

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27
Q

o Fragment crystalline

A

Fc fragment

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28
Q

halves of the two heavy chains

A

carboxy-terminal end

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29
Q

o This portion of the molecule has no antigen binding ability

A

Fc fragment

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30
Q

o The carboxy-terminal end of the immunoglobulin molecule, where the amino acid sequence is the same for all chains of that type

A

Constant region

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31
Q

o Responsible for the type and antigen-antibody reaction that occurs

A

Constant region

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32
Q

o (?) of heavy chain differs from one antibody class to the other

A

Constant region

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33
Q

o The amino-terminal end of the immunoglobulin molecule, where the amino acid sequence varies

A

Variable region

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34
Q

o This part of the molecule is responsible for the specificity of a particular immunoglobulin

A

Variable region

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35
Q

Variable region is also known as the

A

ANTIGEN-RECOGNITION UNITS

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36
Q

o Different for each antibody molecule

A

Variable region

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37
Q

o Regions within the variable region that actually form the antigen-binding site

A

Hypervariable region

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38
Q

o Through changes in the (?), an immense diversity of antigen-binding sites can be created

A

Hypervariable region

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39
Q

o number of binding sites

A

Valence

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40
Q

o The flexible portion of the heavy chain, located between the first and second constant regions

A

Hinge region

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41
Q

o This allows the molecule to bend to let the two (2) antigen-binding sites operate independently

A

Hinge region

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42
Q

o A glycoprotein that serves to link immunoglobulin monomers together

A

Joining chain

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43
Q

Joining chain is only found in __________ and _________________________

A

IgM and IgA2

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44
Q

• Predominant immunoglobulin in humans comprising approximately 75-80% of the total serum immunoglobulins

A

IgG

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45
Q

• 7S molecule with a molecular weight (MW) of approximately 150,000 Daltons

A

IgG

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46
Q

• Made up of one basic structural unit known as a monomer consisting of two heavy and two light chains, which may be kappa or lambda (but not both)

A

IgG

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47
Q

• Has the longest half-life, approximately 23-25 days

A

IgG

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48
Q

• Functions of IgG:
o Providing (?) for the newborn
o (?) of the complement
o (?)
o (?) of toxins and viruses
o Participation in (?) reactions

A

immunity
Fixation
Opsonization
Neutralization
agglutination

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49
Q

• Most primitive; first to appear in phylogeny and the last to leave in senescence

A

IgM

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50
Q

• First to appear after a primary antigenic stimulus

A

IgM

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51
Q

• Made up of five basic structural units (pentamer) in circular arrangement, 10 heavy chains and 10 heavy light chains

A

IgM

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52
Q

• Possess J chain (MW: approximately 15,000 Daltons)

A

IgM

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53
Q

• 19S molecule with a MW of approximately 900,000 Daltons

A

IgM

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54
Q

IgM Functions:

A

o Complement fixation .
o Agglutination
o Opsonization
o Neutralization of toxins

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55
Q

• In the serum, it primarily appears as a monomer

A

IgA

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56
Q

• is also found as a dimer in body secretions along the respiratory and intestinal mucosa and in milk, saliva, tears and sweat

A

IgA (IgA2)

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57
Q

• The dimer consists of two monomers held together by a J chain

A

IgA

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58
Q

is synthesized in the plasma cells found mainly in mucosal-associated lymphoid tissue (MALT) and it is released in dimeric form

A

Secretory IgA

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59
Q

Secretory component

A

Secretory IgA

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60
Q

is found on the surface of immunocompetent but unstimulated B lymphocytes

A

IgD

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61
Q

• Postulated to be an anti-idiotypic antibody (antibody to antibody) and as such may be involved in the feedback mechanism to switch off B cells

A

IgD

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62
Q

• Function of IgD:

A

o Immunoregulation

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63
Q

• Least abundant immunoglobulin in the serum

A

IgE

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64
Q

• Heat-labile antibody

A

IgE

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65
Q

o Mediates some types of hypersensitivity (allergic reaction), allergies, and anaphylaxis and is generally responsible for an individual’s immunity to invading parasites

A

IgE

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66
Q

o Binds strongly to a receptor on mast cells and basophils and together with antigen, mediates the release of histamine and heparin from these cells

A

IgE

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67
Q

• A defensive system consisting of over 30 proteins produced by the liver and found in circulating blood serum

A

COMPLEMENT SYSTEM

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68
Q

o Serum proteins that interact to enhance the host defense reactions

A

COMPLEMENT SYSTEM

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69
Q

o Most are inactive enzyme precursors that are converted to active enzymes in a precise order

A

COMPLEMENT SYSTEM

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70
Q

• It works as a cascade system: when one reaction triggers another reaction which triggers others and so on; these types of systems can grow exponentially very fast

A

COMPLEMENT SYSTEM

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71
Q

o Following activation, opsonization occurs as complement components coat pathogenic organisms or immune complexes, facilitating the process of phagocytosis

A
  1. Opsonization
72
Q

o Activation of the complement system results in induction of histamine release from mast cells and basophils, and stimulation of inflammatory response

A
  1. Inflammation
73
Q

o In the final stage of the complement cascade membrane attack of target cells (e.g. bacteria and tumor cells) occur, leading to cell death

A
  1. Cytotoxic
74
Q

Nomenclature:
1. ([?] for complement, [?] for the components)
2. The peptide chains
3. Cleaved peptides
4. If further proteolysis results in the loss of fragment activity
5. When a complement protein acquires enzymatic activity

A

“C”, 1 to 9
Greek letters (e.g. C3-α, C4-β)
lower case Arabic letters (e.g. C3a)
subscript “i”
horizontal bar

75
Q

• Complement components are serum proteins produced by the __________ EXCEPT:
o ____________________________________________________
o ____________________________________________________

A
76
Q

• Present in HIGHEST concentration in plasma: _____

A
77
Q

• Key component of the pathways: _____

A
78
Q

o Involves a more recently evolved mechanism of specific adaptive immunity

A

Classical Pathway

79
Q

o It is initiated by the presence of antigen-antibody complex (immune complex)

A

Classical Pathway

80
Q

o Classical pathway normally requires suitable antibodies bound to an antigen, complement components 1, 4, 2 and 3, and calcium (Ca++) and magnesium (Mg++) cations

A

Classical Pathway

81
Q

Binds to Fc of IgM and IgG

A

C1q

82
Q

Activates C1s

A

C1r

83
Q

Cleaves C4 and C2

A

C1s

84
Q

Part of C3 convertase

A

C4

85
Q

Binds to C4b

A

C2

86
Q

Key intermediate in all pathways

A

C3

87
Q

Initiates membrane attack complex (MAC)

A

C5

88
Q

Binds C5b in MAC

A

C6

89
Q

Binds to C5bC6 in MAC

A

C7

90
Q

Starts pore formation on membrane

A

C8

91
Q

Polymerizes to cause cell

A

C9

92
Q

It requires the interaction of all nine (9) major complement components

A

Classical Pathway

93
Q

• A trimolecular complex (C1q, C1r, and C1s) held together by Ca+2 ions

A

C1: Recognition Unit

94
Q

• C1q is the largest and consists of 6 globes held on slender shafts that fuse a common base

A

C1: Recognition Unit

95
Q

o The 6 globes act as the recognition units that bind to the Fc region of IgM and IgG

A

C1: Recognition Unit

96
Q

• For C1q to initiate the cascade, it must attach to two Fc fragments from IgG and/or IgM

A

C1: Recognition Unit

97
Q

attaches to the immunoglobulin and initiates complement activation

A

C1q

98
Q

initiates C1r

A

C1q binding

99
Q

cleaves C1s

A

C1r

100
Q

• C4 is a beta globulin originates from a proC4 synthesized by the macrophage

A

C4: First activation unit

101
Q

• It consists of 3 peptide chains (C4-α, C4-β, C4-γ) joined by disulfide bonds

A

C4: First activation unit

102
Q

• C4 is cleaved into C4a and C4b by C1s

A

C4: First activation unit

103
Q

mediates cleavage of C4 into C4a and C4b

A

C1s

104
Q

is bound to cell membrane while C4a is released into the fluid phase

A

C4b

105
Q

• C2 is cleaved into C2a and C2b by C1s in the presence of C4b

A

C2: Second activation unit

106
Q

in the presence of C4b (C14b) cleaves C2 units into C2a and C2b

A

C1s

107
Q

is bound to the cell-bound C4b while C2b is released in the fluid phase

A

C2a

108
Q

• It is the most abundant complement component in the serum.

A

C3: Third activation unit

109
Q

• It is cleaved by C3 convertase into C3a and C3b.

A

C3: Third activation unit

110
Q

is cleaved by C3 convertase into C3a and C3b

A

C3

111
Q

remains unbound C3b is bound to the cell bound C4b2a (C4b2a3b: _______________)

A

C3a

112
Q

• C5 is cleaved by C5 convertase into C5a and C5b

A

C5: First membrane attack unit

113
Q

is cleaved by C5 convertase into a smaller C5a and a larger C5b

A

C5

114
Q

is released into the surrounding fluid medium

A

C5a

115
Q

is the first component of the membrane attack complex. It is the receptor of C6 and C7

A

C5b

116
Q

binds to C6 forming a stable C5b6 complex

A

C5b

117
Q

: Second membrane attack unit

A

C6

118
Q

: Third membrane attack unit

A

C7

119
Q

binds to C7 forming the stable C5b67 that is bound to the target cell membrane

A

C5b6

120
Q

: Final membrane attack unit

A

C8

121
Q

binds to C5b67 complex and leakage of membrane begins.

A

C8

122
Q

Cell lysis can occur by the C5b678 complex in the absence of

A

C9

123
Q

: Final membrane attack unit

A

C9

124
Q

binds to C5b678 complex and accelerates cytolysis by producing circular lesions in the membrane

A

C9

125
Q

induces the formation of hollow cylinders (tubules) in the bilipid layer of the cell membrane allowing exit of electrolytes and water out of the cell

A

C5b6789 complex

126
Q

o Provides nonspecific innate immunity

A

Alternate Pathway

127
Q

o It is considered a primitive defense mechanism, a bypass mechanism that does not require C1, C4 and C2 interaction

A

Alternate Pathway

128
Q

o An antigen-antibody complex is not required for it to take place

A

Alternate Pathway

129
Q

Binds C3b to form C3 convertase

A

Factor B

130
Q

Cleaves Factor B

A

Factor D

131
Q

Stabilizes C3 convertase

A

Properdin

132
Q

Begins with the activation of C3 and requires Factors B and D, and magnesium cation (Mg++), all present in normal serum

A

Alternate Pathway

133
Q

The initial recognition necessary for the alternative pathway is the presence of C3, specifically (?) which is probably continuously generated in small amounts in the circulation

A

C3b

134
Q

C3 activation: o Non-immunologic

A

• Lipopolysaccharide (LPS)
• Endotoxin from the cell walls of gram-negative bacteria
• Cell walls of some bacteria
• Cell walls of yeasts (zymosan)
• Cobra venom factor (CVF)

135
Q

C3 activation: o Immunologic

A

• IgA
• Other antibodies

136
Q

exists in trace amounts in normal serum

A

C3b

137
Q

interacts with Factor B (C3 proactivator) to form C3bB, which is a magnesium ion-dependent complex

A

C3b

138
Q

is cleaved by Factor D (C3 proactivator convertase) into 2 fragments, Ba and Bb Ba is released and Bb is bound to C3b forming the C3bBb complex: amplification C3 convertase

A

C3bB

139
Q

When stabilized by (?), the C3bBb complex becomes the C3 convertase that cleaves C3 into C3a and C3b

A

Properdin (P)

140
Q

As more (?) is generated, the complex expands (C3bnBb) and becomes a C5 convertase

A

C3b

141
Q

cleaves C5 into C5a and C5b initiating the membrane attack pathway

A

C5 convertase

142
Q

Membrane attack complex

A

(C5b6789)

143
Q

• Involved attachment of mannose-binding lectin to mannose residues on glycoproteins or carbohydrates on surface of microorganisms

A

Mannose-Binding Lectin (MBL) Pathway

144
Q

Binds to mannose

A

Mannose Binding Lectin (MBL)

145
Q

Helps cleave C4 and C2

A

MBL-associated Serine Protease-1 (MASP-1)

146
Q

Cleaves C4 and C2

A

MBL-associated Serine Protease-2 (MASP-2)

147
Q

Macrophages that digest microbes release chemicals that cause the liver to produce (?): proteins bind to carbohydrates on the microbe surface

A

lectins

148
Q

is produced by liver in acute phase inflammatory reactions

A

MBL

149
Q

binds to mannose on many bacterial cells

A

MBL (mannose-binding lectin)

150
Q

Once MBL binds to target cell, (?) bind to bacterial surface Acts like C1

A

2 serine proteases (MASP-1, MASP-2)

151
Q

Cleaving of C4 and C2 forming

A

C3 convertase

152
Q

Cleaving C3 forming

A

C5 convertase

153
Q

Cleaving of C5 initiates the formation of the

A

membrane attack complex (C5b6789)

154
Q

are the key elements in a serologic reaction.

A

Antigens and antibodies

155
Q

The study of the properties and types of antigens and antibodies are essential in the understanding of (?)as well as the (?) of the immune system.

A

serologic reactions ; responses

156
Q

usually are present in humans as well as in animal serum. They may participate in serologic reactions, although some tests in serology, human complement is often inactivated, and an exogenous complement is used.

A

complement proteins

157
Q

are activated in a cascade of reactions when these participate in a serologic reaction

A

complement proteins

158
Q

The pathogens capable of causing infectious diseases in humans include bacteria, viruses, fungi, parasites and infectious proteins. (?) are usually associated with these pathogens.

A

Antigens

159
Q

The J chain is found only in the following immunoglobulins

A
160
Q

Activation Sequence: C1q attaches to the immunoglobulin and initiates complement activation ® C1q binding initiates C1r ® C1r cleaves C1s

A

C1: Recognition Unit

161
Q

Activation Sequence: C1s mediates cleavage of C4 into C4a and C4b ® C4b is bound to cell membrane while C4a is released into the fluid phase

A

C4: First activation unit

162
Q

Activation sequence: C1s in the presence of C4b (C14b) cleaves C2 units into C2a and
C2b ® C2a is bound to the cell-bound C4b while C2b is released in the fluid phase ® C4b2a complex is now attached on the surface of the cell membrane

A

C2: Second activation unit

163
Q

Activation sequence: C3 is cleaved by C3 convertase into C3a and C3b ® C3a remains
unbound ® C3b is bound to the cell-bound C4b2a ® C4b2a3b complex is now attached on the surface of the cell membrane

A

C3: Third activation unit

164
Q

Activation Sequence: C5 is cleaved by C5 convertase into a smaller C5a and a larger
C5b ® C5a is released into the surrounding fluid medium ® C5b is the first component of the membrane attack complex that is bound on the surface of the cell membrane that serves as the receptor of C6 and C7

A

C5: First membrane attack unit

165
Q

Activation Sequence: C6 binds to cell-bound C5b forming a stable C5b6 complex

A

C6: Second membrane attack unit

166
Q

Activation Sequence: C7 binds to cell-bound C5b6 forming the stable C5b67 that is bound to the target cell membrane

A

C7: Third membrane attack unit

167
Q

Activation Sequence: C8 binds to C5b67 complex and leakage of membrane begins ® Cell lysis can occur by the C5b678 complex in the absence of

A

C8: Final membrane attack unit

168
Q

Activation Sequence: C9 binds to cell-bound C5b678 complex accelerates cytolysis by
producing circular lesions in the membrane ® C5b6789 complex induces the formation of hollow cylinders (tubules) in the bilipid layer of the cell membrane allowing exit of electrolytes and water out of the cell

A

C9: Final membrane attack unit

169
Q

where C3b that exists in trace amounts in normal serum becomes membrane bound on the surface of target cells

A

C3 activation

170
Q

The membrane-bound (?) interacts with Factor B (C3 proactivator) to form C3bB, which is a magnesium ion-dependent complex

A

C3b

171
Q

is cleaved by Factor D (C3 proactivator convertase) into 2 fragments, Ba and Bb

A

C3bB

172
Q

is released, and Bb is bound to C3b forming the C3bBb complex: amplification C3 convertase

A

Ba

173
Q

When stabilized by (?), the C3bBb complex becomes the C3 convertase that cleaves C3 into C3a and C3b

A

Properdin (Factor P)

174
Q

As more (?) is generated, the complex expands (C3bnBb) and becomes a C5 convertase (e.g., C3bBb3b)

A

C3b

175
Q

MBL acts like (?) of the classical pathway but binds to mannose on many bacterial cells

A

C1q

176
Q

Once MBL binds to the target cell, (?) bind to the bacterial surface. MASP-1 and MASP-2 act like C1r and C1s of the classical pathway, respectively

A

two serine proteases (MASP-1, MASP-2)