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Complement C9 is inserted into membranes in a globular conformation.

D Marazziti¹, J P Luzio, K K Stanley

¹European Molecular Biology Laboratory, Heidelberg, FRG.

|January 30, 1989

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Complement component C9 requires elevated temperatures to change from its globular to an extended form for membrane attack complex (MAC) formation. At 0°C, C9 inserts in its globular state, remaining accessible and sensitive to digestion.

Area of Science:

Immunology
Molecular Biology
Biochemistry

Background:

The complement system plays a crucial role in innate and adaptive immunity.
Complement component C9 is the terminal component of the membrane attack complex (MAC).
MAC formation involves the polymerization of C9 within the target membrane.

Purpose of the Study:

To investigate the conformational changes of complement component C9 during membrane insertion.
To determine the temperature-dependent requirements for MAC formation.
To elucidate the mechanism of C9 insertion into biological membranes.

Main Methods:

Utilized low-temperature (0°C) incubation to study C9 binding to membranes.
Assessed C9 accessibility to the intracellular space.

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Performed trypsin digestion assays to evaluate C9 conformation and integrity.

Main Results:

At 0°C, single C9 molecules bind to the membrane but do not form a functional MAC.
C9 bound at 0°C is accessible to intracellular reagents and susceptible to trypsin digestion.
Elevated temperatures are necessary for C9 to adopt its extended conformation and facilitate MAC assembly.

Conclusions:

Complement component C9 inserts into membranes in a globular conformation at low temperatures.
A conformational transition from globular to extended is essential for C9 function in MAC formation.
Temperature is a critical factor regulating C9 conformational changes and downstream complement effector functions.