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Related Experiment Video

Updated: Jul 7, 2026

Real-time Live Imaging of T-cell Signaling Complex Formation

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Published on: June 23, 2013

Quaternary structure of the immunostimulating complex (iscom).

M Ozel¹, S Höglund, H R Gelderblom

¹Robert Koch-Institute of the Federal Health Office, Berlin, Federal Republic of Germany.

Journal of Ultrastructure and Molecular Structure Research

|December 1, 1989

Summary

This summary is machine-generated.

Immunostimulating complexes (iscoms) were formed using viral proteins, Quil A, and cholesterol. These stable, cage-like particles exhibit icosahedral symmetry, enhancing antigen presentation for vaccines.

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Area of Science:

Biochemistry
Structural Biology
Immunology

Background:

Proteins from HIV-1, hepatitis B, and rabies viruses were studied.
The adjuvant substance Quil A and cholesterol were used.
The formation of immunostimulating complexes (iscoms) was investigated.

Purpose of the Study:

To analyze the formation and symmetry of regular iscoms.
To understand the structural properties of iscoms for antigen presentation.

Main Methods:

Electron microscopy was used to analyze iscom structure.
Freeze-drying preserved the matrix structures.
Tilting experiments and rotational image analysis determined symmetry.

Main Results:

Quil A formed micellar structures (12 nm).
Mixing Quil A and cholesterol created fragile matrix structures (40 nm).
Stable iscoms (32 nm) with cage-like, icosahedral symmetry were formed, irrespective of viral proteins.

Conclusions:

Iscoms exhibit uniform, cage-like structures with icosahedral symmetry.
The symmetrical shape contributes to iscom stability.
The structure facilitates efficient antigen presentation to the immune system.