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From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins

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The M13 Phage Assembly Machine Has a Membrane-Spanning Oligomeric Ring Structure.

Maximilian Haase¹, Lutz Tessmer¹, Lilian Köhnlechner¹

¹Institute of Biology, University of Hohenheim, 70599 Stuttgart, Germany.

|June 24, 2022

Summary

Bacteriophage M13 uses a membrane machine, including G1p and G11p proteins, to assemble progeny. This complex forms a pore, facilitating phage filament passage through the outer membrane secretin for efficient viral replication.

Keywords:

affinity chromatography bacteriophage M13 circular dichroism membrane protein phage assembly machine

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Area of Science:

Molecular biology
Virology
Structural biology

Background:

Bacteriophage M13 assembles progeny in the host inner membrane.
Key components include G1p and G11p, forming a complex with a pore and ATP-hydrolyzing domain.
Phage filament formation involves G8p coat protein and single-stranded DNA.

Purpose of the Study:

To elucidate the structural details of the M13 phage assembly machine.
To investigate the complex formed by inner membrane proteins G1p/G11p and outer membrane G4p secretin.

Main Methods:

Purification of G1p from infected E. coli.
Overproduction of G1p and G11p.
Solubilization of the multimeric complex from the membrane.

Main Results:

A multimeric complex of approximately 320 kDa was purified.
The complex exhibited a pore-like structure with an outer diameter of about 12 nm.
This structure matches the dimensions of the outer membrane G4p secretin.

Conclusions:

The purified complex represents a key part of the M13 assembly machine.
Structural data supports the proposed mechanism of phage assembly and secretion.
Further understanding of this machine aids in comprehending viral replication strategies.