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Viral Structure

Viral Structure

Viruses are extraordinarily diverse in shape and size, but they all have several structural features in common. All viruses have a core that contains a DNA- or RNA-based genome. The core is surrounded by a protective coat of proteins called the capsid. The capsid is composed of subunits called capsomeres. The capsid and genome-containing core are together known as the nucleocapsid.

Leaky Scanning

Leaky Scanning

During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA. Marilyn Kozak discovered that the sequence RCCAUGG (where R...

Viral Recombination

Viral Recombination

Cells are sometimes infected by more than one virus at once. When two viruses disassemble to expose their genomes for replication in the same cell, similar regions of their genomes can pair together and exchange sequences in a process called recombination. Alternatively, viruses with segmented genomes can swap segments in a process called reassortment.

Viral Mutations

Viral Mutations

A mutation is a change in the sequence of bases of DNA or RNA in a genome. Some mutations occur during replication of the genome due to errors made by the polymerase enzymes that replicate DNA or RNA. Unlike DNA polymerase, RNA polymerase is prone to errors because it is not capable of “proofreading” its work. Viruses with RNA-based genomes, like HIV, therefore accrue mutations faster than viruses with DNA-based genomes. Because mutation and recombination provide the raw material...

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Author Spotlight: Improved Method for Production and Purification of Adeno-Associated Viral Vectors

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Structural Changes Likely Cause Chemical Differences between Empty and Full AAV Capsids.

Caryn L Heldt^1,2, Molly A Skinner¹, Ganesh S Anand³

¹Department of Chemical Engineering, Michigan Technological University, Houghton, MI 49931, USA.

|September 28, 2024

Summary

This summary is machine-generated.

Adeno-associated virus (AAV) manufacturing requires better methods to separate empty and full capsids. Understanding structural differences can improve AAV therapies by ensuring patients receive optimal, effective doses.

Keywords:

biomanufacturing cryo-EM gene therapy virus structure

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Area of Science:

Biotechnology
Molecular Biology
Virology

Background:

Adeno-associated viruses (AAVs) show promise for treating single-gene disorders.
Current AAV manufacturing faces challenges in separating empty from full viral capsids.
The presence of empty capsids leads to higher, potentially unnecessary, viral doses for patients.

Purpose of the Study:

To address the need for improved AAV manufacturing processes.
To identify novel strategies for separating empty and full AAV capsids.
To enhance therapeutic efficacy and minimize side effects by optimizing capsid dosing.

Main Methods:

Reviewing current limitations of ultracentrifugation and anion exchange chromatography for capsid separation.
Proposing four theoretical structural differences between empty and full AAV capsids.
Investigating potential structural variations related to genome encapsulation.

Main Results:

Identified four hypotheses regarding structural changes in AAV capsids upon genome encapsulation.
Theories include capsid expansion/contraction, N-terminus constraint, and increased VP3 protein content in full capsids.
These proposed structural differences offer potential targets for improved separation techniques.

Conclusions:

Current AAV empty/full capsid separation methods have limitations.
Understanding structural differences is key to developing more efficient purification processes.
Further research into these theoretical structural changes could significantly advance AAV manufacturing and therapeutic applications.