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Related Experiment Video

Updated: May 17, 2026

Modeling The Lifecycle Of Ebola Virus Under Biosafety Level 2 Conditions With Virus-like Particles Containing Tetracistronic Minigenomes

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Published on: September 27, 2014

African swine fever virus morphogenesis.

María L Salas¹, Germán Andrés

¹Centro de Biología Molecular Severo Ochoa (Consejo Superior de Investigaciones Científicas-Universidad Autónoma de Madrid), 28049 Madrid, Spain. mlsalas@cbm.uam.es

|October 13, 2012

Summary

African swine fever virus (ASFV) assembly involves intricate cytoplasmic viral factories. Studies reveal key structural proteins and membrane interactions during ASFV morphogenesis.

Area of Science:

Structural biology
Molecular biology
Virology

Background:

African swine fever virus (ASFV) is an enveloped virus with icosahedral morphology.
ASFV virions comprise four concentric layers: nucleoid, core shell, inner envelope, and capsid.
ASFV assembly occurs in specialized cytoplasmic regions known as viral factories.

Purpose of the Study:

To review recent structural and molecular biology findings on ASFV morphogenesis.
To elucidate the roles of structural proteins and cellular components in virus assembly.
To understand the sequential steps in the formation of the ASFV particle.

Main Methods:

Immunocytochemical techniques
Electron microscopy
Molecular biology studies

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Biochemical studies

Use of ASFV inducible recombinants

Main Results:

Identified genes for 19 of 54 structural proteins and localization of 18 within the virion.
Recognized endoplasmic reticulum membranes as precursors for the inner envelope.
Described capsid formation on the inner envelope's convex face and core shell assembly on the concave side.
Highlighted the role of viral polyproteins and protease in core shell development.

Conclusions:

ASFV morphogenesis is a complex, multi-step process involving specific protein-membrane interactions.
Viral factories are crucial sites for ASFV assembly.
Inducible recombinants are valuable tools for dissecting protein functions in ASFV assembly.