Key result
Recombinant ASFV major capsid p72 trimers depolymerized in an acidic environment simulating late endosomes, explaining the disassembly mechanism of the viral icosahedral capsid.
Why the study?
How pH affects African swine fever virus capsid stability is limited, and which protein acts as an essential pH sensor during endosomal uncoating remains unknown.
The study identifies the ASFV major capsid protein p72 as a pH sensor that depolymerizes in acidic environments, explaining the virus's uncoating mechanism in endosomes.
p72 may mediate ASFV pH sensing; leaves open target validation for uncoating inhibitors.
African swine fever virus (ASFV) belongs to nucleocytoplasmic large DNA viruses (NCLDVs), the only member of Asfarviridae. So far, it is revealed that the ASFV uncoating is a pH-dependent process undergone in late endosomes. But, the research on how pH affects capsid stability is limited, and which protein plays an essential role in pH sensing remains unknown. In this study, we identified the main component of the ASFV capsid -- major capsid protein p72, as a pH sensitive residue abundance protein, and it is speculated that the conformational change of the p72 trimer is possibly responsible for the ASFV uncoating process. To test this speculation, we obtained recombinant p72 trimers, treated with the acidic environment that simulated endosomes and displayed structural analysis. The results showed that the p72 trimer depolymerized at low pH. The depolymerization of trimers rationally explains the disassembly mechanism of the ASFV icosahedral capsid in endosomes.
No takes yet. Share an insight, caveat, or question.
Meng et al. (2023) studied African swine fever virus (ASFV). Acidic environment simulating endosomes was evaluated on p72 trimer depolymerization. Recombinant ASFV major capsid p72 trimers depolymerized in an acidic environment simulating late endosomes, explaining the disassembly mechanism of the viral icosahedral capsid.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: