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Identification of the nucleolar localization signal in Autographa californica multiple nucleopolyhedrovirus

Guoqing Chen1, Yihong Wu1, Jing Yang1

  • 1State Key Laboratory of Rice Biology and Breeding, China National Rice Research Institute, Hangzhou, PR China.

The Journal of General Virology
|April 1, 2026
PubMed

Insights

Autographa californica multiple nucleopolyhedrovirus Ac16 protein has nuclear and nucleolar localization signals. It interacts with IE1 and SfVhaD, potentially moving partners from nucleoli to viral replication sites.

Area of Science:

  • Virology
  • Molecular Biology
  • Cell Biology

Background:

  • Autographa californica multiple nucleopolyhedrovirus (AcMNPV) Ac16 is a multifunctional protein unique to group I NPVs.
  • Understanding Ac16's function and localization is crucial for comprehending NPV infection.
  • Previous studies highlighted Ac16's multifunctionality, but its precise localization mechanisms remained unclear.

Purpose of the Study:

  • To investigate the nucleolar localization signals of AcMNPV Ac16 protein.
  • To identify Ac16 interaction partners and elucidate their role in viral replication.
  • To understand how Ac16 influences the subcellular localization of its interacting proteins.

Main Methods:

  • Protein truncation and subcellular localization analysis to identify Ac16 localization signals.
  • Point mutation analysis to pinpoint key residues for nuclear and nucleolar localization.
  • Yeast two-hybrid screening and co-immunoprecipitation to identify Ac16 interaction partners.
  • Co-expression assays to study the effect of interacting proteins on Ac16 localization.

Main Results:

  • Residues 78-113 of Ac16 contain functional nuclear (NLS) and nucleolar (NoLS) localization signals, specifically basic-amino-acid-rich clusters 78-84 and 108-113.
  • Ac16's nucleolar localization is modulated by its interaction with the AcMNPV IE1 protein, independently of Ac16's NoLS.
  • Vacuolar (H+)-ATPase subunit D (SfVhaD) was identified as an Ac16 interaction partner.
  • Ac16 influences SfVhaD localization, with both proteins co-localizing in nucleoli during transient expression and in the virogenic stroma during AcMNPV infection.

Conclusions:

  • Ac16 possesses a functional nucleolar localization signal and interacts with viral protein IE1 and host protein SfVhaD.
  • Ac16 may play a role in transporting interaction partners from the nucleolus to viral replication centers during AcMNPV infection.
  • These findings provide new insights into the complex mechanisms of AcMNPV replication and protein trafficking.
Keywords:
Ac16IE1baculovirusnucleolar localization signal

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