First-pass extracted concept

AAV11 VP1-importin-α interaction interface

Candidate: concept label1 source documents3 linked claims

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Aliases

VP1-IMPα recognition

Evidence Snippets

In this study, we characterize the molecular interface between AAV11 VP1 and host importin-α (IMPα). Structural and biochemical analyses reveal that the basic regions BR1 and BR3 of the VP1 N-terminal domain engage IMPα in a bipartite nuclear localization signal (NLS)-like manner.

Evidence 1Source 1DOI PubMedprovenance

Supporting Sources

Source 1primary paper2025MEDDOI PubMed

1 evidence snippet 3 linked claims Claim 1 Claim 2 Claim 3

Linked Claims

Claim 1engineering relevancesupports2025Source 1DOI PubMed

This study establishes a molecular basis for AAV11 VP1-host protein binding that can inform future capsid engineering.

Quoted textsource-backed

While direct functional evidence is pending, this work establishes the molecular basis for VP1-host protein binding and informs future capsid engineering.

Claim 2mechanismsupports2025Source 1DOI PubMed

The AAV11 VP1 N-terminal basic regions BR1 and BR3 engage host importin-α in a bipartite NLS-like manner.

Quoted textsource-backed

Structural and biochemical analyses reveal that the basic regions BR1 and BR3 of the VP1 N-terminal domain engage IMPα in a bipartite nuclear localization signal (NLS)-like manner.

Claim 3mechanistic implicationsupports2025Source 1DOI PubMed

The characterized VP1-importin-α interaction suggests a role in AAV11 nuclear import.

Quoted textsource-backed

These findings provide mechanistic insight into VP1-IMPα recognition and suggest a role for these interactions in AAV11 nuclear import.