. 2022 Aug 24;118(4):295–308. doi: 10.1111/mmi.14974

TABLE 1.

Key facts on nuclear entry of parvovirus capsids

	Nuclear entry requirements	Active transport NPC	Interaction with Nups	NEBD
Autonomous parvovirus	B19V: Potential depletion of capsid‐associated divalent cations for uncoating (Caliaro et al., 2019) CPV and H‐1PV: Ca²⁺ release for NE disruption (Porwal et al., 2013)	CPV: Capsids recruit importin β to form capsid‐importin β complex (Mäntylä et al., 2020) capsid‐importin β complex is transported into the nucleus (Mäntylä et al., 2018)	H‐1PV: Coprecipitation with Nup358, Nup153 and Nup62 (Porwal et al., 2013) Interaction with Nups may trigger PLA₂ exposure to induce initial Ca²⁺ release for NE disintegration (Porwal et al., 2013)	MVM: NE invagination and redistribution of lamin A/C (Cohen et al., 2006) H‐1PV: Ca²⁺ release triggers activation of mitotic factors (PKC, cdk2/cdk1 and caspase 3) for NE disintegration by local lamin B depolymerization. No soluble cytosolic factors needed in permeabilized cells (Porwal et al., 2013) CPV failed to infect cells preloaded with hepatitis B capsids by microinjection (Porwal et al., 2013)
Dependo‐parvovirus	AAV2: Capsid acidification (pH 5.2) and Ca²⁺ release was required for NE disruption (Porwal et al., 2013)	AAV2: Three NLS‐like motifs in VP1 and VP2 essential for infection (Johnson et al., 2010). Three PDZ‐motifs on VP1u essential for nuclear entry and infection (Popa‐Wagner et al., 2012). Labeled capsids pass‐through NPC, no evidence of NE disintegration: (Kelich et al., 2015) rAAV2: Interaction with importin β with or without interaction with importin α (Nicolson & Samulski, 2014)	AAV2 coprecipitates with Nup358, Nup153 and Nup62 (Porwal et al., 2013)	NEBD limited to microinjected AAV2 capsid exposed to pH 5.2 (Porwal et al., 2013) NE invagination showed by EM (Cohen et al., 2006; Cohen & Panté, 2005)

Nuclear entry requirements

Active transport NPC

Interaction with Nups

NEBD

Autonomous parvovirus

B19V: Potential depletion of capsid‐associated divalent cations for uncoating (Caliaro et al., 2019)

CPV and H‐1PV: Ca²⁺ release for NE disruption (Porwal et al., 2013)

CPV: Capsids recruit importin β to form capsid‐importin β complex

(Mäntylä et al., 2020)

capsid‐importin β complex is transported into the nucleus (Mäntylä et al., 2018)

H‐1PV: Coprecipitation with Nup358, Nup153 and Nup62 (Porwal et al., 2013)

Interaction with Nups may trigger PLA₂ exposure to induce initial Ca²⁺ release for NE disintegration (Porwal et al., 2013)

MVM: NE invagination and redistribution of lamin A/C (Cohen et al., 2006)

H‐1PV: Ca²⁺ release triggers activation of mitotic factors (PKC, cdk2/cdk1 and caspase 3) for NE disintegration by local lamin B depolymerization. No soluble cytosolic factors needed in permeabilized cells (Porwal et al., 2013)

CPV failed to infect cells preloaded with hepatitis B capsids by microinjection (Porwal et al., 2013)

Dependo‐parvovirus

AAV2: Capsid acidification (pH 5.2) and Ca²⁺ release was required for NE disruption (Porwal et al., 2013)

AAV2: Three NLS‐like motifs in VP1 and VP2 essential for infection (Johnson et al., 2010).

Three PDZ‐motifs on VP1u essential for nuclear entry and infection (Popa‐Wagner et al., 2012).

Labeled capsids pass‐through NPC, no evidence of NE disintegration: (Kelich et al., 2015)

rAAV2: Interaction with importin β with or without interaction with importin α (Nicolson & Samulski, 2014)

AAV2 coprecipitates with Nup358, Nup153 and Nup62 (Porwal et al., 2013)

NEBD limited to microinjected AAV2 capsid exposed to pH 5.2 (Porwal et al., 2013)

NE invagination showed by EM (Cohen et al., 2006; Cohen & Panté, 2005)