(Q39326353)

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Essential role of the unordered VP2 n-terminal domain of the parvovirus MVM capsid in nuclear assembly and endosomal enlargement of the virion fivefold channel for cell entry.

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6 February 2020

Essential role of the unordered VP2 n-terminal domain of the parvovirus MVM capsid in nuclear assembly and endosomal enlargement of the virion fivefold channel for cell entry (English)

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6 February 2020

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6 February 2020

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Cristina Sánchez-Martínez

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6 February 2020

Miles Carroll

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6 February 2020

Jean Rommelaere

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6 February 2020

José M Almendral

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23 June 2012

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6 February 2020

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6 February 2020

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6 February 2020

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6 February 2020

Functional implications of the structure of the murine parvovirus, minute virus of mice

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A conserved leucine that constricts the pore through the capsid fivefold cylinder plays a central role in parvoviral infection

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The VP1 capsid protein of adeno-associated virus type 2 is carrying a phospholipase A2 domain required for virus infectivity

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Structural determinants of tissue tropism and in vivo pathogenicity for the parvovirus minute virus of mice

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The infectivity and lytic activity of minute virus of mice wild-type and derived vector particles are strikingly different.

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A beta-stranded motif drives capsid protein oligomers of the parvovirus minute virus of mice into the nucleus for viral assembly

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Complementary roles of multiple nuclear targeting signals in the capsid proteins of the parvovirus minute virus of mice during assembly and onset of infection

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Low pH-dependent endosomal processing of the incoming parvovirus minute virus of mice virion leads to externalization of the VP1 N-terminal sequence (N-VP1), N-VP2 cleavage, and uncoating of the full-length genome

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The minor capsid protein VP1 of the autonomous parvovirus minute virus of mice is dispensable for encapsidation of progeny single-stranded DNA but is required for infectivity.

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