Abstract：
:Cell-penetrating peptides (CPPs) are short protein segments that can transport cargos into cells. Although CPPs are widely studied as potential drug delivery tools, their role in normal cell physiology is poorly understood. Early during infection, the L2 capsid protein of human papillomaviruses binds retromer, a cytoplasmic trafficking factor required for delivery of the incoming non-enveloped virus into the retrograde transport pathway. Here, we show that the C terminus of HPV L2 proteins contains a conserved cationic CPP that drives passage of a segment of the L2 protein through the endosomal membrane into the cytoplasm, where it binds retromer, thereby sorting the virus into the retrograde pathway for transport to the trans-Golgi network. These experiments define the cell-autonomous biological role of a CPP in its natural context and reveal how a luminal viral protein engages an essential cytoplasmic entry factor.
journal_name
Celljournal_title
Cellauthors
Zhang P,Monteiro da Silva G,Deatherage C,Burd C,DiMaio Ddoi
10.1016/j.cell.2018.07.031subject
Has Abstractpub_date
2018-09-06 00:00:00pages
1465-1476.e13issue
6eissn
0092-8674issn
1097-4172pii
S0092-8674(18)30958-9journal_volume
174pub_type
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