A Ran-binding protein facilitates nuclear import of human papillomavirus type 16

Human papillomaviruses (HPVs) utilize an atypical mode of nuclear import during cell entry. Residing in the Golgi apparatus until mitosis onset, a subviral complex composed of the minor capsid protein L2 and viral DNA (L2/vDNA) is imported into the nucleus after nuclear envelope breakdown by associa...

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Published inPLoS pathogens Vol. 17; no. 5; p. e1009580
Main Authors Lai, Kun-Yi, Rizzato, Matteo, Aydin, Inci, Villalonga-Planells, Ruth, Drexler, Hannes C A, Schelhaas, Mario
Format Journal Article
LanguageEnglish
Published United States Public Library of Science 11.05.2021
Public Library of Science (PLoS)
Subjects
Binding proteins
Biology and life sciences
Candidates
Cell cycle
Cellular precipitates
Chromatin
Chromosomes
Diagnosis
Gene expression
Genomes
Health aspects
Human papillomavirus
Imports
Infections
Infectivity
Localization
Mass spectrometry
Mass spectroscopy
Medicine and Health Sciences
Mitosis
Nuclear transport
Papillomavirus infections
Protein transport
Proteins
Ran-binding protein
Research and analysis methods
Risk factors
Roles
Scientific imaging
Spectroscopy
Germany
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Summary:Human papillomaviruses (HPVs) utilize an atypical mode of nuclear import during cell entry. Residing in the Golgi apparatus until mitosis onset, a subviral complex composed of the minor capsid protein L2 and viral DNA (L2/vDNA) is imported into the nucleus after nuclear envelope breakdown by associating with mitotic chromatin. In this complex, L2 plays a crucial role in the interactions with cellular factors that enable delivery and ultimately tethering of the viral genome to mitotic chromatin. To date, the cellular proteins facilitating these steps remain unknown. Here, we addressed which cellular proteins may be required for this process. Using label-free mass spectrometry, biochemical assays, microscopy, and functional virological assays, we discovered that L2 engages a hitherto unknown protein complex of Ran-binding protein 10 (RanBP10), karyopherin alpha2 (KPNA2), and dynein light chain DYNLT3 to facilitate transport towards mitotic chromatin. Thus, our study not only identifies novel cellular interactors and mechanism that facilitate a poorly understood step in HPV entry, but also a novel cellular transport complex.
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The authors have declared that no competing interests exist.
ISSN:1553-7374
1553-7366
1553-7374
DOI:10.1371/journal.ppat.1009580