Publications by authors named "D Pim"
Human papillomavirus (HPV) E7 plays a major role in HPV-induced malignancy, perturbing cell cycle regulation, and driving cell proliferation. Major targets of cancer-causing HPV E7 proteins are the pRB family of tumor suppressors, which E7 targets for proteasome-mediated degradation and whose interaction is promoted through an acidic patch, downstream of the LXCXE motif in E7, that is subject to phosphorylation by casein kinase II (CKII). In this study we show that HPV-16 E7 targets the AP2-complex, which plays a critical role in cargo recognition in clathrin-mediated endocytosis.
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- HPV infection involves complex interactions between viral particles and cellular proteins, particularly the L1 and L2 structural proteins that facilitate viral entry and intracellular trafficking of viral DNA.
- Proteomic studies identified CCT proteins, specifically CCT3, as novel interaction partners of HPV-16 L2, essential for effective viral infection and capsid uncoating.
- The research highlights the critical role of the CCT chaperonin complex in HPV's infectious process, showing that disrupting CCT components significantly impairs viral entry and processing within host cells.
Article Synopsis
- - Previous research established a link between HPV's L2 minor capsid protein and sorting nexins 17 and 27 (SNX17 and SNX27) during the virus's infection process.
- - This study reveals that both the retromer and retriever complexes are crucial for HPV infection, with L2 interacting with components of each complex and these proteins being imperative for successful infection.
- - It was found that while SNX17 is important for recruiting retromer, it does not aid in retriever recruitment, which more likely involves a direct connection between L2 and the retriever's C16orf62 subunit, highlighting the complex's role in HPV infection.
Previous studies have shown that the endoplasmic reticulum (ER)-anchored protein VAP is strictly required by human papillomavirus type 16 (HPV-16) for successful infectious entry. Entry appeared to be mediated in part through the induction of endosomal tubulation and subsequent transport of the virion to the trans-Golgi network (TGN). In this study, we were interested in investigating whether this mechanism of infectious entry is conserved across multiple Papillomavirus types.
View Article and Find Full Text PDFTo infect mammalian cells, all infectious viruses must cross a common set of biophysical membrane barriers to gain access to the cell. The virus capsid proteins attach to a host cell, become endocytosed, and traffic the viral genome to sites of replication. To do this they must interact with the membrane-confined organelles that control endocytosis, endosomal sorting, processing, and degradation of biological molecules.
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