Journal
VIROLOGY
Volume 458, Issue -, Pages 93-105Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2014.04.024
Keywords
HPV; Entry; L2; L1; Cyclophilin; Trans-Golgi network
Categories
Funding
- National Institute of Allergy and Infectious Diseases [R01AI081809]
- National Center for Research Resources [5P20RR018724-10]
- National Institute of General Medical Sciences from the National Institutes of Health [8 P20 GM10343310]
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The Human papillomavirus (HPV) capsid is composed of the major and minor capsid proteins, L1 and L2, respectively. Infectious entry requires a complex series of conformational changes in both proteins that lead to uptake and allow uncoating to occur. During entry, the capsid is disassembled and host cyclophilins dissociate L1 protein from the L2/DNA complex. Herein, we describe a mutant HPV16 L2 protein (HPV16 L2-R302/5A) that traffics pseudogenome to the trans-Golgi network (TGN) but fails to egress. Our data provide further evidence that HPV16 traffics through the TGN and demonstrates that L2 is essential for TGN egress. Furthermore, we show that cyclophilin activity is required for the L2/DNA complex to be transported to the TGN which is accompanied by a reduced L1 protein levels. (C) 2014 Elsevier Inc. All rights reserved.
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