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Virus-Cell Interactions

Cyclophilins Facilitate Dissociation of the Human Papillomavirus Type 16 Capsid Protein L1 from the L2/DNA Complex following Virus Entry

Malgorzata Bienkowska-Haba, Carlyn Williams, Seong Man Kim, Robert L. Garcea, Martin Sapp
Malgorzata Bienkowska-Haba
aDepartment of Microbiology and Immunology, LSU Health Shreveport, Shreveport, Louisiana, USA
bCenter for Molecular Tumor Virology, LSU Health Shreveport, Shreveport, Louisiana, USA
cFeist-Weiller Cancer Center, LSU Health Shreveport, Shreveport, Louisiana, USA
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Carlyn Williams
dDepartment of Molecular, Cellular and Developmental Biology, University of Colorado, Boulder, Colorado, USA
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Seong Man Kim
aDepartment of Microbiology and Immunology, LSU Health Shreveport, Shreveport, Louisiana, USA
bCenter for Molecular Tumor Virology, LSU Health Shreveport, Shreveport, Louisiana, USA
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Robert L. Garcea
dDepartment of Molecular, Cellular and Developmental Biology, University of Colorado, Boulder, Colorado, USA
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Martin Sapp
aDepartment of Microbiology and Immunology, LSU Health Shreveport, Shreveport, Louisiana, USA
bCenter for Molecular Tumor Virology, LSU Health Shreveport, Shreveport, Louisiana, USA
cFeist-Weiller Cancer Center, LSU Health Shreveport, Shreveport, Louisiana, USA
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DOI: 10.1128/JVI.00980-12
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ABSTRACT

Human papillomaviruses (HPV) are composed of the major and minor capsid proteins, L1 and L2, that encapsidate a chromatinized, circular double-stranded DNA genome. At the outset of infection, the interaction of HPV type 16 (HPV16) (pseudo)virions with heparan sulfate proteoglycans triggers a conformational change in L2 that is facilitated by the host cell chaperone cyclophilin B (CyPB). This conformational change results in exposure of the L2 N terminus, which is required for infectious internalization. Following internalization, L2 facilitates egress of the viral genome from acidified endosomes, and the L2/DNA complex accumulates at PML nuclear bodies. We recently described a mutant virus that bypasses the requirement for cell surface CyPB but remains sensitive to cyclosporine for infection, indicating an additional role for CyP following endocytic uptake of virions. We now report that the L1 protein dissociates from the L2/DNA complex following infectious internalization. Inhibition and small interfering RNA (siRNA)-mediated knockdown of CyPs blocked dissociation of L1 from the L2/DNA complex. In vitro, purified CyPs facilitated the dissociation of L1 pentamers from recombinant HPV11 L1/L2 complexes in a pH-dependent manner. Furthermore, CyPs released L1 capsomeres from partially disassembled HPV16 pseudovirions at slightly acidic pH. Taken together, these data suggest that CyPs mediate the dissociation of HPV L1 and L2 capsid proteins following acidification of endocytic vesicles.

  • Copyright © 2012, American Society for Microbiology. All Rights Reserved.
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Cyclophilins Facilitate Dissociation of the Human Papillomavirus Type 16 Capsid Protein L1 from the L2/DNA Complex following Virus Entry
Malgorzata Bienkowska-Haba, Carlyn Williams, Seong Man Kim, Robert L. Garcea, Martin Sapp
Journal of Virology Aug 2012, 86 (18) 9875-9887; DOI: 10.1128/JVI.00980-12

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Cyclophilins Facilitate Dissociation of the Human Papillomavirus Type 16 Capsid Protein L1 from the L2/DNA Complex following Virus Entry
Malgorzata Bienkowska-Haba, Carlyn Williams, Seong Man Kim, Robert L. Garcea, Martin Sapp
Journal of Virology Aug 2012, 86 (18) 9875-9887; DOI: 10.1128/JVI.00980-12
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