Tissue-spanning redox gradient-dependent assembly of native human papillomavirus type 16 virions.
Papillomavirus capsids are composed of 72 pentamers reinforced through inter- and intrapentameric disulfide bonds. Recent research suggests that virus-like particles and pseudovirions (PsV) can undergo a redox-dependent conformational change involving disulfide interactions. We present here evidence that native virions exploit a tissue-spanning redox gradient that facilitates assembly events in the context of the complete papillomavirus life cycle. DNA encapsidation and infectivity titers are redox dependent in that they can be temporally modulated via treatment of organotypic cultures with oxidized glutathione. These data provide evidence that papillomavirus assembly and maturation is redox-dependent, utilizing multiple steps within both suprabasal and cornified layers.
Conway
Michael J
MJ
Department of Microbiology and Immunology, The Pennsylvania State University College of Medicine, 500 University Dr., Hershey, PA 17033, USA.
Alam
Samina
S
Ryndock
Eric J
EJ
Cruz
Linda
L
Christensen
Neil D
ND
Roden
Richard B S
RB
Meyers
Craig
C
D002213:Capsid / Q000378:metabolism* / Q000502:physiology; D036022:Capsid Proteins / Q000235:genetics / Q000378:metabolism; D002460:Cell Line; D004279:DNA, Viral / Q000235:genetics / Q000378:metabolism; D018274:Electroporation; D005978:Glutathione / Q000378:metabolism / Q000494:pharmacology; D052162:Human papillomavirus 16 / Q000235:genetics / Q000378:metabolism* / Q000472:pathogenicity; D006801:Humans; D015603:Keratinocytes / Q000378:metabolism* / Q000821:virology; D016297:Mutagenesis, Site-Directed; D009924:Organ Culture Techniques; D010084:Oxidation-Reduction; D014771:Virion / Q000235:genetics / Q000378:metabolism* / Q000472:pathogenicity; D019065:Virus Assembly
D036022:Capsid Proteins; D004279:DNA, Viral; D005978:Glutathione