作者: Stephen DiGiuseppe , Timothy R. Keiffer , Malgorzata Bienkowska-Haba , Wioleta Luszczek , Lucile G. M. Guion
DOI: 10.1128/JVI.01588-15
关键词:
摘要: The human papillomavirus (HPV) capsid is composed of the major protein L1 and minor L2. During entry, HPV undergoes numerous conformational changes that result in endosomal uptake subsequent trafficking L2 complex with viral DNA to trans-Golgi network. To facilitate this transport, harbors a number putative motifs that, if capable direct interaction, would interact cytosolic host cell factors. These data imply portion becomes during infection. Using low concentration digitonin selectively permeabilize plasma membrane infected cells, we mapped topography We observed epitopes within amino acid residues 64 81 163 170 C-terminal tag HPV16 are exposed on side intracellular membranes, whereas an epitope 20 38, which upstream transmembrane region, luminal. Corroborating these findings, also found sensitive trypsin digestion demonstrate majority accessible membranes order factors vesicular trafficking. IMPORTANCE In complete infectious nonenveloped viruses have pass cellular membranes. This often achieved through associating or integrating into membrane. Here, determine endocytic compartment, suggesting short luminal facing for interaction transport