CYTOPATHIC EFFECT IN HUMAN PAPILLOMAVIRUS TYPE-1 INDUCED INCLUSION WARTS - IN-VITRO ANALYSIS OF THE CONTRIBUTION OF 2 FORMS OF THE VIRAL E4 PROTEIN

被引:24
作者
ROGELGAILLARD, C [1 ]
PEHAUARNAUDET, G [1 ]
BREITBURD, F [1 ]
ORTH, G [1 ]
机构
[1] INST PASTEUR, INSERM, U190, UNITE PAPILLOMAVIRUS, F-75724 PARIS 15, FRANCE
关键词
INTERMEDIATE FILAMENT-ASSOCIATED PROTEIN; CYTOKERATIN; MYRMECIA WART; IMMUNOELECTRON MICROSCOPY;
D O I
10.1111/1523-1747.ep12371705
中图分类号
R75 [皮肤病学与性病学];
学科分类号
100206 ;
摘要
Myrmecia warts induced by human papillomavirus type 1 (HPV1) are characterized by abundant eosinophilic inclusions associated with HPV1 E4 gene products. The major HPV1 E4 proteins are a 17-kilodalton (kDa) E1-E4 fusion protein and a 16-kDa species lacking the five El aminoacids and a few E4 residues. To study the contribution of E4 proteins to the formation of myrmecia inclusions, we used a previously designed transient expression system in the rabbit VX2-R keratinocyte line. We find that the E1-E4 and an E4 protein without the E1 residues (E4-3200) form eosinophilic inclusions. Ultrastructural and immunoelectron microscopic studies show that the electron-dense, keratohyalin-like myrmecia inclusions are recognized by anti-E4 antibodies. They are associated with tonofilament bundles at their periphery in the cytoplasm or free of filaments in the nucleus. The E1-E4 inclusions formed in vitro are also homogeneously electron dense, and are usually associated with tonofilaments at their periphery in the cytoplasm and free of filaments in the nucleus. The E4-3200 inclusions are exclusively cytoplasmic and heterogeneously electron dense, with a fibrillar structure made of entangled 10-nm filaments. The expression of either protein in VX2-R cells does not result in the collapse of the cytokeratin network, as shown by immunofluorescence double-labeling experiments. This is in contrast to data reported for the HPV16 E1-E4 protein. Our findings indicate that the E1-E4 protein by itself accounts for the formation of myrmecia inclusions, and suggest that the five N-terminal E1 aminoacids play a major role in the interaction of E4 proteins with intermediate filaments.
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收藏
页码:843 / 851
页数:9
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