Interactions of heterologous DNA with polyomavirus major structural protein, VP1
نویسندگان
چکیده
منابع مشابه
Hydroxyproline in the major capsid protein VP1 of polyomavirus.
Amino acid analysis of [3H]proline-labeled polyomavirus major capsid protein VP1 by two-dimensional paper chromatography of the acid-hydrolyzed protein revealed the presence of 3H-labeled hydroxyproline. Addition of the proline analog L-azetidine-2-carboxylic acid to infected mouse kidney cell cultures prevented or greatly reduced hydroxylation of proline in VP1. Immunofluorescence analysis per...
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The major capsid protein of polyomavirus, VP1, was separated into at least four subspecies by isoelectric focusing. One of these subspecies was selectively extracted from purified virions by mild treatment with sodium dodecyl sulfate, leaving a 140S particle enriched in the other three forms. The two most acidic subspecies were labeled in vivo with [32P]phosphate, and these subspecies are among...
متن کاملPersistence and tissue distribution of DNA in normal and immunodeficient mice inoculated with polyomavirus VP1 pseudocapsid complexes or polyomavirus.
Introduction of DNA into normal and immunodeficient mice, alone or in complex with VP1 pseudocapsids, has been compared to DNA transfer by viral infection. Similar to natural infection and in contrast to plasmid alone, VP1 pseudocapsids efficiently introduced DNA, which remained for months in normal mice and possibly longer in B- and T-cell-deficient mice.
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The major structural viral protein, VP1, of the human polyomavirus JC virus (JCV), the causative agent of progressive multifocal leukoencephalopathy (PML), was expressed by using recombinant baculoviruses. Recombinant VP1 formed virus-like particles (VLP) with the typical morphology of empty JCV capsids. Purified VP1 VLP bind to SVG, B, and T cells, as well as to monkey kidney cells. After bind...
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Predicting binding sites of a transcription factor in the genome is an important, but challenging, issue in studying gene regulation. In the past decade, a large number of protein-DNA co-crystallized structures available in the Protein Data Bank have facilitated the understanding of interacting mechanisms between transcription factors and their binding sites. Recent studies have shown that both...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1999
ISSN: 0014-5793
DOI: 10.1016/s0014-5793(99)00003-4