Acta Virologica Vol.54, No.3, p.197-203, 2010

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ISSN 0001-723X
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Acta Virologica Vol.54, No.3, p.197-203, 2010
Title: Human immunodeficiency virus 1 Vpu protein does not affect the conversion of Influenza A virus hemagglutinin to its low-pH conformation in an acidic trans-Golgi compartment
Author: T. BETÁKOVÁ

Abstract: The 81-aa Vpu protein of Human immunodeficiency virus 1 (HIV-1) is a structural analogue of the M2 protein of Influenza A virus (IAV). Expression of Vpu in Xenopus oocytes has showed that it can form a voltage-activated ion channel permeable to Na+ and K+ ions (Ewart et al., 1996). To investigate whether Vpu has a pH-modulating activity comparable to that of M2, Vpu was co-expressed with the pH-sensitive hemagglutinin (HA) from IAV. The results indicated that Vpu was unable to reduce the acidity of the exocytic pathway and reduce the conversion of the pH-sensitive HA to its low-pH conformation during transport to the cell surface. Despite these findings, we did not exclude the possibility that Vpu formed a weak ion channel with almost pore-like characteristics as was recently suggested.

Keywords: Human immunodeficiency virus 1; ion channel; Influenza A virus; M2 protein; Vpu protein

Year: 2010, Volume: 54, Issue: 3	Page From: 197, Page To: 203
doi:10.4149/av_2010_03_197
Price: 16.80 €

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