Membrane voltage of vpu (Viral Protein Unique)

Range -80 mV
Organism HIV
Reference Fischer WB, Sansom MS. Viral ion channels: structure and function. Biochim Biophys Acta. 2002 Mar 19 1561(1):27-45. DOI: 10.1016/S0304-4157(01)00009-0 p.34 left column top paragraphPubMed ID11988179
Method "Channel activity of Vpu is proved by reconstitution of the whole protein into planar lipid bilayers [ref 76]. For this study, Vpu is transcribed in E. coli and purified. Reconstitution has been done either from a detergent solution or from a suspension of Vpu-containing vesicles. It could be shown that Vpu channel activity is more in preference of monovalent cations than anions. Currents of up to 2 pA (-80 mV) in a 0.5/0.05 M NaCl solution have been recorded. Reconstitution into a lipid membrane of a synthetic analogous to the TM [transmembrane] region of Vpu shows channel activity of up to 60 pS with a preference to monovalent cations [ref 29]. A peptide of the same length with a scrambled sequence does not exhibit any channel activity."
Entered by Uri M
ID 110623