PuSH - Publikationsserver des Helmholtz Zentrums München: HIV-1 Nef protein exhibits structural and functional similarity to scorpion peptides interacting with K+ channels.

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Werner, T. ; Ferroni, S.* ; Særmark, T.* ; Brack-Werner, R. ; Banati, R.B.* ; Mager, R.* ; Steinaa, L.* ; Kreutzberg, G.W.* ; Erfle, V.F.

HIV-1 Nef protein exhibits structural and functional similarity to scorpion peptides interacting with K+ channels.

Aids 5, 1301-1308 (1991)

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Open Access Gold möglich sobald Verlagsversion bei der ZB eingereicht worden ist.

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The persistent infection of human glial cells with HIV-1 is characterized by prominent expression of the Nef protein. In order to evaluate the possible role of Nef in the development of HIV-1-associated neurological disorders, we compared Nef with known neuroactive proteins. We found that HIV Nef shares sequence and structural features with scorpion peptides known to interact with K+ channels. Sequence similarity encompasses two distinct regions of scorpion peptides. Based on crystallography data, both regions in scorpion peptides cooperate in forming a common domain stabilized by ion pairs between charged amino-acid residues. Recombinant Nef protein, as well as a synthetic part of a scorpion channel active peptide (M10), reversibly increased the total K+ current of chick dorsal root ganglions in patch-clamp experiments without killing the cells. These results indicate that a region conserved in HIV Nef and scorpion peptides concurs in both structure and electrophysiological activity and suggest that Nef, like scorpion peptides, may affect neuronal cell function.

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