PuSH - Publikationsserver des Helmholtz Zentrums München

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)
DOI PMC
Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
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.
Altmetric
Weitere Metriken?
Zusatzinfos bearbeiten [➜Einloggen]
Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Korrespondenzautor
Schlagwörter Brain ; Electrophysiological Activity ; Hiv ; K+ Channel ; Nef ; Neurons ; Neuropathy
ISSN (print) / ISBN 0269-9370
e-ISSN 1473-5571
Zeitschrift AIDS
Quellenangaben Band: 5, Heft: 11, Seiten: 1301-1308 Artikelnummer: , Supplement: ,
Verlag Lippincott Williams & Wilkins
Nichtpatentliteratur Publikationen
Begutachtungsstatus Peer reviewed