       Document 0792
 DOCN  M9590792
 TI    Membrane permeabilization by different regions of the human
       immunodeficiency virus type 1 transmembrane glycoprotein gp41.
 DT    9509
 AU    Arroyo J; Boceta M; Gonzalez ME; Michel M; Carrasco L; Centro Nacional
       de Biotecnologia, Universidad Autonoma, Madrid,; Spain.
 SO    J Virol. 1995 Jul;69(7):4095-102. Unique Identifier : AIDSLINE
       MED/95287459
 AB    The transmembrane glycoprotein (gp41) of human immunodeficiency virus
       type 1 (HIV-1) has been implicated in the cytopathology observed during
       HIV infection. The first amino acids located at the amino terminus are
       involved in membrane fusion and syncytium formation, while sequences
       located at the carboxy terminus have been predicted to interact with
       membranes and modify membrane permeability. The HIV-1 gp41 gene has been
       cloned and expressed in Escherichia coli cells by using pET vectors to
       analyze changes in membrane permeability produced by this protein. This
       system is well suited for expressing toxic genes in an inducible manner
       and for analyzing the function of proteins that modify membrane
       permeability. gp41 enhances the permeability of the bacterial membrane
       to hygromycin B despite the low level of expression of this protein. To
       localize the regions of gp41 responsible for these effects, a number of
       fragments spanning different portions of gp41 were inducibly expressed
       in E. coli. Two regions of gp41 were shown to increase membrane
       permeability: one located at the carboxy terminus, where two highly
       amphipathic helices have been predicted, and another one corresponding
       to the membrane-spanning domain. Expression of the central region of
       gp41 comprising this domain was highly lytic for E. coli cells and
       increased membrane permeability to a number of compounds. These findings
       are discussed in the light of HIV-induced cytopathology and gp41
       structure.
 DE    Base Sequence  Cell Membrane Permeability/*DRUG EFFECTS  Escherichia
       coli/GENETICS  Flow Cytometry  HIV Envelope Protein gp41/*PHARMACOLOGY
       HIV-1/*PHYSIOLOGY  Molecular Sequence Data  Peptide
       Fragments/*PHARMACOLOGY  Recombinant Proteins/PHARMACOLOGY  Support,
       Non-U.S. Gov't  JOURNAL ARTICLE

       SOURCE: National Library of Medicine.  NOTICE: This material may be
       protected by Copyright Law (Title 17, U.S.Code).

