HIV type 2 Vpx interaction with Gag and incorporation into virus-like particles.
The domain of HIV-2 Vpx previously shown to be important for virion incorporation has been mapped to residues 73--89. Mutational analysis of this domain was employed to further define the sequences important for incorporation into virus-like particles, using a vaccinia virus expression system. Deletion of residues 73--89 did not abrogate Vpx packaging, but substitution with alanines markedly reduced incorporation into virus-like particles. Moreover, alanine substitution also disrupted Vpx interaction with Gag, as demonstrated with glutathione S-transferase fusion proteins and the yeast two-hybrid system.
Jin
L
L
Department of Medicine, Washington University School of Medicine, St. Louis, Missouri 63110, USA.
Zhou
Y
Y
Ratner
L
L
D000409:Alanine / Q000235:genetics; D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D001345:Autoradiography; D002460:Cell Line; D004591:Electrophoresis, Polyacrylamide Gel; D015685:Fusion Proteins, gag-pol / Q000378:metabolism; D017353:Gene Deletion; D015683:Gene Products, gag / Q000032:analysis / Q000378:metabolism*; D005982:Glutathione Transferase / Q000378:metabolism; D015498:HIV-2 / Q000378:metabolism*; D006801:Humans; D015151:Immunoblotting; D008969:Molecular Sequence Data; D009154:Mutation; D054334:Viral Regulatory and Accessory Proteins / Q000032:analysis / Q000235:genetics / Q000378:metabolism*
D015685:Fusion Proteins, gag-pol; D015683:Gene Products, gag; C074286:VPX protein, Human immunodeficiency virus 2; D054334:Viral Regulatory and Accessory Proteins; D005982:Glutathione Transferase; D000409:Alanine