Document 0537 DOCN M9460537 TI Complementation of human immunodeficiency virus (HIV-1) gag particle formation. DT 9404 AU Zhoa Y; Jones IM; Hockley DJ; Nermut MV; Roy P; Department of Biochemistry, University of Oxford. SO Virology. 1994 Mar;199(2):403-8. Unique Identifier : AIDSLINE MED/94167874 AB The human immunodeficiency virus gag precursor protein Pr55Gag exhibits the ability of particle assembly when expressed using recombinant baculoviruses. In order to delineate the sequences required for particle formation, two mutants of Gag (D1 and D2) were constructed in which 10 amino acids within the CA domain were deleted. Both mutants yielded stable high levels of Gag antigen following expression in Spodoptera frugiperda insect cells. Electron microscopy of sections through infected cells revealed that neither mutant was able to assemble particles although targeting of the protein to the plasma membrane still occurred. The Gag antigen that accumulated beneath the plasma membrane exhibited distinctive morphologies when compared to each other and to parental (Pr46Gag) particles. Particle assembly was rescued when S. frugiperda cells were coinfected with both AcD1 and AcD2 viruses, or with AcD1 and a carboxyl-terminal deletion of Gag (Pr41.5) which was previously shown not to form particles (J.B.M., D.J. Hockley, M.V. Nermot, and I.M. Jones, 1992, J. Gen. Virol. 73, 3079-3086). The genetic complementation of Gag-driven assembly is discussed. DE Amino Acid Sequence Animal Antigens, Viral/*BIOSYNTHESIS Baculoviridae Capsid/GENETICS/*METABOLISM Gene Expression/PHYSIOLOGY Gene Products, gag/GENETICS/*METABOLISM HIV-1/GENETICS/*METABOLISM Molecular Sequence Data Moths Recombinant Proteins/BIOSYNTHESIS 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).