title: HIV-1 matrix domain removal ameliorates virus assembly and processing defects incurred by positive nucleocapsid charge elimination.
abstract: Human immunodeficiency virus type 1 nucleocapsid (NC) basic residues presumably contribute to virus assembly via RNA, which serves as a scaffold for Gag-Gag interaction during particle assembly. To determine whether NC basic residues play a role in Gag cleavage (thereby impacting virus assembly), Gag processing efficiency and virus particle production were analyzed for an HIV-1 mutant NC15A, with alanine serving as a substitute for all NC basic residues. Results indicate that NC15A significantly impaired virus maturation in addition to significantly affecting Gag membrane binding and assembly. Interestingly, removal of the matrix (MA) central globular domain ameliorated the NC15A assembly and processing defects, likely through enhancement of Gag multimerization and membrane binding capacities.
authors.affiliation: Department of Medical Research, Taipei Veterans General Hospital, Taipei, Taiwan ; Institute of Public Health, National Yang-Ming University School of Medicine, Taipei, Taiwan.
authors.forename: Li-Jung
authors.initials: LJ
authors.lastname: Ko
authors.affiliation: Institute of Clinical Medicine, National Yang-Ming University School of Medicine, Taipei, Taiwan.
authors.forename: Fu-Hsien
authors.initials: FH
authors.lastname: Yu
authors.affiliation: Department of Medical Research, Taipei Veterans General Hospital, Taipei, Taiwan.
authors.forename: Kuo-Jung
authors.initials: KJ
authors.lastname: Huang
authors.affiliation: Department of Medical Research, Taipei Veterans General Hospital, Taipei, Taiwan ; Institute of Clinical Medicine, National Yang-Ming University School of Medicine, Taipei, Taiwan.
authors.forename: Chin-Tien
authors.initials: CT
authors.lastname: Wang
keywords: CA, capsid; Gag cleavage; HIV-1; MA, matrix; Matrix; Membrane association; NC, nucleocapsid; Nucleocapsid; PR, viral protease; VLP, virus-like particle; Virus assembly