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Covalent bonded Gag multimers in human immunodeficiency virus type‐1 particles
Author(s) -
Kitagawa Yoshinori,
MaedaSato Masae,
Tanaka Keiko,
Tobiume Minoru,
Sawa Hirofumi,
Hasegawa Hideki,
Kojima Asato,
Hall William W.,
Kurata Takeshi,
Sata Tetsutaro,
Takahashi Hidehiro
Publication year - 2009
Publication title -
microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0385-5600
DOI - 10.1111/j.1348-0421.2009.00164.x
Subject(s) - biology , covalent bond , virology , human immunodeficiency virus (hiv) , chemistry , organic chemistry
The oligomerization of HIV‐1 Gag and Gag‐Pol proteins, which are assembled at the plasma membrane, leads to viral budding. The budding generally places the viral components under non‐reducing conditions. Here the effects of non‐reducing conditions on Gag structures and viral RNA protection were examined. Using different reducing conditions and SDS‐PAGE, it was shown that oligomerized Gag possesses intermolecular covalent bonds under non‐reducing conditions. In addition, it was demonstrated that the mature viral core contains a large amount of covalent bonded Gag multimers, as does the immature core. Viral genomic RNA becomes sensitive to ribonuclease in reducing conditions. These results suggest that, under non‐reducing conditions, covalent bonded Gag multimers are formed within the viral particles and play a role in protection of the viral genome.