The conserved carboxy terminus of the capsid domain of human immunodeficiency virus type 1 gag protein is important for virion assembly and release

Journal of Virology
Daniel MelamedEran Bacharach

Abstract

The retroviral Gag precursor plays an important role in the assembly of virion particles. The capsid (CA) protein of the Gag molecule makes a major contribution to this process. In the crystal structure of the free CA protein of the human immunodeficiency virus type 1 (HIV-1), 11 residues of the C terminus were found to be unstructured, and to date no information exists on the structure of these residues in the context of the Gag precursor molecule. We performed phylogenetic analysis and demonstrated a high degree of conservation of these 11 amino acids. Deletion of this cluster or introduction of various point mutations into these residues resulted in significant impairment of particle infectivity. In this cluster, two putative structural regions were identified, residues that form a hinge region (353-VGGP-356) and those that contribute to an alpha-helix (357-GHKARVL-363). Overall, mutations in these regions resulted in inhibition of virion production, but mutations in the hinge region demonstrated the most significant reduction. Although all the Gag mutants appeared to have normal Gag-Gag and Gag-RNA interactions, the hinge mutants were characterized by abnormal formation of cytoplasmic Gag complexes. Gag proteins with mutati...Continue Reading

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Citations

Nov 10, 2010·The Journal of Physical Chemistry. B·Min GuoPaul Schimmel
May 4, 2011·Proceedings of the National Academy of Sciences of the United States of America·Pengfei FangMin Guo
Aug 19, 2011·AIDS Research and Human Retroviruses·Abdul A Waheed, Eric O Freed
Jan 14, 2005·Bioinformatics·Adi Doron-FaigenboimTal Pupko
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Aug 7, 2013·BMC Evolutionary Biology·Itay MayroseTal Pupko
Feb 15, 2016·Purinergic Signalling·Zhuoran Hou, Jun Cao
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