Identification of a membrane-binding domain within the amino-terminal region of human immunodeficiency virus type 1 Gag protein which interacts with acidic phospholipids Journal Article
| Authors: | Zhou, W.; Parent, L. J.; Wills, J. W.; Resh, M. D. |
| Article Title: | Identification of a membrane-binding domain within the amino-terminal region of human immunodeficiency virus type 1 Gag protein which interacts with acidic phospholipids |
| Abstract: | Retroviral Gag proteins are targeted to the plasma membrane, where they play the central role in virion formation. Several studies have suggested that the membrane-binding signal is contained within the amino-terminal matrix sequence; however, the precise location has never been determined for the Gag protein of any retrovirus. In this report, we show that the first 31 residues of human immunodeficiency virus type 1 Gag protein can function independently as a membrane-targeting domain when fused to heterologous proteins. A bipartite membrane-targeting motif was identified, consisting of the myristylated N-terminal 14 amino acids and a highly basic region that binds acidic phospholipids. Replacement of the N-terminal membrane-targeting domain of pp60(v-src) with that of human immunodeficiency virus type 1 Gag elicits efficient membrane binding and a transforming phenotype. Removal of myristate or the basic region results in decreased membrane binding of Gag- Src chimeras in vitro and impaired virion formation by Pr55(gag) in vivo. We propose that the N-terminal Gag sequence functions as a targeting signal to direct interaction with acidic phospholipids on the cytoplasmic leaflet of the plasma membrane. |
| Keywords: | nonhuman; comparative study; protein localization; animal cell; mouse; phenotype; protein binding; structure-activity relationship; cell transformation, neoplastic; chimera; amino acid sequence; molecular sequence data; protein processing, post-translational; amino terminal sequence; messenger rna; immunocytochemistry; cell membrane; cytoplasm; base sequence; tetrahydrofolate dehydrogenase; cell strain 3t3; acids; biological transport; retrovirus; human immunodeficiency virus 1; membrane binding; hiv-1; virus protein; phospholipids; phospholipid; virus assembly; protein precursors; protein lipid interaction; myristic acid; gag protein; virion; gene products, gag; viral genetics; myristic acids; oncogene protein pp60(v-src); human; priority journal; article; cell compartmentation; support, non-u.s. gov't; support, u.s. gov't, p.h.s.; chimeric proteins |
| Journal Title: | Journal of Virology |
| Volume: | 68 |
| Issue: | 4 |
| ISSN: | 0022-538X |
| Publisher: | American Society for Microbiology |
| Date Published: | 1994-04-01 |
| Start Page: | 2556 |
| End Page: | 2569 |
| Language: | English |
| PROVIDER: | scopus |
| PMCID: | PMC236733 |
| PUBMED: | 8139035 |
| DOI/URL: | |
| Notes: | Export Date: 14 January 2019 -- Article -- CODEN: JOVIA C2 -- Source: Scopus |
