Formation and release of virus-like particles by HIV-1 matrix protein

Wang, J J; Horton, Robert A.; Varthakavi, Vasundhara; Spearman, Paul; Ratner, Lee

doi:10.1097/00002030-199902040-00018

Cited by 27 publications

(15 citation statements)

References 13 publications

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“…We identified HIV‐1 RNA sequences which are efficiently incorporated in exosomes. Exosomes and HIV‐1 are structurally quite similar vesicles, being the density of exosomes 1.13 to 1.21 g ml −1 (Thery et al ., ), while that of HIV‐1 is 1.16 to 1.18 g ml −1 (Wang et al ., ). Virions are slightly larger than exosomes, i.e.…”

Section: Discussionmentioning

confidence: 97%

Sequences within RNA coding for HIV-1 Gag p17 are efficiently targeted to exosomes

Columba-Cabezas

Federico

2012

Cellular Microbiology

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Section: Discussionmentioning

confidence: 97%

Sequences within RNA coding for HIV-1 Gag p17 are efficiently targeted to exosomes

Columba-Cabezas

Federico

2012

Cellular Microbiology

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“…A number of studies have shown that recombinant or naturally expressed HIV-1 MA can form trimers (Hill et al, 1996;Massiah et al, 1994) or hexamers (Alfadhli et al, 2007), suggesting that MA possesses a self-interaction property in addition to playing a role in RNA packaging. It has also been demonstrated that either HIV or SIV MA expression alone is capable of producing VLPs (Gonzalez et al, 1993;Wang et al, 1999). These findings suggest that MA is somewhat similar to NC in its self-association characteristic and the possibility that it promotes Gag multimerization.…”

Section: Contents Lists Available At Sciencedirectmentioning

confidence: 89%

HIV-1 matrix protein repositioning in nucleocapsid region fails to confer virus-like particle assembly

Chang

Wang

et al. 2008

Virology

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The HIV-1 matrix (MA) protein is similar to nucleocapsid (NC) proteins in its propensity for self-interaction and association with RNA. Here we report on our finding that replacing MA with NC results in the production of wild type (wt)-level RNA and virus-like particles (VLPs). In contrast, constructs containing MA as a substitute for NC are markedly defective in VLP production and form virions with lower densities than wt, even though their RNA content is over 50% that of wt level. We also noted that a DeltaMN mutant lacking both MA and NC produces a relatively higher amount of VLPs than those in which MA was substituted for NC. Although DeltaMN contains approximately 30% the RNA of wt, it still exhibits virion densities equal (or very similar) to those of wt. The data suggest that neither NC nor RNA are major virion density determinants. Furthermore, we noted that NC(ZIP)--a NC replacement with a leucine zipper dimerization motif--produces VLPs as efficiently as wt. However, the markedly reduced assembly efficiency of NC(ZIP) is associated with the formation of VLPs with densities slightly lower than those of wt following MA removal, suggesting that (a) MA is required to help the inserted leucine zipper motif perform efficient Gag multimerization, and (b) MA plays a role in the virus assembly process.

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“…It has been reported that p17(MA) as well as p41 (MA-CA) Gag proteins can form trimers in a baculovirus overexpression system (35), and SIV MA is reportedly capable of forming VLPs (18,19). HIV-1 MA has also been observed by some (56) but not by others (18) to form low-density particles. We find a low level of pelletable material produced by expression of MA.…”

Section: Discussionmentioning

confidence: 99%

Relationship between Human Immunodeficiency Virus Type 1 Gag Multimerization and Membrane Binding

Ono

Demirov

Freed

2000

J Virol

104

106

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The human immunodeficiency virus type 1 (HIV-1) Gag precursor, Pr55Gag , is necessary and sufficient for the assembly and release of viruslike particles. Binding of Gag to membrane and Gag multimerization are both essential steps in virus assembly, yet the domains responsible for these events have not been fully defined. In addition, the relationship between membrane binding and Gag-Gag interaction remains to be elucidated. To investigate these issues, we analyzed, in vivo, the membrane-binding and assembly properties of a series of C-terminally truncated Gag mutants. Pr55Gag was truncated at the C terminus of matrix (MAstop), between the N-and C-terminal domains of capsid (CA146stop), at the C terminus of capsid (p41stop), at the C terminus of p2 (p43stop), and after the N-terminal 35 amino acids of nucleocapsid (NC35stop). The ability of these truncated Gag molecules to assemble and release viruslike particles and their capacity to copackage into particles when coexpressed with full-length Gag were determined. We demonstrate that the amount of truncated Gag incorporated into particles is incrementally increased by extension from CA146 to NC35, suggesting that multiple sites in this region are involved in Gag multimerization. Using membrane flotation centrifugation, we observe that MA shows significantly reduced membrane binding relative to full-length Gag but that CA146 displays steady-state membrane-binding properties comparable to those of Pr55Gag . The finding that the CA146 mutant, which contains only matrix and the N-terminal domain of capsid, exhibits levels of steady-state membrane binding equivalent to those of full-length Gag indicates that strong Gag-Gag interaction domains are not required for the efficient binding of HIV-1 Gag to membrane.

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Formation and release of virus-like particles by HIV-1 matrix protein

Cited by 27 publications

References 13 publications

Sequences within RNA coding for HIV-1 Gag p17 are efficiently targeted to exosomes

Sequences within RNA coding for HIV-1 Gag p17 are efficiently targeted to exosomes

HIV-1 matrix protein repositioning in nucleocapsid region fails to confer virus-like particle assembly

Relationship between Human Immunodeficiency Virus Type 1 Gag Multimerization and Membrane Binding

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