Differential membrane binding of the human immunodeficiency virus type 1 matrix protein
Open accessAbstract
The human immunodeficiency virus type 1 matrix protein (p17MA) plays a central role at both the early and late stages of the virus life cycle. During viral assembly, the p17MA domain of Pr55gag promotes membrane association, which is essential for the formation of viral particles. When viral infection occurs, the mature p17MA dissociates from the plasma membrane and participates in the nuclear targeting process. Thus, p17MA contains a reversible membrane binding signal to govern its differential subcellular localization and biological functions. We previously identified a membrane binding signal within the amino-terminal 31 amino acids of the matrix domain of human immunodeficiency virus type 1 Gag, consisting of myristate and a highly basic region (W. Zhou, L. J. Parent, J. W. Wills, and M. D. Resh, J. Virol. 68:2556-2569, 1994). Here we show that exposure of this membrane binding signal is regulated in different Gag protein contexts. Within full-length Pr55gag, the membrane targeting signal is exposed and can direct Pr55gag as well as heterologous proteins to the plasma membrane. However, in the context of p17MA alone, this signal is hidden and unable to confer plasma membrane binding. To investigate the molecular mechanism for regulation of membrane binding, a series of deletions within p17MA was generated by sequentially removing alpha-helical regions defined by the nuclear magnetic resonance structure. Removal of the last alpha helix (amino acids 97 to 109) of p17MA was associated with enhancement of binding to biological membranes in vitro and in vivo. Liposome binding experiments indicated that the C-terminal region of p17MA exerts a negative effect on the N-terminal MA membrane targeting domain by sequestering the myristate signal. We propose that mature p17MA adopts a conformation different from that of the p17MA domain within Pr55gag and present evidence to support this hypothesis. It is likely that such a conformational change results in an N-terminal myristyl switch which governs differential membrane binding.
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InfluentialRole of HIV-1 Gag domains in viral assembly
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“According to this model, the myristate moiety is highly exposed in the context of Pr55 but is sequestered within p17(MA) following proteolytic cleavage of the precursor by PR (21, 48, 63).”
BackgroundTritel, M., & Resh, M. D. (2000) · Journal of Virology · doi:10.1128/jvi.74.13.5845-5855.2000 · Cited by 113 · see citing works
“p65-Gag-green fluorescent protein (GFP) chimeras have been previously described (36).”
BackgroundSelf-citationSandefur, S. L., Smith, R. M., Varthakavi, V., & Spearman, P. W. (2000) · Journal of Virology · doi:10.1128/jvi.74.16.7238-7249.2000 · Cited by 113 · see citing works
“Several groups have now provided supporting data for the presence of the myristyl switch within MA (25, 26, 30, 43).”
BackgroundMembrane association induces a conformational change in the Ebola virus matrix protein
Scianimanico, S., Schoehn, G., Timmins, J., Ruigrok, R. W. H., Klenk, H., & Weissenhorn, W. (2000) · The EMBO Journal · doi:10.1093/emboj/19.24.6732 · Cited by 110 · see citing works
The Role of Lipids in Retrovirus Replication
Waheed, A. A., & Freed, E. O. (2010) · Viruses · doi:10.3390/v2051146 · Cited by 112 · see citing works
“Mutating basic residues in the MA domain mistargets Gag, such that it associates with internal compartments rather than the plasma membrane [122,163–169].”
Point Mutations in the HIV-1 Matrix Protein Turn Off the Myristyl Switch
Saad, J. S., Loeliger, E., Luncsford, P. J., Liriano, M., Tai, J., Kim, A., Miller, J. L., Joshi, A., Freed, E. O., & Summers, M. F. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.11.068 · Cited by 111 · see citing works
Larson, D. R., Ma, Y. M., Vogt, V. M., & Webb, W. W. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200303200 · Cited by 109 · see citing works
“Second, HIV-1 MA is reported to bind to membranes in vitro less efficiently than full-length Gag, suggesting a cooperative role for Gag multimerization in this process (Zhou and Resh, 1996; Sandefur et al., 1998).”
BackgroundOno, A., Waheed, A. A., & Freed, E. O. (2006) · Virology · doi:10.1016/j.virol.2006.10.011 · Cited by 106 · see citing works
“In the WT context, Gag multimerization likely promotes the exposure of the myristate moiety (Hermida-Matsumoto and Resh, 1999;Perez-Caballero et al., 2004;Sandefur et al., 2000;Sandefur et al., 1998;Spearman et al., 1997;Tang et al., 2004;Zhou and Resh, 1996).”
BackgroundA myristoyl switch regulates membrane binding of HIV-1 Gag
Resh, M. D. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308043101 · Cited by 103 · see citing works
Self-citationSaad, J. S., Ablan, S. D., Ghanam, R. H., Kim, A., Andrews, K., Nagashima, K., Soheilian, F., Freed, E. O., & Summers, M. F. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.07.027 · Cited by 95 · see citing works
Murray, P. S., Li, Z., Wang, J., Tang, C. L., Honig, B. H., & Murray, D. (2005) · Structure · doi:10.1016/j.str.2005.07.010 · Cited by 96 · see citing works
“Hence, the membrane binding free energies for both monomeric HIV-1 Gag and EIAV Gag are weak (w−5 kcal/mol) but sufficient to direct a significant amount of protein to the plasma membrane surface, which is preferentially enriched in acidic phospholipids with respect to other intracellular membranes (Pomorski et al., 2…”
BackgroundInfluentialInteractions Between Virus Proteins and Host Cell Membranes During the Viral Life Cycle
Villanueva, R. A., Rouillé, Y., & Dubuisson, J. (2005) · International review of cytology · doi:10.1016/s0074-7696(05)45006-8 · Cited by 94 · see citing works
Maurer‐Stroh, S., Gouda, M., Novatchkova, M., Schleiffer, A., Schneider, G., Sirota, F. L., Wildpaner, M., Hayashi, N., & Eisenhaber, F. (2004) · Genome biology · doi:10.1186/gb-2004-5-3-r21 · Cited by 94 · see citing works
“Complex conformational switches can trigger changes in accessibility of the lipid moiety [10-13].”
BackgroundHermida-Matsumoto, L., & Resh, M. D. (1999) · Journal of Virology · doi:10.1128/jvi.73.3.1902-1908.1999 · Cited by 95 · see citing works
“This steady-state distribution of p17MA was similar to that found for p17MA expressed exogenously in vitro and in vivo (30, 39).”
BackgroundMethodResultInfluentialSelf-citationThe Role of Ubiquitin in Retroviral Egress
Martin‐Serrano, J. (2007) · Traffic · doi:10.1111/j.1600-0854.2007.00609.x · Cited by 92 · see citing works
Derdowski, A., Ding, L.-M., & Spearman, P. (2004) · Journal of Virology · doi:10.1128/jvi.78.3.1230-1242.2004 · Cited by 110 · see citing works
“The M domain is essential for mediating interactions of the Gag polyprotein with the inner leaflet of the plasma membrane, where both myristic acid and electrostatic interactions between basic residues within the N-terminal end of MA and negatively charged membrane phospholipids play a role (14, 46).”
BackgroundHow HIV-1 Gag assembles in cells: Putting together pieces of the puzzle
Lingappa, J. R., Reed, J. C., Tanaka, M., Chutiraka, K., & Robinson, B. A. (2014) · Virus Research · doi:10.1016/j.virusres.2014.07.001 · Cited by 91 · see citing works
“A uthor M anuscript A uthor M anuscript A uthor M anuscript A uthor M anuscript Paillart and Gottlinger, 1999; Perez-Caballero et al., 2004; Saad et al., 2007; Spearman et al., 1997; Tang et al., 2004; Zhou and Resh, 1996), discussed further in Section 3.2.”
BackgroundInfluentialOno, A., Waheed, A. A., Joshi, A., & Freed, E. O. (2005) · Journal of Virology · doi:10.1128/jvi.79.22.14131-14140.2005 · Cited by 91 · see citing works
“, MA-CA) have suggested that Gag multimerization can enhance both membrane binding and DRM association (51, 74, 75, 78, 100).”
BackgroundOno, A., Huang, M. ‐., & Freed, E. O. (1997) · Journal of Virology · doi:10.1128/jvi.71.6.4409-4418.1997 · Cited by 91 · see citing works
“It is possible that the structures of p17 (MA) and the MA domain of Pr55 are not equivalent; the observation that an anti-MA monoclonal antibody reacts with p17 (MA) but not with Pr55 (25, 39) suggests that this is the case.”
BackgroundMurray, D., Arbuzova, A., Honig, B. H., & McLaughlint, S. (2002) · Current topics in membranes · doi:10.1016/s1063-5823(02)52012-3 · Cited by 89 · see citing works
“…of the BIV-l matrix domain is regulated by proteolysis: In the context of a newly formed virion, the Gag polyprotein is cleaved by the viral protease, exposing an as-yet-unknown "signal" on the matrix domain that sequesters the myristate chain (Spearman et at., 1997; Zhou and Resh, 1996).”
BackgroundLi, H., Dou, J., Ding, L., & Spearman, P. W. (2007) · Journal of Virology · doi:10.1128/jvi.01280-07 · Cited by 89 · see citing works
“The interaction of the N terminus of Gag with membranes is facilitated by a myristoyl switch (31, 37, 45).”
BackgroundPérez-Caballero, D., Hatziioannou, T., Martin‐Serrano, J., & Bieniasz, P. D. (2004) · Journal of Virology · doi:10.1128/jvi.78.17.9560-9563.2004 · Cited by 86 · see citing works
“These effects confer concentration dependence on the HIV-1 Gag-membrane interaction and are consistent with the notion that multimerization triggers the “myristoyl switch” (18, 22, 25), thereby imparting a high degree of cooperativity on HIV-1 Gag trafficking to membranes.”
BackgroundHamard-Peron, E., Juillard, F., Saad, J. S., Roy, C., Roingeard, P., Summers, M. F., Darlix, J.-L., Picart, C., & Muriaux, D. (2010) · Journal of Virology · doi:10.1128/jvi.01134-09 · Cited by 92 · see citing works
“, a conformational change during which the N-terminal myristoylation of Gag, initially sequestered in the MA, becomes exposed and is able to interact with membrane phospholipids (25, 40, 45, 47, 48, 53, 55, 61).”
BackgroundLlewellyn, G. N., Hogue, I. B., Grover, J. R., & Ono, A. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1001167 · Cited by 85 · see citing works
“When cells expressing Gag-iYFP were immunostained with an anti-p17MA antibody, which only recognizes the mature, cleaved matrix domain of Gag [100,101], the YFP signal was observed to colocalize substantially with p17MA signal at the uropod (Figure 2A and Table 3).”
BackgroundHIV Type 1 Gag as a Target for Antiviral Therapy
Waheed, A. A., & Freed, E. O. (2011) · AIDS Research and Human Retroviruses · doi:10.1089/aid.2011.0230 · Cited by 81 · see citing works
“Resh and colleagues proposed that Gag– membrane binding is regulated by a ‘‘myristyl switch’’ mechanism, whereby the myristate can shift between exposed and sequestered conformations.(39) Summers and coworkers used nuclear magnetic resonance (NMR) methods to confirm this hypothesis and to demonstrate that myristate ex…”
BackgroundHogue, I. B., Hoppe, A. D., & Ono, A. (2009) · Journal of Virology · doi:10.1128/jvi.02545-08 · Cited by 79 · see citing works
“74, 82), and others previously reported that mutations or truncations of NC affect membrane binding (13, 78, 89, 107).”
Vlach, J., & Saad, J. S. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1216655110 · Cited by 75 · see citing works
Biomedicine and Diseases: Review¶Assembling the human immunodeficiency virus type 1
Cimarelli, A., & Darlix, J. (2002) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-002-8495-6 · Cited by 79 · see citing works
Inlora, J., Chukkapalli, V., Derse, D., & Ono, A. (2011) · Journal of Virology · doi:10.1128/jvi.02383-10 · Cited by 73 · see citing works
Functions of the HIV-1 matrix protein p17.
Fiorentini, S., Marini, E., Caracciolo, S., & Caruso, A. (2006) · PubMed · Cited by 72 · see citing works
Liang, C., Hu, J., Whitney, J. B., Kleiman, L., & Wainberg, M. A. (2003) · Journal of Virology · doi:10.1128/jvi.77.3.1772-1783.2003 · Cited by 72 · see citing works
“This concept agrees with the myristyl switch model in which a lesser extent of exposure of myristate acid is believed to be the reason for the weak association of MA with the plasma membrane in comparison with the results observed for Pr55 (27, 48, 55, 68).”
ResultSpecific Interaction of a Novel Foamy Virus Env Leader Protein with the N-Terminal Gag Domain
Wilk, T., Geiselhart, V., Frech, M., Fuller, S., Flügel, R., & Löchelt, M. (2001) · Journal of Virology · doi:10.1128/jvi.75.17.7995-8007.2001 · Cited by 72 · see citing works
“amino-terminal acyl moiety and other motifs in MA (16, 57).”
BackgroundThe molecular basis of HIV capsid assembly—five years of progress
Adamson, C. S., & Jones, I. M. (2004) · Reviews in Medical Virology · doi:10.1002/rmv.418 · Cited by 69 · see citing works
“The subsequent cleavage event releases MA from CA-SP1 [126] leaving a mature MA associated with the membrane albeit with a considerably weaker affinity than MA within the context of Gag [73,77].”
BackgroundLee, Y. M., Liu, B., & Yu, X.-F. (1999) · Journal of Virology · doi:10.1128/jvi.73.7.5654-5662.1999 · Cited by 67 · see citing works
“It has also been proposed that HIV-1 Gag protein in the cytosol may adapt a different conformation once it has bound to the membrane (31, 45).”
BackgroundSingle-Cell and Single-Cycle Analysis of HIV-1 Replication
Holmes, M., Zhang, F., & Bieniasz, P. D. (2015) · PLoS Pathogens · doi:10.1371/journal.ppat.1004961 · Cited by 66 · see citing works
Virus assembly and plasma membrane domains: Which came first?
Kerviel, A., Thomas, A., Chaloin, L., Favard, C., & Muriaux, D. M. (2012) · Virus Research · doi:10.1016/j.virusres.2012.08.014 · Cited by 64 · see citing works
Biochemical Characterization of Rous Sarcoma Virus MA Protein Interaction with Membranes
Dalton, A. K., Murray, P. S., Murray, D., & Vogt, V. M. (2005) · Journal of Virology · doi:10.1128/jvi.79.10.6227-6238.2005 · Cited by 65 · see citing works
“model for the sequence of Gag(88-100) based on the C-terminal regions of other”
BackgroundMethodInfluentialMultiple, Switchable Protein:RNA Interactions Regulate Human Immunodeficiency Virus Type 1 Assembly
Bieniasz, P. D., & Telesnitsky, A. (2018) · Annual Review of Virology · doi:10.1146/annurev-virology-092917-043448 · Cited by 62 · see citing works
Membrane Binding of HIV-1 Matrix Protein: Dependence on Bilayer Composition and Protein Lipidation
Barros, M., Heinrich, F., Datta, S. A. K., Rein, A. R., Karageorgos, I. L., Nanda, H., & Lösche, M. (2016) · Journal of Virology · doi:10.1128/jvi.02820-15 · Cited by 63 · see citing works
“In cells, myristoylation of Gag is a prerequisite for plasma membrane targeting (49–52), since mutation of the N-terminal glycine completely blocks membrane localization of Gag and the subsequent assembly of infectious virus particles (53).”
BackgroundCrystal structure of bet3 reveals a novel mechanism for Golgi localization of tethering factor TRAPP
Kim, Y., Sohn, E. J., Seo, J., Lee, K., Lee, H., Hwang, I., Whiteway, M. S., Sacher, M. G., & Oh, B. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb871 · Cited by 62 · see citing works
“Although many examples of lipidation-mediated compartment-specific localization of cytosolic proteins are found in the literatur”
Retroviral Matrix Proteins: A Structural Perspective
Conte, M. R., & Matthews, S. (1998) · Virology · doi:10.1006/viro.1998.9206 · Cited by 61 · see citing works
“According to the hypothesis of a conformational myristoyl switch mechanism (Zhou and Resh, 1996; Spearman et al., 1997), the myristic acid has been proposed to be a key regulator of the Gag–membrane and MA–membrane interaction.”
BackgroundSimon, J. H., Carpenter, E. A., Fouchier, R. A. M., & Malim, M. H. (1999) · Journal of Virology · doi:10.1128/jvi.73.4.2667-2674.1999 · Cited by 62 · see citing works
“It was therefore unexpected when processed p17 (MA) was found to be present in postentry HIV-1 nucleoprotein complexes (7, 20, 25, 39); a conformational switch that results in the myristoyl residue becoming hidden from the surface of MA (53, 60), in conjunction with the phosphorylation of MA (6, 24, 25, 33), is though…”
BackgroundAfrican Swine Fever Virus Proteinase Is Essential for Core Maturation and Infectivity
Alejo, A., Andrés, G., & Salas, M. L. (2003) · Journal of Virology · doi:10.1128/jvi.77.10.5571-5577.2003 · Cited by 60 · see citing works
“This anomaly in the defective particles might hinder the disassembly process, as has been postulated for the uncoating of the incoming particle during human immunodeficiency virus infection (32, 49).”
BackgroundConte, M. R., Rumlová, M., Hunter, E., Ruml, T., & Matthews, S. (1997) · The EMBO Journal · doi:10.1093/emboj/16.19.5819 · Cited by 59 · see citing works
“Zhou and Resh (1996) have proposed that, when the myristate is exposed, it enables HIV Gag to bind todirects Gag to an intracellular assembly site.”
BackgroundMethodInfluentialLlewellyn, G. N., Grover, J. R., Olety, B., & Ono, A. (2013) · Journal of Virology · doi:10.1128/jvi.00040-13 · Cited by 56 · see citing works
Retroviral matrix and lipids, the intimate interaction
Hamard-Péron, É., & Muriaux, D. M. (2011) · Retrovirology · doi:10.1186/1742-4690-8-15 · Cited by 56 · see citing works
“This supports a pre-existing hypothesis first proposed by Zhou et al [31]: the existence of a “myristyl switch”, that is actually an entropic equilibrium between the [T] conformation that sequesters the myristate inside the protein, and the [R] conformation that promotes trimeristation and exposure of the myristate mo…”
BackgroundInfluentialGhanam, R. H., Samal, A. B., Fernandez, T. F., & Saad, J. S. (2012) · Frontiers in Microbiology · doi:10.3389/fmicb.2012.00055 · Cited by 55 · see citing works
“In vitro studies have established that Gag binds membranes more efficiently than the isolated MA protein (Zhou and Resh, 1996; Spearman et al., 1997; Hermida-Matsumoto and Resh, 1999; Ono and Freed, 1999; Paillart and Gottlinger, 1999; Bouamr et al., 2003).”
BackgroundInlora, J., Collins, D. R., Trubin, M. E., Chung, J. Y. J., & Ono, A. (2014) · mBio · doi:10.1128/mbio.02202-14 · Cited by 55 · see citing works
Human Immunodeficiency Virus Type 1 Matrix Protein Assembles on Membranes as a Hexamer
Alfadhli, A., Huseby, D. L., Kapit, E., Colman, D., & Barklis, E. (2006) · Journal of Virology · doi:10.1128/jvi.02122-06 · Cited by 53 · see citing works
“Evidence supports a myristoyl switch model for HIV, in which the MA myristate is partially buried until PrGag oligomerization, when its hydrocarbon tail is exposed, fostering membrane binding and virus assembly (5, 15, 22, 47, 49, 54, 56, 61).”
BackgroundElectrostatic Interactions and Binding Orientation of HIV-1 Matrix Studied by Neutron Reflectivity
Nanda, H., Datta, S. A. K., Heinrich, F., Lösche, M., Rein, A. R., Krueger, S., & Curtis, J. E. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2010.07.062 · Cited by 53 · see citing works
Wu, Z., Alexandratos, J. N., Ericksen, B., Lubkowski, J. T., Gallo, R. C., & Lu, W. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404649101 · Cited by 53 · see citing works
Guo, X., Roldán, A., Hu, J., Wainberg, M. A., & Liang, C. (2005) · Journal of Virology · doi:10.1128/jvi.79.3.1803-1812.2005 · Cited by 53 · see citing works
“Indeed, a correlation between Gag multimerization and Gag-membrane binding has been proposed in a “myristyl switch” model (21, 42, 45, 57).”
BackgroundThe frantic play of the concealed HIV envelope cytoplasmic tail
da Silva, E. S., Mulinge, M. M., & Perez-Bercoff, D. (2013) · Retrovirology · doi:10.1186/1742-4690-10-54 · Cited by 51 · see citing works
“The myristoylated moiety is cotranslationally coupled to the p55 MA domain, and its exposure is regulated by binding to calmodulin: binding to calmodulin induces conformational changes within MA [93,94] which lead to p55 binding to lipid rafts [95-97], where it oligomerises [73,86,87,98], through the C-terminal domain…”
BackgroundMembrane Targeting Properties of a Herpesvirus Tegument Protein-Retrovirus Gag Chimera
Bowzard, J. B., Visalli, R. J., Wilson, C., Loomis, J. S., Callahan, E. M., Courtney, R. J., & Wills, J. W. (2000) · Journal of Virology · doi:10.1128/jvi.74.18.8692-8699.2000 · Cited by 51 · see citing works
“Why is the M domain inactive in this context? It is possible that cleavage of MA from the remainder of Gag allows conformational rearrangements that disrupt the M domain and prevent plasma membrane binding (37, 50).”
BackgroundChen, S. S.-L., Lee, S.-F., & Wang, C.-T. (2001) · Journal of Virology · doi:10.1128/jvi.75.20.9925-9938.2001 · Cited by 49 · see citing works
“HIVgptmyr encodes a glycine-to-alanine substitution at residue 2 of MA, which abolishes the Pr55 myristylation signal and severely impairs Gag membrane binding (7, 47, 55, 72).”
BackgroundMembrane-induced alterations in HIV-1 gag and matrix protein-protein interactions
Scarlata, S., Ehrlich, L. S., & Carter, C. A. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1615 · Cited by 48 · see citing works
Fogarty, K., Chen, Y., Grigsby, I. F., Macdonald, P. J., Smith, E. M., Johnson, J. L., Rawson, J. M. O., Mansky, L. M., & Mueller, J. D. (2011) · Biophysical Journal · doi:10.1016/j.bpj.2011.02.008 · Cited by 44 · see citing works
“This result is consistent with the myristoyl switch model (16,17,23,24).”
ResultRoles played by acidic lipids in HIV-1 Gag membrane binding
Olety, B., & Ono, A. (2014) · Virus Research · doi:10.1016/j.virusres.2014.06.015 · Cited by 47 · see citing works
Jäger, S., Gottwein, E., & Kräusslich, H. (2007) · Journal of Virology · doi:10.1128/jvi.00044-07 · Cited by 47 · see citing works
“This difference in membrane binding is believed to be due to a myristoyl switch masking the hydrophobic properties of MA (41, 49).”
BackgroundSolution structure and dynamics of the bioactive retroviral M domain from rous sarcoma virus
McDonnell, J. M., Fushman, D., Cahill, S. M., Zhou, W., Wolven, A., Wilson, C., Nelle, T. D., Resh, M. D., Wills, J. W., & Cowburn, D. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.1788 · Cited by 47 · see citing works
Self-citationMass spectrometric characterization of lipid‐modified peptides for the analysis of acylated proteins
Hoffman, M. D., & Kast, J. (2006) · Journal of Mass Spectrometry · doi:10.1002/jms.981 · Cited by 46 · see citing works
- Authors
- Zhou, W., & Resh, M. D.
- Affiliations
- Memorial Sloan Kettering Cancer Center (US)
- ORCID
- Resh, M D
- Venue
- Journal of Virology
- Publisher
- American Society for Microbiology
- Published
- 1996-12
- Volume
- 70
- Issue
- 12
- Pages
- 8540-8548
- ISSN
- 0022-538X (ISSN-L)
- 1098-5514
- PMC
- PMC190946
- OpenAlex
- W2102965972
- Cited by
- 226
- References
- 47
- Citations by year
- 2026: 1 · 2025: 2 · 2023: 3 · 2022: 6 · 2021: 4 · 2020: 5 · 2019: 3 · 2018: 9 · 2017: 3 · 2016: 4 · 2015: 6 · 2014: 10 · 2013: 10 · 2012: 13
- FWCI
- 3.01
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Virology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Cancer Institute (CA 72309, R01CA072309)
- Topics
- Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Life Sciences › Immunology and Microbiology › Immunology › T-cell and Retrovirus Studies
- Keywords
- HIV-1, Pr55gag, membrane binding, myristate, myristoylation, plasma membrane targeting, viral assembly, nuclear targeting, protein conformational change, liposome binding, subcellular localization
- MeSH terms
- Animals, Epitopes, Cell Membrane, Humans, Myristic Acids, Protein Precursors, Viral Proteins, Signal Transduction, HIV Antigens, HIV-1, Gene Products, gag, Sequence Deletion, COS Cells, Myristic Acid, gag Gene Products, Human Immunodeficiency Virus
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