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Envelope surface glycoprotein gp120
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env
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HIV-1 gp120-treated vaginal epithelial cells show upregulation of myxovirus resistance 2 (MX2, MXB) expression as compared to untreated control |
PubMed
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Tat
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tat
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HIV-1 and the viral protein Tat modulate the expression of MX dynamin-like GTPase 2 (MX2; MxB) in immature dendritic cells and monocyte-derived macrophages |
PubMed
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Vpr
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vpr
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HIV-1 Vpr upregulates the gene expression of MX2 in human monocyte-derived macrophages |
PubMed
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vpr
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HIV-1 Vpr upregulates the gene expression of MX2 in human monocyte-derived dendritic cells |
PubMed
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capsid
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gag
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HIV-1 CA binds MX2 (MxB) dependent upon G208 in CA, which is not related to IFN-alpha restriction in THP-1, HT-1080, and U87 MG cell lines |
PubMed
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gag
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HIV-1 CA H87P, G116A, and P207A mutants are resistant to inhibition by MX2 (MxB), but still interact with MX2 (MxB) |
PubMed
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gag
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CA-NC complex/core (in vitro-assembled from HIV-1 NL4-3 Gag amino acids 133-433; fusion protein) DOES NOT bind to MX2 (MxB) with mutations in interface 2 (Q644D, M574D, Y651D and M574D/Y651D, each preventing MX2 oligomerization) |
PubMed
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gag
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CA binding to MX2 (MxB) involves the N-terminal 25 amino acids of MX2 (MxB) |
PubMed
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gag
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Anti-HIV-1 activity of MX2 is greatly enhanced when MX2 is directly targeted to HIV-1 CA by fusion with PPIA (CypA) |
PubMed
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gag
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CA-NC complex/core (in vitro-assembled from HIV-1 NL4-3 Gag amino acids 133-433; fusion protein) binds to MX2 (MxB) with mutations in interface 1 (E424R, K663D, L669D) as strongly as wild-type MX2 (MxB) |
PubMed
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gag
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Disruption of the leucine zipper by a single point mutation L661K abolishes the ability of MX2 to oligomerize, leading to neither binding to in vitro assembled HIV-1 CA-NC complexes nor restrict HIV-1 infection |
PubMed
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gag
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MX2 binds to in vitro assembled HIV-2 and SIVmac CA-NC complexes |
PubMed
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gag
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HIV-1 CA tubes bind MX2 (MxB) directly in vitro, indicating that cellular cofactors are not required for the direct interaction of these two proteins |
PubMed
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gag
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WT CA binds MX2 (MX2-HA) efficiently as well as interface 1 mutants K663D, I423D/K663D, and M666D; hinge 1 mutant E681A and interface 2 mutants M574D and Y651D do not bind CA efficiently |
PubMed
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gag
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HIV-1 CA in assembled lattices bind MX2, but not single CA hexamers (pentamers or monomers) |
PubMed
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gag
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HIV-1 CA binds MBP-MX2-YRGK/IKM directly, indicating that cellular cofactors are not required for the binding between CA and MX2 |
PubMed
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gag
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HIV-1 CA-MX2 interaction plays a role in in restriction of HIV-1 replication (negative correlation of CA-MX2 binding scatterplot analysis yields a Spearman rank correlation coefficient p value of 0.028) |
PubMed
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gag
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Efficient HIV-1 CA binding to MX2 requires the first 84 amino acids of MX2 (N-terminus) |
PubMed
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gag
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CA/MX2 (MxB) binding requires an intact 'RRR' motif located at amino acids 11-13 in the N-terminal of MX2 (MxB) |
PubMed
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gag
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MX2 binds to the HIV-1 core and inhibits the uncoating process of HIV-1 during infection, which is prevented by a benzimidazole-based inhibitor that binds to a specific pocket in the HIV-1 capsid |
PubMed
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gag
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HIV-1 CA N57S, K70R, N74D, A88T, G89V, P90A, and T107N mutants are resistant to inhibition by MX2, suggesting that CA is a specific target of MX2 |
PubMed
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gag
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HIV-1 CA mutants V86A, V86Q, H87P, H87Q, A88V, and A92P in the cyclophilin A-binding loop of CA are resistant to MxB restriction |
PubMed
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gag
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HIV-1 CA mutants E45A, N57A, N57S, K70R, G89V, and T107N are significantly less sensitive than the wild-type to MxB restriction |
PubMed
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gag
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MX2 binds to in vitro assembled HIV-1 CA-NC complexes, whereas MX1 is not able to interact with in vitro assembled HIV-1 CA-NC complexes |
PubMed
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gag
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MX2 co-localizes with HIV-1 CA, suggesting that MX2 directly associates with HIV-1 cores in living cells |
PubMed
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gag
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A protein chimera MX2(1-90)-MX1(43-662) has the ability to bind in vitro assembled HIV-1 CA-NC complexes, suggesting that the N-terminal region (residues 1-90) of MX2 is involved in its ability to bind capsid |
PubMed
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gag
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The cryo-EM images show distinct protein densities decorating the HIV-1 CA tubes in the presence of MX2 compared to MX2(84-715) mutant, confirming both direct protein binding and the importance of the MX2 N terminus in this interaction |
PubMed
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gag
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HIV-1 CA mutants M10I, N57S, H87R, P90T, Q95L, M185I, P207S, G208R, and T210K are entirely or partially resistant to human MX2 |
PubMed
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integrase
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gag-pol
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HIV-1 IN mutant D64N/D116N is significantly more resistant than the wild-type and D167K IN mutant to MxB restriction |
PubMed
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nucleocapsid
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gag
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CA-NC complex/core (in vitro-assembled from HIV-1 NL4-3 Gag amino acids 133-433; fusion protein) DOES NOT bind to MX2 (MxB) with the L661K mutation (prevents oligomerization) in the putative leucine zipper region |
PubMed
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gag
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CA-NC complex/core (in vitro-assembled from HIV-1 NL4-3 Gag amino acids 133-433; fusion protein) DOES NOT bind to MX2 (MxB) with mutations in interface 2 (Q644D, M574D, Y651D and M574D/Y651D, each preventing MX2 oligomerization) |
PubMed
|
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gag
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CA-NC complexes (in vitro-assembled from HIV-1 NL4-3 Gag amino acids 133-433; fusion protein) bind to MX2 (MxB) with mutations in interface 1 (E424R, K663D, L669D) as strongly as wild-type MX2 (MxB) |
PubMed
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