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Envelope surface glycoprotein gp120
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env
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The interaction between exposed cyclophilin A (CypA) and cell surface heparans represents the initial step of HIV-1 attachment and is a necessary step for HIV-1 gp120 binding to CD4 |
PubMed
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env
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Macrophage- and T-cell-tropic V3 loop peptides of HIV-1 gp120 bind specifically to the active site of the immunophilins FK506-binding protein (FKBP12), and cyclophilins A and B, and inhibit their peptidyl-prolyl cis-trans isomerase (PPIase) activities |
PubMed
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Nef
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nef
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HIV-1 Nef downregulates the expression of cyclophilin A protein in Nef-transfected SupT1 cells |
PubMed
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nef
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Cyclophilin A has been demonstrated to bind to HIV-1 Nef using a biochemical binding assay, however the biological significance of this interaction is currently not known |
PubMed
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Pr55(Gag)
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gag
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Treatment of cells with cyclosporine A blocks the interaction of HIV-1 Gag with eEF2, indicating that cyclophilin A (CypA) stabilizes the Gag-eEF2 association |
PubMed
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gag
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Targeting of the catalytic HECT domain (residues 598-952) of NEDD4-2s to HIV-1 Gag via CypA is sufficient to rescue HIV-1 budding defects |
PubMed
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gag
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H219Q and H219P substitutions in the viral CypA binding loop of HIV-1 Gag reduces CypA incorporation into HIV-1 and potentiates viral replication in CypA-rich MT-2 and H9 cells |
PubMed
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gag
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A fusion protein CypA-Nef consisting of cyclophilin A (CypA) linked to the amino terminus of Nef enhances the infectivity of Nef-defective HIV-1 particles and is incorporated into virions via association with Gag during particle assembly |
PubMed
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gag
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Binding of HIV-1 Gag to cyclophilin A requires a region within the nucleocapsid domain of Gag which is important for Gag self-association |
PubMed
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|
gag
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Cyclophilin A modulates processing of HIV-1 Gag by the viral protease |
PubMed
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Vif
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vif
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Vif has been demonstrated to bind to cyclophilin A using a biochemical binding assay |
PubMed
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Vpr
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vpr
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The complete C-terminal peptide Vpr75-90, comprising the 16 residues 75GCRHSRIGVTRQRRAR90, is required for maintaining the strong interaction with CypA in a 1:1 binding model. Replacement of R80 with alanine significantly reduces the binding affinity |
PubMed
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vpr
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Cyclophilin A catalyzes the prolyl cis/trans interconversion of proline residues at positions 5, 10, 14, and 35 in HIV-1 Vpr |
PubMed
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vpr
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Cyclophilin A interacts directly with HIV-1 Vpr to mediate the cis/trans-proline isomerization of Vpr, which is important for Vpr synthesis and function |
PubMed
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capsid
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gag
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HIV-1 HXB2 CA binds PPIA (CypA) and increasing amounts of PPIA can destabilize CA assembly |
PubMed
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gag
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HIV-1 CA binds PPIA (CypA); the crystal structure has been solved |
PubMed
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gag
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HIV-1 CA binds PPIA; binding is dependent upon residues W23, A77, and L189 in CA |
PubMed
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gag
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HIV-1 CA binds PPIA |
PubMed
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gag
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Binding of HIV-1 Capsid to cyclophilin A requires HIV-1 Gag dimerization |
PubMed
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gag
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The interaction of HIV-1 Capsid to cyclophilin A can be inhibited by cyclosporin A leading to inhibition of virus replication |
PubMed
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gag
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HIV-1 Capsid and Gag proteins bind to cyclophilin A, resulting in the incorporation of cyclophilin A into virions, which is important for the completion of early steps in HIV-1 replication following entry of the virus into cells |
PubMed
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gag
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Viral particles containing the CA mutations, H87Q, A88P and I91V (located in the PPIA- binding site), encapsidate 30% less PPIA (CypA) into virions relative to viral particles conatining wild type CA |
PubMed
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gag
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CA mutations (H87Q, A88P and I91V) in the PPIA (CypA) binding site reduce PPIA (CypA) affinity for CA BUT do not prevent PPIA (CypA) from binding to CA in a CA/NC biochemical based assay |
PubMed
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gag
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HIV-1 N74D CA mutant has less binding affinity to CypA and less HIV-1 infectivity than wild type |
PubMed
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gag
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V86M capsid mutant, a single amino acid change in the cyclophilin-binding loop of the HIV-1 capsid protein, can replicate in cells expressing TRIM5alpha(rh). This involves decreased binding to TRIM5alpha(rh) and retention of binding to cyclophilin A |
PubMed
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|
gag
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Substitution of Thr for Ala at position 105 of CA (A105T) rescues the impaired single-cycle infectivity of T54A and A92E mutants, indicating that CA determinants outside the CypA-binding loop can modulate the dependence of HIV-1 infection on CypA |
PubMed
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gag
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The enhancement of infection of A92E and G94D HIV-1 Capsid mutants by CypA is a result of enhanced reverse transcription in HeLa-P4 cells |
PubMed
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gag
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Proline-90 and Glycine-89 of HIV-1 Capsid are required for the binding of cyclophilin A to Capsid |
PubMed
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|
gag
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HIV-1 CA mutants N74D and P90A fail to bind to CPSF6 and cyclophilins (Nup358 and CypA), respectively, and trigger innate sensors, leading to nuclear translocation of NFkappaB and IRF3, production of type 1 IFN and induction of an antiviral state |
PubMed
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gag
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Cyclophilin A inhibits HIV-1 nuclear entry by promoting HIV-1 CA core stability |
PubMed
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gag
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The effect of inhibition of CA-CypA interaction by TRIM5alpha is virus isolate-dependent, which can result in inhibition, no change, or an increase in viral infectivity |
PubMed
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gag
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Cyclophilin A stabilizes the HIV-1 CA and antagonizes TNPO3 acceleration of uncoating in vitro |
PubMed
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|
gag
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Inhibition of the HIV-1 CA-CypA interaction rescues the infectivity of CA-N121K HIV-1. The N121K mutant is inhibited by CypA in HIV-1 infected cells |
PubMed
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gag
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Cyclophilin A mutants, R55K, R55A, F113W, and H126A, exhibit the most pronounced decrease in PPIase activity compared to wild type. These mutants bind to HIV-1 CA with low affinity |
PubMed
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gag
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A small molecule HIV-1 inhibitor PF74 destabilizes the viral capsid in vitro and its antiviral activity is promoted by binding of the host protein cyclophilin A to the HIV-1 capsid |
PubMed
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gag
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Cyclophilin A decreases the stability of the in vitro-assembled HIV-1 CA-NC complexes in the presence of cellular cytosolic extracts |
PubMed
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gag
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Delaying reverse transcription leads to a time-dependent loss in viral infectivity that is increased by inhibiting capsid-cyclophilin A interactions, but does not result in increased viral sensitivity to hTRIM5alpha |
PubMed
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gag
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CypA-CA interactions dictate the use of a NUP358/NUP153 dependent nuclear entry pathway |
PubMed
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gag
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Cyclophilin A is acetylated at amino acid residue Lys125 in human cells. Acetylated cyclophilin A inhibits its catalysis, inhibits cyclosporine binding, and alters HIV-1 capsid interaction |
PubMed
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gag
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TRIM5 alpha-mediated resistance to HIV-1 in Old World monkey cells is modulated by the HIV-1 Capsid and cyclophilin A interaction |
PubMed
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|
gag
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The interaction between cyclophilin A and HIV-1 CA is required for the enhanced restriction of HIV-1 due to rhTRIM5alpha in non-dividing cells |
PubMed
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|
gag
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Alignment of primate lentiviral capsid protein sequences demonstrates that they have conserved the proline rich cyclophilin A binding loop on their outer surface |
PubMed
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gag
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Reducing the binding of CypA to the A92E mutant capsid, either by cyclosporine treatment or by an additional P90A change in the CA protein, increases the amount of particulate capsids and viral infectivity in HeLa cells |
PubMed
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gag
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H219Q and H219P substitutions in the cyclophilin A binding loop of HIV-1 CA enhance HIV-1 replication by reducing viral cyclophilin A content in resulting virions as produced in cyclophilin A-rich cells |
PubMed
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gag
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HIV-1 CA R264K mutant is impaired in generating late reverse transcription products, is inhibited by the presence of normal levels of cyclophilin A, and is rescued with the development of a rare secondary mutation S173A |
PubMed
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gag
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Increasing CypA levels in permissive TE671 cells restrict HIV-1 CA mutants A92E and G94D in a CypA-dependent way |
PubMed
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gag
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Cyclophilin A binding to HIV-1 Capsid modulates the sensitivity of HIV-1 to host restriction factors |
PubMed
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|
gag
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Cyclophilin A decreases the degree of capsid protein processing by the HIV-1 protease |
PubMed
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gag
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The HIV-1 p2 peptide (spacer peptide in the HIV-1 Gag polyprotein between Capsid and Nucleocapsid; SP1) is involved in the interaction between HIV-1 Capsid and cyclophilin A |
PubMed
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|
gag
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Cyclophilin A catalyzes efficiently the cis/trans isomerization of the Gly-89-Pro-90 peptide bond of HIV-1 Capsid |
PubMed
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|
gag
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Cyclophilin A has a higher affinity for HIV-1 Gag than for the mature HIV-1 Capsid protein, as a result of additional interactions with the 12 C-terminal amino acids of HIV-1 Matrix |
PubMed
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|
gag
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The active site hydrophobic binding pocket of cyclophilin A (amino acids 54-126) binds to the N-Terminal and central portion of HIV-1 Capsid, most importantly to Capsid amino acids 85-93 |
PubMed
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|
integrase
|
gag-pol
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Compared to the HIV-1 IN wild type, two IN mutants (DeltaIN and C130S) have reduced levels of the cytoplasmic CA, suggesting accelerated uncoating. Virus derived from the IN mutants incorporates decreased levels of cyclophilin A (CypA) |
PubMed
|
|
matrix
|
gag
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The 12 carboxy-terminal amino acids of HIV-1 Matrix (p17; amino acids 121-132) are important for optimal binding of cyclophilin to HIV-1 Gag and Capsid (p24) |
PubMed
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|
gag
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Cyclophilin A binds to HIV-1 Matrix |
PubMed
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|
nucleocapsid
|
gag
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Cyclophilin A decreases the stability of the in vitro-assembled HIV-1 CA-NC complexes in the presence of cellular cytosolic extracts |
PubMed
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|
gag
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Binding of HIV-1 Gag to cyclophilin A requires a region within the nucleocapsid domain of Gag which is important for Gag self-association |
PubMed
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p6
|
gag
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HIV-1 p6 binds to cyclophilin A, particularly, through the p6 proline residues, located at positions 5, 7, 10, 11, 24, 30, 37 and 49 |
PubMed
|
|
retropepsin
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gag-pol
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Positional proteomics analysis identifies the cleavage of human peptidylprolyl isomerase A (PPIA; cyclophilin A) at amino acid residues 6-9 and 23-24 by the HIV-1 protease |
PubMed
|
|
reverse transcriptase
|
gag-pol
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The enhancement of infection of A92E and G94D HIV-1 Capsid mutants by CypA is a result of enhanced reverse transcription in HeLa-P4 cells |
PubMed
|