| Interacting proteins: Q8IUX4 and Q9HC16 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q8IUX4 and Q9HC16 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q8IUX4 and Q9HC16 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q8IUX4 and Q9HC16 |
Pubmed |
SVM Score :0.0 |
| Similar to APOBEC3G , APOBEC3F also induced G to A hypermutations in HIV genomic DNA , and the viral Vif protein counteracted its activity . ^^^ |
|
| Interacting proteins: Q8IUX4 and Q9HC16 |
Pubmed |
SVM Score :0.0 |
| Surprisingly , APOBEC3F and APOBEC3G are extensively coexpressed in nonpermissive human cells , including primary lymphocytes and the cell line CEM , where they form heterodimers . ^^^ |
|
| Interacting proteins: Q8IUX4 and Q9HC16 |
Pubmed |
SVM Score :0.0 |
| Like APOBEC3G , human APOBEC3F preferentially restricts vif deficient virus . ^^^ Indeed , the mutation spectra and expression profile found for APOBEC3F indicate that this enzyme , together with APOBEC3G , accounts for the G to A hypermutation of proviruses described in HIV infected individuals . ^^^ |
|
| Interacting proteins: Q8IUX4 and Q9HC16 |
Pubmed |
SVM Score :0.0 |
| Two members of this family , APOBEC3G and APOBEC3F , have been found to have potent activity against virion infectivity factor deficient ( Deltavif ) human immunodeficiency virus 1 ( HIV 1 ) . ^^^ The lentiviral Vif protein prevents the deamination by inducing the degradation of APOBEC3G and APOBEC3F . ^^^ |
|
| Interacting proteins: Q8IUX4 and Q9HC16 |
Pubmed |
SVM Score :0.0 |
| Primate lentivirus Vif proteins function by suppressing the antiviral activity of the cell encoded apolipoprotein B mRNA editing enzyme catalytic polypeptide like ( APOBEC ) proteins APOBEC3G and APOBEC3F . ^^^ Consistent with this view and with previous results , we report that the Vif proteins of several diverse simian immunodeficiency viruses ( SIVs ) that are not known to infect humans are not effective inhibitors of human APOBEC3G or APOBEC3F when assessed in transient transfection experiments . ^^^ |
|
| Interacting proteins: Q8IUX4 and Q9HC16 |
Pubmed |
SVM Score :0.0 |
| The retroviral hypermutation specificity of APOBEC3F and APOBEC3G is governed by the C terminal DNA cytosine deaminase domain . ^^^ The human proteins APOBEC3F and APOBEC3G restrict retroviral infection by deaminating cytosine residues in the first cDNA strand of a replicating virus . ^^^ A chimeric protein with the N terminal cytosine deaminase domain from APOBEC3G and the C terminal cytosine deaminase domain from APOBEC3F elicited a dinucleotide hypermutation preference nearly indistinguishable from that of APOBEC3F . ^^^ An N terminal APOBEC3G deletion mutant displayed a preference indistinguishable from that of the full length protein , and replacing the C terminal deaminase domain of APOBEC3F with AID resulted in an AID like mutational signature . ^^^ |
|
| Interacting proteins: Q8IUX4 and Q9HC16 |
Pubmed |
SVM Score :0.0 |
| The HIV 1 viral accessory protein Vif prevents the encapsidation of the antiviral cellular cytidine deaminases APOBEC3F and APOBEC3G by inducing their proteasomal degradation . ^^^ |
|
| Interacting proteins: Q8IUX4 and Q9HC16 |
Pubmed |
SVM Score :0.0 |
| Here , we show that APOBEC3F is also a potent retroviral restrictor but that its activity , unlike that of APOBEC3G , is partially resistant to HIV 1 Vif and results in a clear 5 ' GA > AA retroviral hypermutation preference . ^^^ Moreover , APOBEC3F and APOBEC3G appear to be coordinately expressed in a wide range of human tissues and are independently able to inhibit retroviral infection . ^^^ Thus , APOBEC3F and APOBEC3G are likely to function alongside one another in the provision of an innate immune defense , with APOBEC3F functioning as the major contributor to HIV 1 hypermutation in vivo . . ^^^ |
|
| Interacting proteins: Q8IUX4 and Q9HC16 |
Pubmed |
SVM Score :0.0 |
| The human cytidine deaminase Apobec3F ( h A3F ) , a protein related to the previously recognized antiviral factor Apobec3G ( h A3G ) , has antiviral activity against human immunodeficiency virus type 1 ( HIV 1 ) that is suppressed by the viral protein Vif . ^^^ |
|
| Interacting proteins: Q8IUX4 and Q9HC16 |
Pubmed |
SVM Score :0.0 |
| In conclusion , APOBEC3G and APOBEC3F but not rat APOBEC 1 can downregulate the production of replication competent hepadnaviral nucleocapsids . ^^^ |
|
| Interacting proteins: Q8IUX4 and Q9HC16 |
Pubmed |
SVM Score :0.0 |
| Human APOBEC3F and APOBEC3G are double domained deaminases that can catalyze dC > dU deamination in HIV 1 and MLV retroviral DNA replication intermediates , targeting T C or C C dinucleotides , respectively . ^^^ Here , we compare APOBEC3F and APOBEC3G to APOBEC3C , a single domained deaminase that can also act on both HIV 1 and MLV . ^^^ We find that whereas APOBEC3C contains all the information necessary for both Vif binding and cytidine deaminase activity in a single domain , it is the C terminal domain of APOBEC3F and APOBEC3G that confer their target site specificity for cytidine deamination . ^^^ |
|
| Interacting proteins: Q8IUX4 and Q9HC16 |
Pubmed |
SVM Score :0.0 |
| Human APOBEC3F and APOBEC3G are specifically incorporated into human immunodeficiency virus type 1 ( HIV 1 ) progeny virions in the absence of virion infectivity factor ( Vif ) , where they deaminate deoxycytidine to deoxyuridine on the minus strand of nascent reverse transcripts . ^^^ When expressed in the yeast Saccharomyces cerevisiae , human APOBEC3C , APOBEC3F , or APOBEC3G or mouse APOBEC 3 potently inhibit replication of the Ty 1 LTR retrotransposon . ^^^ |
|
| Interacting proteins: Q8IUX4 and Q9HC16 |
Pubmed |
SVM Score :0.0 |
| We demonstrate that MLV is highly sensitive to inhibition by human APOBEC3G and APOBEC3B but resistant to inhibition by murine APOBEC 3 or by other human APOBEC 3 proteins , including APOBEC3F . ^^^ This sensitivity fully correlates with the ability of these proteins to be packaged into MLV virion particles : i . e . , human APOBEC3G and APOBEC3B are packaged while murine APOBEC 3 and human APOBEC3F are excluded . ^^^ |
|
| Interacting proteins: Q8IUX4 and Q9HC16 |
Pubmed |
SVM Score :0.0 |
| While the human antiretroviral defense factors APOBEC3F and APOBEC3G are potent inhibitors of the replication of HIV 1 mutants lacking a functional vif gene , the Vif protein expressed by wild type HIV 1 blocks the function of both host cell proteins . ^^^ APOBEC3B , which shows approximately 58 % sequence identity to both APOBEC3F and APOBEC3G , shares the ability of these other human proteins to bind the nucleocapsid domain of HIV 1 Gag specifically and to thereby package into progeny virion particles . ^^^ However , APOBEC3B differs from APOBEC3F and APOBEC3G in that it is unable to bind to HIV 1 Vif in co expressing cells and is therefore efficiently packaged into HIV 1 virions regardless of Vif expression . ^^^ Unfortunately , APOBEC3B also differs from APOBEC3F and APOBEC3G in that it is not normally expressed in the lymphoid cells that serve as targets for HIV 1 infection . ^^^ |
|
| Interacting proteins: Q8IUX4 and Q9HC16 |
Pubmed |
SVM Score :0.0 |
| This unique genetic system further enabled us to show that expression of APOBEC3G or its homolog APOBEC3F was able to inhibit the mobility of the retrotransposon Ty 1 by a mechanism that involves the deamination of cDNA cytosines . ^^^ |
|
| Interacting proteins: Q8IUX4 and Q9HC16 |
Pubmed |
SVM Score :0.0 |
| The HIV 1 Vif protein counteracts the antiviral activity exhibited by the host cytidine deaminases APOBEC3G and APOBEC3F . ^^^ Interestingly , not all the detected defects lead to a complete inactivation of Vif function since some mutants retained selective neutralizing activity against APOBEC3F but not APOBEC3G or vice versa . ^^^ Concordantly , independently hypermutated proviruses with distinguishable patterns of G to A substitution attributable to cytidine deamination induced by APOBEC3G , APOBEC3F , or both enzymes were present in individuals carrying proviruses with completely or partly defective Vif variants . ^^^ |
|
| Interacting proteins: Q8IUX4 and Q9HC16 |
Pubmed |
SVM Score :0.0 |
| Both molecular FV clones and primary uncloned viruses were susceptible to APOBEC3G , and viral infectivity was also inhibited by murine and simian APOBEC3G homologues , as well as by human APOBEC3F . ^^^ |
|
| Interacting proteins: Q8IUX4 and Q9HC16 |
Pubmed |
SVM Score :0.0 |
| APOBEC3F and APOBEC3G mRNA levels do not correlate with human immunodeficiency virus type 1 plasma viremia or CD4+ T cell count . ^^^ APOBEC3F and APOBEC3G ( hA3F and hA3G ) are part of an innate mechanism of antiretroviral defense . ^^^ |
|
| Interacting proteins: Q8IUX4 and Q9HC16 |
Pubmed |
SVM Score :0.0 |
| Comparative analysis of the antiretroviral activity of APOBEC3G and APOBEC3F from primates . ^^^ APOBEC3G and APOBEC3F exhibit antiretroviral activity primarily as a consequence of their ability to deaminate cytidines in retroviral DNA . ^^^ Here , we compare the properties of APOBEC3F and APOBEC3G from human , macaque , and African green monkey ( AGM ) . ^^^ While all APOBEC proteins tested exhibited anti HIV 1 activity , human APOBEC3F was , surprisingly , 10 to 50 fold less potent than human APOBEC3G . ^^^ Overall , highly efficient and species specific neutralization of APOBEC3G , and less efficient neutralization of APOBEC3F , appears to be a general property of Vif proteins . . ^^^ |
|
| Interacting proteins: Q8IUX4 and Q9HC16 |
Pubmed |
SVM Score :0.0 |
| Differential requirement for conserved tryptophans in human immunodeficiency virus type 1 Vif for the selective suppression of APOBEC3G and APOBEC3F . ^^^ APOBEC3G ( A3G ) and related cytidine deaminases , such as APOBEC3F ( A3F ) , are potent inhibitors of retroviruses . ^^^ |
|
| Interacting proteins: Q8IUX4 and Q9HC16 |
Pubmed |
SVM Score :0.0 |
| Members of this family ( APOBEC3G and APOBEC3F ) have been recently shown to be able to restrict HIV 1 replication in physiologically relevant target cells ( macrophages , lymphocytes ) , presumably by triggering extensive deamination of the viral RNA / DNA replication intermediates . ^^^ |
|
| Interacting proteins: Q8IUX4 and Q9HC16 |
Pubmed |
SVM Score :0.0 |
| Human retroviral host restriction factors APOBEC3G and APOBEC3F localize to mRNA processing bodies . ^^^ Similar analysis with other APOBEC 3 family members revealed a potential link between the localization of APOBEC3G and APOBEC3F to a common ribonucleoprotein complex and P bodies with potent anti HIV 1 activity . ^^^ In addition , we present evidence suggesting that an important role for HIV 1 Vif , which subverts both APOBEC3G and APOBEC3F antiviral function by inducing their degradation , could be to selectively remove these proteins from and / or restrict their localization to P bodies . ^^^ Taken together , the results of this study reveal a novel link between innate immunity against retroviruses and P bodies suggesting that APOBEC3G and APOBEC3F could function in the context of P bodies to restrict HIV 1 replication . . ^^^ |
|
| Interacting proteins: Q8IUX4 and Q9HC16 |
Pubmed |
SVM Score :0.0 |
| Hypermutations in hepatitis B virus ( HBV ) DNA by APOBEC 3 cytidine deaminases have been detected in vitro and in vivo , and APOBEC3G ( A3G ) and APOBEC3F ( A3F ) have been shown to inhibit the replication of HBV in vitro , but the presumably low or even absent hepatic expression of these enzymes has raised the question as to their physiological impact on HBV replication . ^^^ |
|
| Interacting proteins: Q8IUX4 and Q9HC16 |
Pubmed |
SVM Score :0.0 |
| Human APOBEC3F ( hA3F ) and APOBEC3G ( hA3G ) are antiretroviral cytidine deaminases that can be encapsidated during virus assembly to catalyze C > U deamination of the viral reverse transcripts in the next round of infection . ^^^ |
|
| Interacting proteins: Q8IUX4 and Q9HC16 |
Pubmed |
SVM Score :0.0 |
| The cytoplasmic single stranded DNA cytidine deaminases APOBEC3G and APOBEC3F block HIV replication by introducing premature stop codons into the viral genome . ^^^ |
|
| Interacting proteins: Q8IUX4 and Q9HC16 |
Pubmed |
SVM Score :0.0 |
| The human cytidine deaminases APOBEC3G ( hA3G ) and APOBEC3F ( hA3F ) are intracellular antiretroviral factors that can hypermutate nascent reverse transcripts and inhibit the replication of human immunodeficiency virus type 1 ( HIV 1 ) . ^^^ |
|
| Interacting proteins: Q8IUX4 and Q9HC16 |
Pubmed |
SVM Score :0.0 |
| APOBEC3G and APOBEC3F restrict human immunodeficiency virus type 1 ( HIV 1 ) replication in vitro through the induction of G > A hypermutation ; however , the relevance of this host antiviral strategy to clinical HIV 1 is currently not known . ^^^ G > A hypermutation conforming to expected APOBEC3G polynucleotide sequence preferences was inferred in 9 . 4 % ( n = 12 ) of the HIV 1 sequences , with a further 2 . 4 % ( n = 3 ) conforming to APOBEC3F , and was independently associated with reduced pretreatment viremia ( reduction of 0 . 7 log ( 10 ) copies / ml ; P = 0 . 001 ) . ^^^ |
|
| Interacting proteins: Q9HC16 and Q8IUX4 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q9HC16 and Q8IUX4 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q9HC16 and Q8IUX4 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q9HC16 and Q8IUX4 |
Pubmed |
SVM Score :0.0 |
| Similar to APOBEC3G , APOBEC3F also induced G to A hypermutations in HIV genomic DNA , and the viral Vif protein counteracted its activity . ^^^ |
|
| Interacting proteins: Q9HC16 and Q8IUX4 |
Pubmed |
SVM Score :0.0 |
| Surprisingly , APOBEC3F and APOBEC3G are extensively coexpressed in nonpermissive human cells , including primary lymphocytes and the cell line CEM , where they form heterodimers . ^^^ |
|
| Interacting proteins: Q9HC16 and Q8IUX4 |
Pubmed |
SVM Score :0.0 |
| Here , we show that APOBEC3F is also a potent retroviral restrictor but that its activity , unlike that of APOBEC3G , is partially resistant to HIV 1 Vif and results in a clear 5 ' GA > AA retroviral hypermutation preference . ^^^ Moreover , APOBEC3F and APOBEC3G appear to be coordinately expressed in a wide range of human tissues and are independently able to inhibit retroviral infection . ^^^ Thus , APOBEC3F and APOBEC3G are likely to function alongside one another in the provision of an innate immune defense , with APOBEC3F functioning as the major contributor to HIV 1 hypermutation in vivo . . ^^^ |
|
| Interacting proteins: Q9HC16 and Q8IUX4 |
Pubmed |
SVM Score :0.0 |
| Like APOBEC3G , human APOBEC3F preferentially restricts vif deficient virus . ^^^ Indeed , the mutation spectra and expression profile found for APOBEC3F indicate that this enzyme , together with APOBEC3G , accounts for the G to A hypermutation of proviruses described in HIV infected individuals . ^^^ |
|
| Interacting proteins: Q9HC16 and Q8IUX4 |
Pubmed |
SVM Score :0.0 |
| Two members of this family , APOBEC3G and APOBEC3F , have been found to have potent activity against virion infectivity factor deficient ( Deltavif ) human immunodeficiency virus 1 ( HIV 1 ) . ^^^ The lentiviral Vif protein prevents the deamination by inducing the degradation of APOBEC3G and APOBEC3F . ^^^ |
|
| Interacting proteins: Q9HC16 and Q8IUX4 |
Pubmed |
SVM Score :0.0 |
| Primate lentivirus Vif proteins function by suppressing the antiviral activity of the cell encoded apolipoprotein B mRNA editing enzyme catalytic polypeptide like ( APOBEC ) proteins APOBEC3G and APOBEC3F . ^^^ Consistent with this view and with previous results , we report that the Vif proteins of several diverse simian immunodeficiency viruses ( SIVs ) that are not known to infect humans are not effective inhibitors of human APOBEC3G or APOBEC3F when assessed in transient transfection experiments . ^^^ |
|
| Interacting proteins: Q9HC16 and Q8IUX4 |
Pubmed |
SVM Score :0.0 |
| The retroviral hypermutation specificity of APOBEC3F and APOBEC3G is governed by the C terminal DNA cytosine deaminase domain . ^^^ The human proteins APOBEC3F and APOBEC3G restrict retroviral infection by deaminating cytosine residues in the first cDNA strand of a replicating virus . ^^^ A chimeric protein with the N terminal cytosine deaminase domain from APOBEC3G and the C terminal cytosine deaminase domain from APOBEC3F elicited a dinucleotide hypermutation preference nearly indistinguishable from that of APOBEC3F . ^^^ An N terminal APOBEC3G deletion mutant displayed a preference indistinguishable from that of the full length protein , and replacing the C terminal deaminase domain of APOBEC3F with AID resulted in an AID like mutational signature . ^^^ |
|
| Interacting proteins: Q9HC16 and Q8IUX4 |
Pubmed |
SVM Score :0.0 |
| The HIV 1 viral accessory protein Vif prevents the encapsidation of the antiviral cellular cytidine deaminases APOBEC3F and APOBEC3G by inducing their proteasomal degradation . ^^^ |
|
| Interacting proteins: Q9HC16 and Q8IUX4 |
Pubmed |
SVM Score :0.0 |
| Human APOBEC3F and APOBEC3G are double domained deaminases that can catalyze dC > dU deamination in HIV 1 and MLV retroviral DNA replication intermediates , targeting T C or C C dinucleotides , respectively . ^^^ Here , we compare APOBEC3F and APOBEC3G to APOBEC3C , a single domained deaminase that can also act on both HIV 1 and MLV . ^^^ We find that whereas APOBEC3C contains all the information necessary for both Vif binding and cytidine deaminase activity in a single domain , it is the C terminal domain of APOBEC3F and APOBEC3G that confer their target site specificity for cytidine deamination . ^^^ |
|
| Interacting proteins: Q9HC16 and Q8IUX4 |
Pubmed |
SVM Score :0.0 |
| Human APOBEC3F and APOBEC3G are specifically incorporated into human immunodeficiency virus type 1 ( HIV 1 ) progeny virions in the absence of virion infectivity factor ( Vif ) , where they deaminate deoxycytidine to deoxyuridine on the minus strand of nascent reverse transcripts . ^^^ When expressed in the yeast Saccharomyces cerevisiae , human APOBEC3C , APOBEC3F , or APOBEC3G or mouse APOBEC 3 potently inhibit replication of the Ty 1 LTR retrotransposon . ^^^ |
|
| Interacting proteins: Q9HC16 and Q8IUX4 |
Pubmed |
SVM Score :0.0 |
| We demonstrate that MLV is highly sensitive to inhibition by human APOBEC3G and APOBEC3B but resistant to inhibition by murine APOBEC 3 or by other human APOBEC 3 proteins , including APOBEC3F . ^^^ This sensitivity fully correlates with the ability of these proteins to be packaged into MLV virion particles : i . e . , human APOBEC3G and APOBEC3B are packaged while murine APOBEC 3 and human APOBEC3F are excluded . ^^^ |
|
| Interacting proteins: Q9HC16 and Q8IUX4 |
Pubmed |
SVM Score :0.0 |
| This unique genetic system further enabled us to show that expression of APOBEC3G or its homolog APOBEC3F was able to inhibit the mobility of the retrotransposon Ty 1 by a mechanism that involves the deamination of cDNA cytosines . ^^^ |
|
| Interacting proteins: Q9HC16 and Q8IUX4 |
Pubmed |
SVM Score :0.0 |
| The human cytidine deaminase Apobec3F ( h A3F ) , a protein related to the previously recognized antiviral factor Apobec3G ( h A3G ) , has antiviral activity against human immunodeficiency virus type 1 ( HIV 1 ) that is suppressed by the viral protein Vif . ^^^ |
|
| Interacting proteins: Q9HC16 and Q8IUX4 |
Pubmed |
SVM Score :0.0 |
| In conclusion , APOBEC3G and APOBEC3F but not rat APOBEC 1 can downregulate the production of replication competent hepadnaviral nucleocapsids . ^^^ |
|
| Interacting proteins: Q9HC16 and Q8IUX4 |
Pubmed |
SVM Score :0.0 |
| The HIV 1 Vif protein counteracts the antiviral activity exhibited by the host cytidine deaminases APOBEC3G and APOBEC3F . ^^^ Interestingly , not all the detected defects lead to a complete inactivation of Vif function since some mutants retained selective neutralizing activity against APOBEC3F but not APOBEC3G or vice versa . ^^^ Concordantly , independently hypermutated proviruses with distinguishable patterns of G to A substitution attributable to cytidine deamination induced by APOBEC3G , APOBEC3F , or both enzymes were present in individuals carrying proviruses with completely or partly defective Vif variants . ^^^ |
|
| Interacting proteins: Q9HC16 and Q8IUX4 |
Pubmed |
SVM Score :0.0 |
| Both molecular FV clones and primary uncloned viruses were susceptible to APOBEC3G , and viral infectivity was also inhibited by murine and simian APOBEC3G homologues , as well as by human APOBEC3F . ^^^ |
|
| Interacting proteins: Q9HC16 and Q8IUX4 |
Pubmed |
SVM Score :0.0 |
| APOBEC3F and APOBEC3G mRNA levels do not correlate with human immunodeficiency virus type 1 plasma viremia or CD4+ T cell count . ^^^ APOBEC3F and APOBEC3G ( hA3F and hA3G ) are part of an innate mechanism of antiretroviral defense . ^^^ |
|
| Interacting proteins: Q9HC16 and Q8IUX4 |
Pubmed |
SVM Score :0.0 |
| While the human antiretroviral defense factors APOBEC3F and APOBEC3G are potent inhibitors of the replication of HIV 1 mutants lacking a functional vif gene , the Vif protein expressed by wild type HIV 1 blocks the function of both host cell proteins . ^^^ APOBEC3B , which shows approximately 58 % sequence identity to both APOBEC3F and APOBEC3G , shares the ability of these other human proteins to bind the nucleocapsid domain of HIV 1 Gag specifically and to thereby package into progeny virion particles . ^^^ However , APOBEC3B differs from APOBEC3F and APOBEC3G in that it is unable to bind to HIV 1 Vif in co expressing cells and is therefore efficiently packaged into HIV 1 virions regardless of Vif expression . ^^^ Unfortunately , APOBEC3B also differs from APOBEC3F and APOBEC3G in that it is not normally expressed in the lymphoid cells that serve as targets for HIV 1 infection . ^^^ |
|
| Interacting proteins: Q9HC16 and Q8IUX4 |
Pubmed |
SVM Score :0.0 |
| Human retroviral host restriction factors APOBEC3G and APOBEC3F localize to mRNA processing bodies . ^^^ Similar analysis with other APOBEC 3 family members revealed a potential link between the localization of APOBEC3G and APOBEC3F to a common ribonucleoprotein complex and P bodies with potent anti HIV 1 activity . ^^^ In addition , we present evidence suggesting that an important role for HIV 1 Vif , which subverts both APOBEC3G and APOBEC3F antiviral function by inducing their degradation , could be to selectively remove these proteins from and / or restrict their localization to P bodies . ^^^ Taken together , the results of this study reveal a novel link between innate immunity against retroviruses and P bodies suggesting that APOBEC3G and APOBEC3F could function in the context of P bodies to restrict HIV 1 replication . . ^^^ |
|
| Interacting proteins: Q9HC16 and Q8IUX4 |
Pubmed |
SVM Score :0.0 |
| Hypermutations in hepatitis B virus ( HBV ) DNA by APOBEC 3 cytidine deaminases have been detected in vitro and in vivo , and APOBEC3G ( A3G ) and APOBEC3F ( A3F ) have been shown to inhibit the replication of HBV in vitro , but the presumably low or even absent hepatic expression of these enzymes has raised the question as to their physiological impact on HBV replication . ^^^ |
|
| Interacting proteins: Q9HC16 and Q8IUX4 |
Pubmed |
SVM Score :0.0 |
| Human APOBEC3F ( hA3F ) and APOBEC3G ( hA3G ) are antiretroviral cytidine deaminases that can be encapsidated during virus assembly to catalyze C > U deamination of the viral reverse transcripts in the next round of infection . ^^^ |
|
| Interacting proteins: Q9HC16 and Q8IUX4 |
Pubmed |
SVM Score :0.0 |
| The cytoplasmic single stranded DNA cytidine deaminases APOBEC3G and APOBEC3F block HIV replication by introducing premature stop codons into the viral genome . ^^^ |
|
| Interacting proteins: Q9HC16 and Q8IUX4 |
Pubmed |
SVM Score :0.0 |
| Comparative analysis of the antiretroviral activity of APOBEC3G and APOBEC3F from primates . ^^^ APOBEC3G and APOBEC3F exhibit antiretroviral activity primarily as a consequence of their ability to deaminate cytidines in retroviral DNA . ^^^ Here , we compare the properties of APOBEC3F and APOBEC3G from human , macaque , and African green monkey ( AGM ) . ^^^ While all APOBEC proteins tested exhibited anti HIV 1 activity , human APOBEC3F was , surprisingly , 10 to 50 fold less potent than human APOBEC3G . ^^^ Overall , highly efficient and species specific neutralization of APOBEC3G , and less efficient neutralization of APOBEC3F , appears to be a general property of Vif proteins . . ^^^ |
|
| Interacting proteins: Q9HC16 and Q8IUX4 |
Pubmed |
SVM Score :0.0 |
| Differential requirement for conserved tryptophans in human immunodeficiency virus type 1 Vif for the selective suppression of APOBEC3G and APOBEC3F . ^^^ APOBEC3G ( A3G ) and related cytidine deaminases , such as APOBEC3F ( A3F ) , are potent inhibitors of retroviruses . ^^^ |
|
| Interacting proteins: Q9HC16 and Q8IUX4 |
Pubmed |
SVM Score :0.0 |
| Members of this family ( APOBEC3G and APOBEC3F ) have been recently shown to be able to restrict HIV 1 replication in physiologically relevant target cells ( macrophages , lymphocytes ) , presumably by triggering extensive deamination of the viral RNA / DNA replication intermediates . ^^^ |
|
| Interacting proteins: Q9HC16 and Q8IUX4 |
Pubmed |
SVM Score :0.0 |
| The human cytidine deaminases APOBEC3G ( hA3G ) and APOBEC3F ( hA3F ) are intracellular antiretroviral factors that can hypermutate nascent reverse transcripts and inhibit the replication of human immunodeficiency virus type 1 ( HIV 1 ) . ^^^ |
|
| Interacting proteins: Q9HC16 and Q8IUX4 |
Pubmed |
SVM Score :0.0 |
| APOBEC3G and APOBEC3F restrict human immunodeficiency virus type 1 ( HIV 1 ) replication in vitro through the induction of G > A hypermutation ; however , the relevance of this host antiviral strategy to clinical HIV 1 is currently not known . ^^^ G > A hypermutation conforming to expected APOBEC3G polynucleotide sequence preferences was inferred in 9 . 4 % ( n = 12 ) of the HIV 1 sequences , with a further 2 . 4 % ( n = 3 ) conforming to APOBEC3F , and was independently associated with reduced pretreatment viremia ( reduction of 0 . 7 log ( 10 ) copies / ml ; P = 0 . 001 ) . ^^^ |
|