人类22号染色体编码了7个具有抗反转录病毒和抗反转录元件功能的胞嘧啶脱氨酶，可以使病毒反转录过程中产生的负链DNA上的胞嘧啶脱氨基变成尿嘧啶，导致正链DNA上出现G→A的突变，即APOBEC3。APOBEC3都有一个或两个催化域，而每个催化域都有保守基序HX₁EX_23-24CX_2-4C。APOBEC3H是唯一一个含有Z3 APOBEC脱氨酶域的蛋白。在外周单核细胞，肝脏、皮肤等不同组织均已检测到APOBE3H的单倍型，包括HapⅠ、HapⅡ、HapⅢ、HapⅣ、HapⅤ、HapⅥ和HapⅦ。不同的APOBEC3H单倍型具有不同的抗病毒功能。APOBEC3H可显著地抑制HIV-1的复制，优化APOBEC3H的体内表达水平，可成为一种治疗HIV-1的新对策。

[1] 利维.艾滋病病毒与艾滋病的发病机制[M].3版.邵一鸣,译.北京:科学出版社,2010:1-27.
[2] DANG Y,SIEW L M,WANG X,et al.Human cytidine deaminase APOBEC3H restricts HIV-1 replication[J].J Biol Chem,2008,283(17):11606-11614.
[3] WANG X,ABUDU A,SON S,et al.Analysis of human APOBEC3H haplotypes and anti-human immunodeficiency virus type 1 activity[J].J Virol,2011,85(7):3142-3152.
[4] ZHEN A,DU J,ZHOU X,et al.Reduced APOBEC3H variant anti-viral activities are associated with altered RNA binding activities[J].PLoS One,2012,7(7):e38771.
[5] MITRA M,SINGER D,MANO Y,et al.Sequence and structural determinants of human APOBEC3H deaminase and anti-HIV-1 activities[J/OL].Retrovirology,2015,12:3[2015-1-22].http://retrovirology.biomedcentral.com/articles/10.1186/s12977-014-0130-8.
[6] IZUMI T,SHIRAKAWA K,TAKAORI-KONDO A.Cytidine deaminases as a weapon against retroviruses and a new target for antiviral therapy[J].Mini Rev Med Chem,2008,8(3):231-238.
[7] VIEIRA V C,SOARES M A.The role of cytidine deaminases on innate immune responses against human viral infections[J].Biomed Res Int,2013,2013:e683095.
[8] SHEEHY A M,GADDIS N C,CHOI J D,et al.Isolation of a human gene that inhabites HIV-1 infecton and is suppressed by the viral Vif protein[J].Nature,2002,418(6898):646-650.
[9] LI M M,EMERMAN M.Polymorphism in human APOBEC3H affects a phenotype dominant for subcellular localization and antiviral activity[J].J Virol,2011,85(16):8197-8207.
[10] HARARI A,OOMS M,MULDER L C,et al.Polymorphisms and splice variants influence the antiretroviral activity of human APOBEC3H[J].J Virol,2009,83(1):295-303.
[11] FENG Y,LOVE R P,ARA A,et al.Natural polymorphisms and oligomerization of human APOBEC3H contribute to single-stranded DNA scanning ability[J].J Biol Chem,2015,290(45):27188-27203.
[12] REFSLAND E W,HULTQUIST J F,LUENGAS E M,et al.Natural polymorphisms in human APOBEC3H and HIV-1 Vif combine in primary T lymphocytes to affect viral G-to-A mutation levels and infectivity[J].PLoS Genet,2014,10(11):e1004761.
[13] GOILA-GAUR R,STREBEL K.HIV-1 Vif,APOBEC,and Intrinsic Immunity[J/OL].Retrovirology,2008,5:51[2008-06-24].http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2443170.
[14] VASUDEVAN A A,SMITS S H,HÖPPNER A,et al.Structure features of antiviral DNA cytidine deaminases[J].Biol Chem,2013,394(11):1357-1370.
[15] OOMS M,MAJDAK S,SEIBERT C W,et al.The localization of APOBEC3H variants in HIV-1 virions determines their antiviral activity[J].J Virol,2010,84(16):7961-7969.
[16] NARUSE T K,SAKURAI D,OHTANI H,et al.APOBEC3H polymorphisms and susceptibility to HIV-1 infection in an Indian population[J].J Hum Genet,2016,61(3):263-265.
[17] LI M M,WU L I,EMERMAN M.The range of human APOBEC3H sensitivity to lentiviral vif proteins[J].J Virol,2010,84(1):88-95.
[18] CAGLIANI R,RIVA S,FUMAGALLI M,et al.A Positively selected APOBEC3H haplotype is associated with natural resistance to HIV-1 infection[J].Evolution,2011,65(11):3311-3322.
[19] GOURRAUD P A,KARAOUNI A,WOO J M,et al.APOBEC3H haplotype and HIV-1 proviral vif DNA sequence diversity in early untreated infection[J].Hum Immunol,2011,72(3):207-212.
[20] LARUE R S,LENGYEL J,JÓNSSON S R,et al.Lentiviral vif degrades the APOBEC3Z3/APOBEC3H protein of its mammalian host and is capable of cross-species activity[J].J Virol,2010,84(16):8193-8201.
[21] ZHAO K,DU J,RUI Y,et al.Evolutionarily conserved pressure for the existence of distinct G2/M cell cycle arrest and A3H inactivation functions in HIV-1 Vif[J].Cell Cycle,2015,14(6):838-847.
[22] ZHU M,WANG Y,WANG C,et al.The eQTL-missense polymorphisms of APOBEC3H are associated with lung cancer risk in a Han Chinese population[J/OL].Sci Rep,2015,5:14969[2015-10-13].http://www.ncbi.nlm.nih.gov/pubmed/26459911.