Saintedym WillsKwan Ki HwangPinghuang LiuS. Moses DennisonMatthew Zirui TayXiaoying ShenJustin PollaraJudith T. LucasRobert ParksSupachai Rerks-NgarmPunnee PitisuttithumSorachai NitayapanJaranit KaewkungwalRasmi ThomasJerome H. KimNelson L. MichaelMerlin L. RobbMike McRavenDavid C. MontefioriThomas J. HopeHua Xin LiaoM. Anthony MoodyGuido FerrariBarton F. HaynesS. Munir AlamMattia BonsignoriGeorgia D. TomarasDuke University Medical CenterInternational Vaccine Institute, SeoulChinese Academy of Agricultural SciencesThailand Ministry of Public HealthHJFNorthwestern University Feinberg School of MedicineWalter Reed Army Institute of ResearchMahidol UniversityRoyal Thai Army2019-08-232019-08-232018-04-01Journal of Virology. Vol.92, No.7 (2018)109855140022538X2-s2.0-85043792777https://repository.li.mahidol.ac.th/handle/123456789/44790© 2018 American Society for Microbiology. Vaccine-elicited humoral immune responses comprise an array of antibody forms and specificities, with only a fraction contributing to protective host immunity. Elucidation of antibody effector functions responsible for protective immunity against human immunodeficiency virus type 1 (HIV-1) acquisition is a major goal for the HIV-1 vaccine field. Immunoglobulin A (IgA) is an important part of the host defense against pathogens; however, little is known about the role of vaccineelicited IgA and its capacity to mediate antiviral functions. To identify the antiviral functions of HIV-1-specific IgA elicited by vaccination, we cloned HIV-1 envelopespecific IgA monoclonal antibodies (MAbs) by memory B cell cultures from peripheral blood mononuclear cells from an RV144 vaccinee and produced two IgA clonal cell lines (HG129 and HG130) producing native, nonrecombinant IgA MAbs. The HG129 and HG130 MAbs mediated phagocytosis by monocytes, and HG129 blocked HIV-1 Env glycoprotein binding to galactosylceramide, an alternative HIV-1 receptor. These findings elucidate potential antiviral functions of vaccine-elicited HIV-1 envelope-specific IgA that may act to block HIV-1 acquisition at the portal of entry by preventing HIV-1 binding to galactosylceramide and mediating antibody Fc receptor-mediated virion phagocytosis. Furthermore, these findings highlight the complex and diverse interactions of vaccine-elicited IgA with pathogens that depend on IgA fine specificity and form (e.g., multimeric or monomeric) in the systemic circulation and mucosal compartments.Mahidol UniversityAgricultural and Biological SciencesImmunology and MicrobiologyArticleSCOPUS10.1128/JVI.01552-17