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Title: HIV-1- specific IgA monoclonal antibodies from an HIV-1 vaccinee mediate galactosylceramide blocking and phagocytosis
Authors: Saintedym Wills
Kwan Ki Hwang
Pinghuang Liu
S. Moses Dennison
Matthew Zirui Tay
Xiaoying Shen
Justin Pollara
Judith T. Lucas
Robert Parks
Supachai Rerks-Ngarm
Punnee Pitisuttithum
Sorachai Nitayapan
Jaranit Kaewkungwal
Rasmi Thomas
Jerome H. Kim
Nelson L. Michael
Merlin L. Robb
Mike McRaven
David C. Montefiori
Thomas J. Hope
Hua Xin Liao
M. Anthony Moody
Guido Ferrari
Barton F. Haynes
S. Munir Alam
Mattia Bonsignori
Georgia D. Tomaras
Duke University Medical Center
International Vaccine Institute, Seoul
Chinese Academy of Agricultural Sciences
Thailand Ministry of Public Health
Northwestern University Feinberg School of Medicine
Walter Reed Army Institute of Research
Mahidol University
Royal Thai Army
Keywords: Agricultural and Biological Sciences;Immunology and Microbiology
Issue Date: 1-Apr-2018
Citation: Journal of Virology. Vol.92, No.7 (2018)
Abstract: © 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.
ISSN: 10985514
Appears in Collections:Scopus 2018

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