Mol. Cells 2012; 34(3): 231-237
Published online June 25, 2012
https://doi.org/10.1007/s10059-012-0104-4
© The Korean Society for Molecular and Cellular Biology
Correspondence to : *Correspondence: ryuse@hanyang.ac.kr (SER); wayne@convex.hhmi.columbia.edu (WAH)
Since the discovery more than 30 years ago of human immunodeficiency virus (HIV) as the causative agent of the deadly disease, acquired immune deficiency disease (AIDS), there have been no efficient vaccines against the virus. For the infection of the virus, the HIV surface glycoprotein gp120 first recognizes the CD4 receptor on the target helper T-cell, which initiates HIV fusion with the target cell and, if unchecked, leads to destruction of the patient’s immune system. Despite the difficulty of developing appropriate immune responses in HIV-infected individuals, patient sera often contain antibodies that have broad neutralization activity, indicating the possibility of immunolo-gical treatment and prevention. Recently, through extensive structural studies of neutralizing antibodies of HIV in complex with gp120, the critical mechanisms of broad neutralization against HIV have been elucidated. Based on these discoveries, the structure-aided designs of antibodies and novel scaffolds were performed to create extremely potent neutralizing antibodies against HIV. These new discoveries and advances shed light on the road to development of efficient immunological therapies against AIDS.
Keywords broadly neutralizing antibody, design, HIV, structure, vaccine
Mol. Cells 2012; 34(3): 231-237
Published online September 30, 2012 https://doi.org/10.1007/s10059-012-0104-4
Copyright © The Korean Society for Molecular and Cellular Biology.
Seong Eon Ryu1,2,*, and Wayne A. Hendrickson3,4,5,*
1Department of Bioengineering, College of Engineering, Hanyang University, Seoul 133-070, Korea, 2Institute of Biopharmaceutical Research, Hanyang University, Seoul 133-070, Korea, 3Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA, 4Depart-ment of Physiology and Cellular Biophysics, Columbia University, New York, NY 10032, USA, 5Howard Hughes Medical Institute, Columbia University, New York, NY 10032, USA
Correspondence to:*Correspondence: ryuse@hanyang.ac.kr (SER); wayne@convex.hhmi.columbia.edu (WAH)
Since the discovery more than 30 years ago of human immunodeficiency virus (HIV) as the causative agent of the deadly disease, acquired immune deficiency disease (AIDS), there have been no efficient vaccines against the virus. For the infection of the virus, the HIV surface glycoprotein gp120 first recognizes the CD4 receptor on the target helper T-cell, which initiates HIV fusion with the target cell and, if unchecked, leads to destruction of the patient’s immune system. Despite the difficulty of developing appropriate immune responses in HIV-infected individuals, patient sera often contain antibodies that have broad neutralization activity, indicating the possibility of immunolo-gical treatment and prevention. Recently, through extensive structural studies of neutralizing antibodies of HIV in complex with gp120, the critical mechanisms of broad neutralization against HIV have been elucidated. Based on these discoveries, the structure-aided designs of antibodies and novel scaffolds were performed to create extremely potent neutralizing antibodies against HIV. These new discoveries and advances shed light on the road to development of efficient immunological therapies against AIDS.
Keywords: broadly neutralizing antibody, design, HIV, structure, vaccine
Min Kyung Jung and Eui-Cheol Shin
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