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About the Authors:
Catarina E. Hioe
* E-mail: [email protected]
Affiliations Department of Pathology, New York University Langone School of Medicine, New York, New York, United States of America, Veterans Affairs New York Harbor Healthcare System, New York, New York, United States of America
Terri Wrin
Affiliation: Monogram Biosciences, Inc., South San Francisco, California, United States of America
Michael S. Seaman
Affiliation: Department of Medicine, Division of Viral Pathogenesis, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, Massachusetts, United States of America
Xuesong Yu
Affiliation: Public Health Sciences Division, Statistical Center for HIV/AIDS Research and Prevention, Fred Hutchinson Cancer Research Center, Seattle, Washington, United States of America
Blake Wood
Affiliation: Public Health Sciences Division, Statistical Center for HIV/AIDS Research and Prevention, Fred Hutchinson Cancer Research Center, Seattle, Washington, United States of America
Steve Self
Affiliation: Public Health Sciences Division, Statistical Center for HIV/AIDS Research and Prevention, Fred Hutchinson Cancer Research Center, Seattle, Washington, United States of America
Constance Williams
Affiliation: Department of Pathology, New York University Langone School of Medicine, New York, New York, United States of America
Miroslaw K. Gorny
Affiliation: Department of Pathology, New York University Langone School of Medicine, New York, New York, United States of America
Susan Zolla-Pazner
Affiliations Department of Pathology, New York University Langone School of Medicine, New York, New York, United States of America, Veterans Affairs New York Harbor Healthcare System, New York, New York, United States of America
Introduction
Gp120, the surface subunit of the HIV-1 envelope (Env) glycoprotein, is a critical target for antibodies (Abs) that neutralize the virus and prevent infection (reviewed in [1]). Gp120 is bound non-covalently to the transmembrane subunit gp41, and the two glycoproteins are expressed on the virion surface as heterotrimers. Gp120 serves as the virus attachment protein by binding to CD4 and the chemokine receptors CCR5 or CXCR4. Because of these crucial functions in the virus infectious process, it is logical that gp120 is a desired target for neutralizing Abs. However, gp120 displays astonishing agility in evading Ab neutralization [2], [3], [4], [5], [6]. Indeed, HIV-1 gp120 is notorious for its genetic and antigenic variability, while at the same time, its conserved regions are poorly immunogenic and/or are not accessible on the surface of the virion at all times [5],...