A Potent and Broad Neutralizing Antibody Recognizes and Penetrates the HIV Glycan Shield
2012; Wiley; Volume: 26; Issue: S1 Linguagem: Inglês
10.1096/fasebj.26.1_supplement.lb263
ISSN1530-6860
AutoresGrant Abass, Ashley Arnell, Noah Barkley, Warren Chick, Nick Ciling, Ian Hammers, Rachel Hodo, Serena Hughes, Ellie Nalaboff, Amy Rodriguez, Noah Trimmer, Savanna VandenHeuvel, Gretchen Schultz, Jean‐Philippe Julien, Ian A. Wilson,
Tópico(s)Glycosylation and Glycoproteins Research
ResumoHIV has evolved many mechanisms to avoid antibody recognition, but one neutralizing antibody, PGT128, is able to recognize the virus and prevent HIV infection. The Murrieta Mesa SMART Team (Students Modeling A Research Topic) modeled PGT128 using 3D printing technology. PGT128 binds to glycans, which are sugars on the viral surface of the HIV envelope protein gp120. The gp120 molecule has a binding site that modulates attachment to the CD4 receptor on human CD4 T cells. Binding of gp120 to these cells leads to membrane fusion between the human cell and HIV. It is this initial infection that ultimately causes AIDS. The function of the PGT128 antibody is to coat gp120 by binding to two glycans on the HIV glycan shield. A glycan shield refers to sugars that protect glycoproteins from recognition by the human immune system. After PGT128 infiltrates the HIV glycan coat, it interacts with a specific part of gp120, the V3 loop, thus preventing membrane fusion and HIV infection. The antibody is thought to be able to bind two separate gp120 molecules via a cross linking mechanism. PGT128 is known to be a broad neutralizer, which means that the antibody can deactivate many different strains of HIV. Since PGT128 is able to neutralize 72% of circulating viruses, there is the possibility a vaccine can be generated for HIV. Supported by a grant from the HHMI Pre‐ College program.
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