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TitleA potent and broad neutralizing antibody recognizes and penetrates the HIV glycan shield.
Journal, issue, pagesScience, Vol. 334, Issue 6059, Page 1097-1103, Year 2011
Publish dateNov 25, 2011
AuthorsRobert Pejchal / Katie J Doores / Laura M Walker / Reza Khayat / Po-Ssu Huang / Sheng-Kai Wang / Robyn L Stanfield / Jean-Philippe Julien / Alejandra Ramos / Max Crispin / Rafael Depetris / Umesh Katpally / Andre Marozsan / Albert Cupo / Sebastien Maloveste / Yan Liu / Ryan McBride / Yukishige Ito / Rogier W Sanders / Cassandra Ogohara / James C Paulson / Ten Feizi / Christopher N Scanlan / Chi-Huey Wong / John P Moore / William C Olson / Andrew B Ward / Pascal Poignard / William R Schief / Dennis R Burton / Ian A Wilson /
PubMed AbstractThe HIV envelope (Env) protein gp120 is protected from antibody recognition by a dense glycan shield. However, several of the recently identified PGT broadly neutralizing antibodies appear to ...The HIV envelope (Env) protein gp120 is protected from antibody recognition by a dense glycan shield. However, several of the recently identified PGT broadly neutralizing antibodies appear to interact directly with the HIV glycan coat. Crystal structures of antigen-binding fragments (Fabs) PGT 127 and 128 with Man(9) at 1.65 and 1.29 angstrom resolution, respectively, and glycan binding data delineate a specific high mannose-binding site. Fab PGT 128 complexed with a fully glycosylated gp120 outer domain at 3.25 angstroms reveals that the antibody penetrates the glycan shield and recognizes two conserved glycans as well as a short β-strand segment of the gp120 V3 loop, accounting for its high binding affinity and broad specificity. Furthermore, our data suggest that the high neutralization potency of PGT 127 and 128 immunoglobulin Gs may be mediated by cross-linking Env trimers on the viral surface.
External linksScience / PubMed:21998254 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.29 - 14.0 Å
Structure data

EMDB-1970:
Negative stained image reconstruction of HIV spike protein in complex with PGT128 Fab at 14 Angstrom resolution
Method: EM (single particle) / Resolution: 14.0 Å

PDB-3tv3:
Crystal structure of broad and potent HIV-1 neutralizing antibody PGT128 in complex with Man9
Method: X-RAY DIFFRACTION / Resolution: 1.29 Å

PDB-3twc:
Crystal structure of broad and potent HIV-1 neutralizing antibody PGT127 in complex with Man9
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

PDB-3tyg:
Crystal structure of broad and potent HIV-1 neutralizing antibody PGT128 in complex with a glycosylated engineered gp120 outer domain with miniV3 (eODmV3)
Method: X-RAY DIFFRACTION / Resolution: 3.25 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-AML:
AMYLAMINE

ChemComp-EPE:
4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID / pH buffer*YM

ChemComp-HOH:
WATER

Source
  • Human immunodeficiency virus
  • homo sapiens (human)
  • human immunodeficiency virus 1
KeywordsIMMUNE SYSTEM / Fab / HIV-1 neutralizing antibody / gp120 / VIRAL PROTEIN / HIV-1 / Env

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