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Science
334:1097-1103
(2011)
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PubMed id:
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A potent and broad neutralizing antibody recognizes and penetrates the HIV glycan shield.
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R.Pejchal,
K.J.Doores,
L.M.Walker,
R.Khayat,
P.S.Huang,
S.K.Wang,
R.L.Stanfield,
J.P.Julien,
A.Ramos,
M.Crispin,
R.Depetris,
U.Katpally,
A.Marozsan,
A.Cupo,
S.Maloveste,
Y.Liu,
R.McBride,
Y.Ito,
R.W.Sanders,
C.Ogohara,
J.C.Paulson,
T.Feizi,
C.N.Scanlan,
C.H.Wong,
J.P.Moore,
W.C.Olson,
A.B.Ward,
P.Poignard,
W.R.Schief,
D.R.Burton,
I.A.Wilson.
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ABSTRACT
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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.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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D.C.Ekiert,
A.K.Kashyap,
J.Steel,
A.Rubrum,
G.Bhabha,
R.Khayat,
J.H.Lee,
M.A.Dillon,
R.E.O'Neil,
A.M.Faynboym,
M.Horowitz,
L.Horowitz,
A.B.Ward,
P.Palese,
R.Webby,
R.A.Lerner,
R.R.Bhatt,
and
I.A.Wilson
(2012).
Cross-neutralization of influenza A viruses mediated by a single antibody loop.
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Nature,
489,
526-532.
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PDB codes:
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P.C.Wilson,
and
S.F.Andrews
(2012).
Tools to therapeutically harness the human antibody response.
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Nat Rev Immunol,
12,
709-719.
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Y.Mao,
L.Wang,
C.Gu,
A.Herschhorn,
S.H.Xiang,
H.Haim,
X.Yang,
and
J.Sodroski
(2012).
Subunit organization of the membrane-bound HIV-1 envelope glycoprotein trimer.
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Nat Struct Mol Biol,
19,
893-899.
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J.S.McLellan,
M.Pancera,
C.Carrico,
J.Gorman,
J.P.Julien,
R.Khayat,
R.Louder,
R.Pejchal,
M.Sastry,
K.Dai,
S.O'Dell,
N.Patel,
S.Shahzad-ul-Hussan,
Y.Yang,
B.Zhang,
T.Zhou,
J.Zhu,
J.C.Boyington,
G.Y.Chuang,
D.Diwanji,
I.Georgiev,
Y.D.Kwon,
D.Lee,
M.K.Louder,
S.Moquin,
S.D.Schmidt,
Z.Y.Yang,
M.Bonsignori,
J.A.Crump,
S.H.Kapiga,
N.E.Sam,
B.F.Haynes,
D.R.Burton,
W.C.Koff,
L.M.Walker,
S.Phogat,
R.Wyatt,
J.Orwenyo,
L.X.Wang,
J.Arthos,
C.A.Bewley,
J.R.Mascola,
G.J.Nabel,
W.R.Schief,
A.B.Ward,
I.A.Wilson,
and
P.D.Kwong
(2011).
Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9.
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Nature,
480,
336-343.
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PDB codes:
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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Links
