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PDBsum entry 6cmi
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Viral protein/immune system
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PDB id
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6cmi
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Contents |
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428 a.a.
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213 a.a.
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228 a.a.
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PDB id:
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| Name: |
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Viral protein/immune system
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Title:
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Crystal structure of the hendra virus attachment g glycoprotein bound to a potent cross-reactive neutralizing human monoclonal antibody m102.3
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Structure:
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Glycoprotein g. Chain: b. Engineered: yes. M102.3 light chain. Chain: c. Engineered: yes. Igg heavy chain. Chain: d. Engineered: yes
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Source:
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Hendra virus. Isolate horse/autralia/hendra/1994. Organism_taxid: 928303. Expressed in: homo sapiens. Expression_system_taxid: 9606. Homo sapiens. Human. Organism_taxid: 9606. Expression_system_taxid: 9606
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Resolution:
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2.72Å
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R-factor:
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0.198
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R-free:
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0.246
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Authors:
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K.Xu,D.Nikolov
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Key ref:
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K.Xu
et al.
(2013).
Crystal structure of the Hendra virus attachment G glycoprotein bound to a potent cross-reactive neutralizing human monoclonal antibody.
PLoS Pathog,
9,
e1003684.
PubMed id:
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Date:
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05-Mar-18
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Release date:
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18-Apr-18
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PROCHECK
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Headers
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References
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O89343
(GLYCP_HENDH) -
Glycoprotein G from Hendra virus (isolate Horse/Autralia/Hendra/1994)
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Seq:
Struc:
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604 a.a.
428 a.a.
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PLoS Pathog
9:e1003684
(2013)
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PubMed id:
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Crystal structure of the Hendra virus attachment G glycoprotein bound to a potent cross-reactive neutralizing human monoclonal antibody.
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K.Xu,
B.Rockx,
Y.Xie,
B.L.DeBuysscher,
D.L.Fusco,
Z.Zhu,
Y.P.Chan,
Y.Xu,
T.Luu,
R.Z.Cer,
H.Feldmann,
V.Mokashi,
D.S.Dimitrov,
K.A.Bishop-Lilly,
C.C.Broder,
D.B.Nikolov.
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ABSTRACT
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The henipaviruses, represented by Hendra (HeV) and Nipah (NiV) viruses are
highly pathogenic zoonotic paramyxoviruses with uniquely broad host tropisms
responsible for repeated outbreaks in Australia, Southeast Asia, India and
Bangladesh. The high morbidity and mortality rates associated with infection and
lack of licensed antiviral therapies make the henipaviruses a potential
biological threat to humans and livestock. Henipavirus entry is initiated by the
attachment of the G envelope glycoprotein to host cell membrane receptors.
Previously, henipavirus-neutralizing human monoclonal antibodies (hmAb) have
been isolated using the HeV-G glycoprotein and a human naïve antibody library.
One cross-reactive and receptor-blocking hmAb (m102.4) was recently demonstrated
to be an effective post-exposure therapy in two animal models of NiV and HeV
infection, has been used in several people on a compassionate use basis, and is
currently in development for use in humans. Here, we report the crystal
structure of the complex of HeV-G with m102.3, an m102.4 derivative, and
describe NiV and HeV escape mutants. This structure provides detailed insight
into the mechanism of HeV and NiV neutralization by m102.4, and serves as a
blueprint for further optimization of m102.4 as a therapeutic agent and for the
development of entry inhibitors and vaccines.
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Links
