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* Residue conservation analysis
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DOI no:
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Proc Natl Acad Sci U S A
98:11181-11186
(2001)
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PubMed id:
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X-ray structures of H5 avian and H9 swine influenza virus hemagglutinins bound to avian and human receptor analogs.
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Y.Ha,
D.J.Stevens,
J.J.Skehel,
D.C.Wiley.
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ABSTRACT
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The three-dimensional structures of avian H5 and swine H9 influenza
hemagglutinins (HAs) from viruses closely related to those that caused outbreaks
of human disease in Hong Kong in 1997 and 1999 were determined bound to avian
and human cell receptor analogs. Emerging influenza pandemics have been
accompanied by the evolution of receptor-binding specificity from the preference
of avian viruses for sialic acid receptors in alpha2,3 linkage to the preference
of human viruses for alpha2,6 linkages. The four new structures show that HA
binding sites specific for human receptors appear to be wider than those
preferring avian receptors and how avian and human receptors are distinguished
by atomic contacts at the glycosidic linkage. alpha2,3-Linked sialosides bind
the avian HA in a trans conformation to form an alpha2,3 linkage-specific motif,
made by the glycosidic oxygen and 4-OH of the penultimate galactose, that is
complementary to the hydrogen-bonding capacity of Gln-226, an avian-specific
residue. alpha2,6-Linked sialosides bind in a cis conformation, exposing the
glycosidic oxygen to solution and nonpolar atoms of the receptor to Leu-226, a
human-specific residue. The new structures are compared with previously reported
crystal structures of HA/sialoside complexes of the H3 subtype that caused the
1968 Hong Kong Influenza virus pandemic and analyzed in relation to HA sequences
of all 15 subtypes and to receptor affinity data to make clearer how
receptor-binding sites of HAs from avian viruses evolve as the virus adapts to
humans.
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Selected figure(s)
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Figure 3.
Fig. 3. Atomic interactions between H5, H9, and H3 HAs
and sialosides. (a) Potential hydrogen bonds (dashed red)
between LSTc and the swine H9 HA. (b) Comparison of the binding
of LSTc (  2,6) with
the 1999 swine H9 (red) and 1968 human H3 (blue) subtype HA.
Purple circles, common contacts; blue, H3 contacts; red, H9
contacts. (c) Comparison of the binding of LSTa ( 2,3) with
the 1997 avian H5 (green), 1999 swine H9 (red), and 1968 human
H3 (blue) subtype HAs. Purple circles, common contacts; blue, H3
contacts; green, H5 contacts; red, H9 contacts.
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Figure 4.
Fig. 4. Swine H9 and human H3 HA binding sites preferring
2,6
linkages are wider than avian H5 preferring 2,3. The H9
swine (gray), H3 human (green), and H5 avian (white) 226/228
loops are superimposed, showing that the H5 avian 220s loop
(Gln-226/Gly-228) is closer to the opposing 130s loop than the
H9 swine (Leu-226/Gly-228) or H3 human (Leu-226/Ser-228).
Contact between Ala-138 and the lower methyl group of Leu-226
requires a more "open" site. The glycosidic oxygen of sialic
acid (atom colors) is labeled with an asterisk. A water molecule
(red sphere) mediates interactions between the amide group of
Gly-228 and the 8- and 9-OHs of sialic acid in H9 swine and H5
avian HAs. The hydroxyl group of Ser-228 "replaces" the water
molecule to form a hydrogen bond with 9-OH in the H3 human HA.
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Figures were
selected
by an automated process.
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PDB codes:
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R.J.Russell,
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T.Nandi
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PDB codes:
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S.Hanashima,
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The structure of H5N1 avian influenza neuraminidase suggests new opportunities for drug design.
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Nature,
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PDB codes:
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S.Yamada,
Y.Suzuki,
T.Suzuki,
M.Q.Le,
C.A.Nidom,
Y.Sakai-Tagawa,
Y.Muramoto,
M.Ito,
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K.Shinya,
T.Sawada,
M.Kiso,
T.Usui,
T.Murata,
Y.Lin,
A.Hay,
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J.J.Skehel,
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Haemagglutinin mutations responsible for the binding of H5N1 influenza A viruses to human-type receptors.
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Nature,
444,
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PDB code:
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Y.Muramoto,
T.Q.Le,
L.S.Phuong,
T.Nguyen,
T.H.Nguyen,
Y.Sakai-Tagawa,
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T.Horimoto,
H.Kida,
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J Virol,
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New genotype of avian influenza H5N1 viruses isolated from tree sparrows in China.
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J Virol,
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H.T.Long,
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N.V.Kaverin,
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Proc Natl Acad Sci U S A,
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Role of quail in the interspecies transmission of H9 influenza A viruses: molecular changes on HA that correspond to adaptation from ducks to chickens.
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J Virol,
77,
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K.S.Li,
K.M.Xu,
J.S.Peiris,
L.L.Poon,
K.Z.Yu,
K.Y.Yuen,
K.F.Shortridge,
R.G.Webster,
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Characterization of H9 subtype influenza viruses from the ducks of southern China: a candidate for the next influenza pandemic in humans?
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J Virol,
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Y.Ha,
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H5 avian and H9 swine influenza virus haemagglutinin structures: possible origin of influenza subtypes.
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EMBO J,
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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.
|
 |
Links
