2fk0: Difference between revisions

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==Overview==

The hemagglutinin (HA) structure at 2.9 angstrom resolution, from a highly, pathogenic Vietnamese H5N1 influenza virus, is more related to the 1918, and other human H1 HAs than to a 1997 duck H5 HA. Glycan microarray, analysis of this Viet04 HA reveals an avian alpha2-3 sialic acid receptor, binding preference. Introduction of mutations that can convert H1 serotype, HAs to human alpha2-6 receptor specificity only enhanced or reduced, affinity for avian-type receptors. However, mutations that can convert, avian H2 and H3 HAs to human receptor specificity, when inserted onto the, Viet04 H5 HA framework, permitted binding to a natural human alpha2-6, glycan, which suggests a path for this H5N1 virus to gain a foothold in, the human population.

The hemagglutinin (HA) structure at 2.9 angstrom resolution, from a highly pathogenic Vietnamese H5N1 influenza virus, is more related to the 1918 and other human H1 HAs than to a 1997 duck H5 HA. Glycan microarray analysis of this Viet04 HA reveals an avian alpha2-3 sialic acid receptor binding preference. Introduction of mutations that can convert H1 serotype HAs to human alpha2-6 receptor specificity only enhanced or reduced affinity for avian-type receptors. However, mutations that can convert avian H2 and H3 HAs to human receptor specificity, when inserted onto the Viet04 H5 HA framework, permitted binding to a natural human alpha2-6 glycan, which suggests a path for this H5N1 virus to gain a foothold in the human population.

==About this Structure==

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[[Category: Protein complex]]

[[Category: Stevens, J.]]

[[Category: Wilson, I.A.]]

[[Category: Wilson, I A.]]

[[Category: glycoprotein]]

[[Category: membrane-fusion precursor]]

[[Category: virus/viral protein]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:22:08 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-The hemagglutinin (HA) structure at 2.9 angstrom resolution, from a highly, pathogenic Vietnamese H5N1 influenza virus, is more related to the 1918, and other human H1 HAs than to a 1997 duck H5 HA. Glycan microarray, analysis of this Viet04 HA reveals an avian alpha2-3 sialic acid receptor, binding preference. Introduction of mutations that can convert H1 serotype, HAs to human alpha2-6 receptor specificity only enhanced or reduced, affinity for avian-type receptors. However, mutations that can convert, avian H2 and H3 HAs to human receptor specificity, when inserted onto the, Viet04 H5 HA framework, permitted binding to a natural human alpha2-6, glycan, which suggests a path for this H5N1 virus to gain a foothold in, the human population.
+The hemagglutinin (HA) structure at 2.9 angstrom resolution, from a highly pathogenic Vietnamese H5N1 influenza virus, is more related to the 1918 and other human H1 HAs than to a 1997 duck H5 HA. Glycan microarray analysis of this Viet04 HA reveals an avian alpha2-3 sialic acid receptor binding preference. Introduction of mutations that can convert H1 serotype HAs to human alpha2-6 receptor specificity only enhanced or reduced affinity for avian-type receptors. However, mutations that can convert avian H2 and H3 HAs to human receptor specificity, when inserted onto the Viet04 H5 HA framework, permitted binding to a natural human alpha2-6 glycan, which suggests a path for this H5N1 virus to gain a foothold in the human population.
 ==About this Structure==
@@ Line 14: / Line 14: @@
 [[Category: Protein complex]]
 [[Category: Stevens, J.]]
-[[Category: Wilson, I.A.]]
+[[Category: Wilson, I A.]]
 [[Category: glycoprotein]]
 [[Category: membrane-fusion precursor]]
 [[Category: virus/viral protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 19:38:13 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:22:08 2008''