About: The Evolutionary Pattern of Glycosylation Sites in Influenza Virus (H5N1) Hemagglutinin and Neuraminidase

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About: The Evolutionary Pattern of Glycosylation Sites in Influenza Virus (H5N1) Hemagglutinin and Neuraminidase Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	The Evolutionary Pattern of Glycosylation Sites in Influenza Virus (H5N1) Hemagglutinin and Neuraminidase
Creator	Li, Z Chen, W Qin, Y Sun, S Zhong, Y
Source	PMC
abstract	Two glycoproteins, hemagglutinin (HA) and neuraminidase (NA), on the surface of influenza viruses play crucial roles in transfaunation, membrane fusion and the release of progeny virions. To explore the distribution of N-glycosylation sites (glycosites) in these two glycoproteins, we collected and aligned the amino acid sequences of all the HA and NA subtypes. Two glycosites were located at HA0 cleavage sites and fusion peptides and were strikingly conserved in all HA subtypes, while the remaining glycosites were unique to their subtypes. Two to four conserved glycosites were found in the stalk domain of NA, but these are affected by the deletion of specific stalk domain sequences. Another highly conserved glycosite appeared at the top center of tetrameric global domain, while the others glycosites were distributed around the global domain. Here we present a detailed investigation of the distribution and the evolutionary pattern of the glycosites in the envelope glycoproteins of IVs, and further focus on the H5N1 virus and conclude that the glycosites in H5N1 have become more complicated in HA and less influential in NA in the last five years.
has issue date	2012-11-01(xsd:dateTime)
bibo:doi	10.1371/journal.pone.0049224
bibo:pmid	23133677
has license	cc-by
sha1sum (hex)	b79088a023db89b12d5630e426661985aba3921e
schema:url	https://doi.org/10.1371/journal.pone.0049224
resource representing a document's title	The Evolutionary Pattern of Glycosylation Sites in Influenza Virus (H5N1) Hemagglutinin and Neuraminidase
has PubMed Central identifier	PMC3486865
has PubMed identifier	23133677
schema:publication	PLoS One
resource representing a document's body	covid:b79088a023db89b12d5630e426661985aba3921e#body_text
is schema:about of	named entity 'sequences' named entity 'cleavage' named entity 'release' named entity 'conserved' named entity 'highly' named entity 'acid' named entity 'conserved' named entity 'Glycosylation' named entity 'Virus' named entity 'INFLUENZA VIRUS' named entity 'PRESENT' named entity 'CLEAVAGE' named entity 'DELETION' named entity 'NEURAMINIDASE' named entity 'RELEASE' named entity 'HIGHLY' named entity 'GLYCOSYLATION' named entity 'SITES' named entity 'DOMAIN' named entity 'REMAINING' covid:arg/b79088a023db89b12d5630e426661985aba3921e named entity 'AMINO ACID SEQUENCES' named entity 'CENTER' named entity 'COLLECTED' named entity 'HEMAGGLUTININ' named entity 'SEQUENCES' named entity 'DISTRIBUTION' named entity 'DISTRIBUTED' named entity 'NEURAMINIDASE' named entity 'FUSION' named entity 'ENVELOPE' named entity 'H5N1' named entity 'AFFECTED' named entity 'BUT' named entity 'INFLUENTIAL' named entity 'SITES' named entity 'PATTERN' named entity 'HAVE' named entity 'MEMBRANE FUSION' named entity 'COMPLICATED' named entity 'CONCLUDE' named entity 'GLOBAL' named entity 'ROLES' named entity 'PLAY' named entity 'SUBTYPES' named entity 'PATTERN' named entity 'IVS' named entity 'YEARS' named entity 'H5N1 VIRUS' named entity 'PROGENY' named entity 'SURFACE' named entity 'CONSERVED' named entity 'GLYCOPROTEINS' named entity 'DETAILED' named entity 'UNIQUE' named entity 'THESE' named entity 'VIRIONS' named entity 'PEPTIDES' named entity 'N-GLYCOSYLATION' named entity 'FOCUS' named entity 'THEIR' named entity 'ALIGNED ' named entity 'INVESTIGATION' named entity 'INFLUENZA VIRUSES' named entity 'SPECIFIC' named entity 'HEMAGGLUTININ' named entity 'HERE' named entity 'STALK' named entity 'FOUND' named entity 'N-glycosylation' named entity 'glycoproteins' named entity 'domain' named entity 'influenza' named entity 'fusion' named entity 'complicated' named entity 'stalk' named entity 'glycoproteins'

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