About: Structural and functional analysis of the hemagglutinin-esterase of infectious salmon anaemia virus

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: Structural and functional analysis of the hemagglutinin-esterase of infectious salmon anaemia virus 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
title	Structural and functional analysis of the hemagglutinin-esterase of infectious salmon anaemia virus
Creator	Markussen, Turhan Drabløs, Finn Mjaaland, Siri Gjøen, Tor Jørgensen, Trond Müller, Anita Solem, Stein
source	Elsevier; Medline; PMC
abstract	Abstract Infectious salmon anaemia virus (ISAV) is a piscine orthomyxovirus causing a serious disease in farmed Atlantic salmon (Salmo salar L.). The virus surface glycoprotein hemagglutinin-esterase (HE) is responsible for both viral attachment and release. Similarity to bovine and porcine torovirus hemagglutinin-esterase (BToV HE, PToV HE), bovine coronavirus HE (BCoV HE) and influenza C hemagglutinin-esterase-fusion (InfC HEF) proteins were exploited in a computational homology-based structure analysis of ISAV HE. The analysis resolved structural aspects of the protein and identified important features of relevance to ISAV HE activity. By recombinant expression and purification of secretory HE (recHE) proteins, receptor-binding and quantitative analyses of enzymatic activities displayed by ISAV HE molecules are presented for the first time. Three different recHE molecules were constructed: one representing a high virulent isolate, one a low virulent, while in the third a Ser32 to Ala32 amino acid substitution was introduced in the enzymatic catalytic site as inferred from the model. The three amino acid differences between the high and low virulent variants, of which two localized to the putative receptor-binding domain and one in the esterase domain, had no impact on receptor-binding or -release activities. In contrast, the Ser32 amino acid substitution totally abolished enzymatic activity while receptor binding increased, as observed by agglutination of Atlantic salmon red blood cells. This demonstrates the essential role of a serine in the enzyme's catalytic site. In conclusion, structural analysis of ISAV HE in combination with selected recHE proteins gave insights into structure–function relationships and opens up for further studies aiming at dissecting molecular determinants of ISAV virulence.
has issue date	2010-08-31(xsd:dateTime)
bibo:doi	10.1016/j.virusres.2010.03.020
bibo:pmid	20398710
has license	els-covid
sha1sum (hex)	ae402e29204598d16eb615bd596149839b79155b
schema:url	https://doi.org/10.1016/j.virusres.2010.03.020
resource representing a document's title	Structural and functional analysis of the hemagglutinin-esterase of infectious salmon anaemia virus
has PubMed Central identifier	PMC7114507
has PubMed identifier	20398710
schema:publication	Virus Research
resource representing a document's body	covid:ae402e29204598d16eb615bd596149839b79155b#body_text
is schema:about of	named entity 'RECEPTOR' named entity 'RECEPTOR BINDING' named entity 'OBSERVED' named entity 'CONTRAST' named entity 'RELEASE' named entity 'STRUCTURE ANALYSIS' named entity 'SERINE' named entity 'PRESENTED' named entity 'PURIFICATION' named entity 'LOW' named entity 'IMPACT' named entity '27S' named entity 'DIFFERENT' named entity 'DISSECTING' named entity 'STRUCTURAL' named entity 'ESSENTIAL' named entity 'MODEL' named entity 'ROLE' named entity 'DISEASE' named entity 'ABOLISHED ENZYMATIC ACTIVITY' named entity 'STRUCTURAL ANALYSIS' named entity 'VIRULENCE' named entity 'SER' named entity 'DISPLAYED' named entity 'INFECTIOUS SALMON ANAEMIA VIRUS' named entity 'ENZYMATIC' named entity 'RED BLOOD CELLS' named entity 'ESTERASE' named entity 'INFECTIOUS SALMON ANAEMIA VIRUS' named entity 'SALAR' named entity 'ANALYSIS' named entity 'ISOLATE' named entity 'AMINO ACID SUBSTITUTION' named entity 'FEATURES' named entity 'ACTIVITY' named entity 'COMBINATION' named entity 'FUNCTION' named entity 'ESTERASE' named entity 'SELECTED' named entity 'PROTEINS' named entity 'RESPONSIBLE' named entity 'MOLECULAR' named entity 'TIME' named entity 'CONCLUSION' named entity 'VIRAL ATTACHMENT' named entity 'ACTIVITIES' named entity 'FUNCTIONAL ANALYSIS' named entity 'HEMAGGLUTININ' named entity 'STRUCTURAL' named entity 'INFERRED' named entity 'STUDIES' named entity 'ENZYME' named entity 'BINDING' named entity 'AMINO ACID' named entity 'DETERMINANTS' named entity 'CAUSING' named entity 'OPENS' named entity 'INSIGHTS' named entity 'INCREASED' named entity 'TOTALLY' named entity 'QUANTITATIVE' named entity 'IMPORTANT' named entity 'INTRODUCED' named entity 'HIGH' named entity 'SIMILARITY' named entity 'IS A' named entity 'LOCALIZED' named entity 'STRUCTURE' named entity 'RELEVANCE' named entity 'ALA' named entity 'IDENTIFIED' named entity 'GAVE' named entity 'ATLANTIC SALMON' named entity 'HOMOLOGY' named entity 'FUSION'

Faceted Search & Find service v1.13.91 as of Mar 24 2020

Alternative Linked Data Documents: Sponger | ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3229 as of Jul 10 2020, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (94 GB total memory)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2025 OpenLink Software