About: IFITMs from Mycobacteria Confer Resistance to Influenza Virus When Expressed in Human Cells

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

About: IFITMs from Mycobacteria Confer Resistance to Influenza Virus When Expressed in Human Cells 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	IFITMs from Mycobacteria Confer Resistance to Influenza Virus When Expressed in Human Cells
Creator	Chesarino, Nicholas Hach, Jocelyn Mcmichael, Temet Melvin, William Yount, Jacob
Source	Medline; PMC
abstract	Interferon induced transmembrane proteins (IFITMs) found in vertebrates restrict infections by specific viruses. IFITM3 is known to be essential for restriction of influenza virus infections in both mice and humans. Vertebrate IFITMs are hypothesized to have derived from a horizontal gene transfer from bacteria to a primitive unicellular eukaryote. Since bacterial IFITMs share minimal amino acid identity with human IFITM3, we hypothesized that examination of bacterial IFITMs in human cells would provide insight into the essential characteristics necessary for antiviral activity of IFITMs. We examined IFITMs from Mycobacterium avium and Mycobacterium abscessus for potential antiviral activity. Both of these IFITMs conferred a moderate level of resistance to influenza virus in human cells, identifying them as functional homologues of IFITM3. Analysis of sequence elements shared by bacterial IFITMs and IFITM3 identified two hydrophobic domains, putative S-palmitoylation sites, and conserved phenylalanine residues associated with IFITM3 interactions, which are all necessary for IFITM3 antiviral activity. We observed that, like IFITM3, bacterial IFITMs were S-palmitoylated, albeit to a lesser degree. We also demonstrated the ability of a bacterial IFITM to co-immunoprecipitate with IFITM3 suggesting formation of a complex, and also visualized strong co-localization of bacterial IFITMs with IFITM3. However, the mycobacterial IFITMs lack the endocytic-targeting motif conserved in vertebrate IFITM3. As such, these bacterial proteins, when expressed alone, had diminished colocalization with cathepsin B-positive endolysosomal compartments that are the primary site of IFITM3-dependent influenza virus restriction. Though the precise evolutionary origin of vertebrate IFITMs is not known, our results support a model whereby transfer of a bacterial IFITM gene to eukaryotic cells may have provided a selective advantage against viral infection that was refined through the course of vertebrate evolution to include more robust signals for S-palmitoylation and localization to sites of endocytic virus trafficking.
has issue date	2015-06-12(xsd:dateTime)
bibo:doi	10.3390/v7062759
bibo:pmid	26075508
has license	cc-by
sha1sum (hex)	b02612aa65049060e0a24064db96105458ac083b
schema:url	https://doi.org/10.3390/v7062759
resource representing a document's title	IFITMs from Mycobacteria Confer Resistance to Influenza Virus When Expressed in Human Cells
has PubMed Central identifier	PMC4488726
has PubMed identifier	26075508
schema:publication	Viruses
resource representing a document's body	covid:b02612aa65049060e0a24064db96105458ac083b#body_text
is schema:about of	named entity 'VIRUSES' named entity 'POTENTIAL' named entity 'IMMUNOPRECIPITATE' named entity 'MYCOBACTERIUM ABSCESSUS' named entity 'VERTEBRATE' named entity 'FORMATION' named entity 'TARGETING' named entity '2015' named entity 'BIOCHEMICAL' named entity 'HUMANS' named entity 'MYCOBACTERIUM AVIUM' named entity 'IDENTIFYING' named entity 'SHARE' named entity 'AUTHORS' named entity 'HORIZONTAL GENE TRANSFER' named entity 'ROBUST' named entity 'SHARED' named entity 'SPECIFIC' named entity 'RESTRICTION' named entity 'DIMINISHED' named entity 'QUANTIFICATION' named entity 'PALMITOYLATION' named entity 'EXAMINED' named entity 'TRAFFICKING' named entity 'FUNCTIONAL' named entity 'ASSOCIATED WITH' named entity 'UNICELLULAR' named entity 'PALMITOYLATED' named entity 'ADVANTAGE' named entity 'SIGNALS' named entity 'THESE' named entity 'PRIMITIVE' named entity 'LIKE' named entity 'RESTRICT' named entity 'HAVE' named entity 'BACTERIAL' named entity 'NOT KNOWN' named entity 'DEGREE' named entity 'ELEMENTS' named entity 'INTERACTIONS' named entity 'NECESSARY' named entity 'INDUCED' named entity 'EXAMINATION' named entity 'LOCALIZATION' named entity 'HUMAN CELLS' named entity 'endocytic' named entity 'origin' named entity 'bacterial' named entity 'model' named entity 'S-palmitoylation' named entity 'viruses' named entity 'Virus' named entity 'EXPRESSED' named entity 'SITE OF' named entity 'INCLUDE' named entity 'MOTIF' named entity 'POSITIVE' named entity 'ABILITY' named entity 'EXPRESSED' named entity 'RESULTS' named entity 'INSIGHT' named entity 'EVOLUTION' named entity 'CO-LOCALIZATION' named entity 'CHARACTERISTICS' named entity 'MODEL' named entity 'OBSERVED' named entity 'SELECTIVE' named entity 'MODERATE LEVEL' named entity 'MYCOBACTERIAL' named entity 'MINIMAL' named entity 'OUR' named entity 'WRITTEN' named entity 'IFITM3' named entity 'INITIAL' named entity 'ORIGIN' named entity 'IDENTIFIED' named entity 'MANUSCRIPT'

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 © 2009-2024 OpenLink Software