Analysis of cathepsin and furin proteolytic enzymes involved in viral fusion protein activation in cells of the bat reservoir host.
Identifieur interne : 002A35 ( Ncbi/Checkpoint ); précédent : 002A34; suivant : 002A36Analysis of cathepsin and furin proteolytic enzymes involved in viral fusion protein activation in cells of the bat reservoir host.
Auteurs : Farah El Najjar [États-Unis] ; Levi Lampe [États-Unis] ; Michelle L. Baker [Australie] ; Lin-Fa Wang [Singapour] ; Rebecca Ellis Dutch [États-Unis]Source :
- PloS one [ 1932-6203 ] ; 2015.
Descripteurs français
- KwdFr :
- MESH :
- métabolisme : Cathepsines, Furine, Peptide hydrolases, Protéines de fusion virale, Protéines virales.
- virologie : Chiroptera.
- Animaux, Cellules Vero, Cricetinae, Lignée cellulaire.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Cathepsins, Furin, Peptide Hydrolases, Viral Fusion Proteins, Viral Proteins.
- virology : Chiroptera.
- Animals, Cell Line, Chlorocebus aethiops, Cricetinae, Vero Cells.
Abstract
Bats of different species play a major role in the emergence and transmission of highly pathogenic viruses including Ebola virus, SARS-like coronavirus and the henipaviruses. These viruses require proteolytic activation of surface envelope glycoproteins needed for entry, and cellular cathepsins have been shown to be involved in proteolysis of glycoproteins from these distinct virus families. Very little is currently known about the available proteases in bats. To determine whether the utilization of cathepsins by bat-borne viruses is related to the nature of proteases in their natural hosts, we examined proteolytic processing of several viral fusion proteins in cells derived from two fruit bat species, Pteropus alecto and Rousettus aegyptiacus. Our work shows that fruit bat cells have homologs of cathepsin and furin proteases capable of cleaving and activating both the cathepsin-dependent Hendra virus F and the furin-dependent parainfluenza virus 5 F proteins. Sequence analysis comparing Pteropus alecto furin and cathepsin L to proteases from other mammalian species showed a high degree of conservation; however significant amino acid variation occurs at the C-terminus of Pteropus alecto furin. Further analysis of furin-like proteases from fruit bats revealed that these proteases are catalytically active and resemble other mammalian furins in their response to a potent furin inhibitor. However, kinetic analysis suggests that differences may exist in the cellular localization of furin between different species. Collectively, these results indicate that the unusual role of cathepsin proteases in the life cycle of bat-borne viruses is not due to the lack of active furin-like proteases in these natural reservoir species; however, differences may exist between furin proteases present in fruit bats compared to furins in other mammalian species, and these differences may impact protease usage for viral glycoprotein processing.
DOI: 10.1371/journal.pone.0115736
PubMed: 25706132
Affiliations:
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: 000E57
- to stream PubMed, to step Curation: 000E57
- to stream PubMed, to step Checkpoint: 000E61
- to stream Ncbi, to step Merge: 002A35
- to stream Ncbi, to step Curation: 002A35
Links to Exploration step
pubmed:25706132Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Analysis of cathepsin and furin proteolytic enzymes involved in viral fusion protein activation in cells of the bat reservoir host.</title>
<author><name sortKey="El Najjar, Farah" sort="El Najjar, Farah" uniqKey="El Najjar F" first="Farah" last="El Najjar">Farah El Najjar</name>
<affiliation wicri:level="2"><nlm:affiliation>Department of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, Kentucky, United States of America.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, Kentucky</wicri:regionArea>
<placeName><region type="state">Kentucky</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Lampe, Levi" sort="Lampe, Levi" uniqKey="Lampe L" first="Levi" last="Lampe">Levi Lampe</name>
<affiliation wicri:level="2"><nlm:affiliation>Department of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, Kentucky, United States of America.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, Kentucky</wicri:regionArea>
<placeName><region type="state">Kentucky</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Baker, Michelle L" sort="Baker, Michelle L" uniqKey="Baker M" first="Michelle L" last="Baker">Michelle L. Baker</name>
<affiliation wicri:level="1"><nlm:affiliation>CSIRO Australian Animal Health Laboratory, East Geelong, Victoria, Australia.</nlm:affiliation>
<country xml:lang="fr">Australie</country>
<wicri:regionArea>CSIRO Australian Animal Health Laboratory, East Geelong, Victoria</wicri:regionArea>
<wicri:noRegion>Victoria</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Wang, Lin Fa" sort="Wang, Lin Fa" uniqKey="Wang L" first="Lin-Fa" last="Wang">Lin-Fa Wang</name>
<affiliation wicri:level="1"><nlm:affiliation>CSIRO Australian Animal Health Laboratory, East Geelong, Victoria, Australia; Program in Emerging Infectious Diseases, Duke-National University of Singapore Graduate Medical School, Singapore, Singapore.</nlm:affiliation>
<country xml:lang="fr">Singapour</country>
<wicri:regionArea>CSIRO Australian Animal Health Laboratory, East Geelong, Victoria, Australia; Program in Emerging Infectious Diseases, Duke-National University of Singapore Graduate Medical School, Singapore</wicri:regionArea>
<wicri:noRegion>Singapore</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Dutch, Rebecca Ellis" sort="Dutch, Rebecca Ellis" uniqKey="Dutch R" first="Rebecca Ellis" last="Dutch">Rebecca Ellis Dutch</name>
<affiliation wicri:level="2"><nlm:affiliation>Department of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, Kentucky, United States of America.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, Kentucky</wicri:regionArea>
<placeName><region type="state">Kentucky</region>
</placeName>
</affiliation>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="2015">2015</date>
<idno type="RBID">pubmed:25706132</idno>
<idno type="pmid">25706132</idno>
<idno type="doi">10.1371/journal.pone.0115736</idno>
<idno type="wicri:Area/PubMed/Corpus">000E57</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000E57</idno>
<idno type="wicri:Area/PubMed/Curation">000E57</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000E57</idno>
<idno type="wicri:Area/PubMed/Checkpoint">000E61</idno>
<idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">000E61</idno>
<idno type="wicri:Area/Ncbi/Merge">002A35</idno>
<idno type="wicri:Area/Ncbi/Curation">002A35</idno>
<idno type="wicri:Area/Ncbi/Checkpoint">002A35</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">Analysis of cathepsin and furin proteolytic enzymes involved in viral fusion protein activation in cells of the bat reservoir host.</title>
<author><name sortKey="El Najjar, Farah" sort="El Najjar, Farah" uniqKey="El Najjar F" first="Farah" last="El Najjar">Farah El Najjar</name>
<affiliation wicri:level="2"><nlm:affiliation>Department of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, Kentucky, United States of America.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, Kentucky</wicri:regionArea>
<placeName><region type="state">Kentucky</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Lampe, Levi" sort="Lampe, Levi" uniqKey="Lampe L" first="Levi" last="Lampe">Levi Lampe</name>
<affiliation wicri:level="2"><nlm:affiliation>Department of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, Kentucky, United States of America.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, Kentucky</wicri:regionArea>
<placeName><region type="state">Kentucky</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Baker, Michelle L" sort="Baker, Michelle L" uniqKey="Baker M" first="Michelle L" last="Baker">Michelle L. Baker</name>
<affiliation wicri:level="1"><nlm:affiliation>CSIRO Australian Animal Health Laboratory, East Geelong, Victoria, Australia.</nlm:affiliation>
<country xml:lang="fr">Australie</country>
<wicri:regionArea>CSIRO Australian Animal Health Laboratory, East Geelong, Victoria</wicri:regionArea>
<wicri:noRegion>Victoria</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Wang, Lin Fa" sort="Wang, Lin Fa" uniqKey="Wang L" first="Lin-Fa" last="Wang">Lin-Fa Wang</name>
<affiliation wicri:level="1"><nlm:affiliation>CSIRO Australian Animal Health Laboratory, East Geelong, Victoria, Australia; Program in Emerging Infectious Diseases, Duke-National University of Singapore Graduate Medical School, Singapore, Singapore.</nlm:affiliation>
<country xml:lang="fr">Singapour</country>
<wicri:regionArea>CSIRO Australian Animal Health Laboratory, East Geelong, Victoria, Australia; Program in Emerging Infectious Diseases, Duke-National University of Singapore Graduate Medical School, Singapore</wicri:regionArea>
<wicri:noRegion>Singapore</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Dutch, Rebecca Ellis" sort="Dutch, Rebecca Ellis" uniqKey="Dutch R" first="Rebecca Ellis" last="Dutch">Rebecca Ellis Dutch</name>
<affiliation wicri:level="2"><nlm:affiliation>Department of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, Kentucky, United States of America.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, Kentucky</wicri:regionArea>
<placeName><region type="state">Kentucky</region>
</placeName>
</affiliation>
</author>
</analytic>
<series><title level="j">PloS one</title>
<idno type="eISSN">1932-6203</idno>
<imprint><date when="2015" type="published">2015</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term>
<term>Cathepsins (metabolism)</term>
<term>Cell Line</term>
<term>Chiroptera (virology)</term>
<term>Chlorocebus aethiops</term>
<term>Cricetinae</term>
<term>Furin (metabolism)</term>
<term>Peptide Hydrolases (metabolism)</term>
<term>Vero Cells</term>
<term>Viral Fusion Proteins (metabolism)</term>
<term>Viral Proteins (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term>
<term>Cathepsines (métabolisme)</term>
<term>Cellules Vero</term>
<term>Chiroptera (virologie)</term>
<term>Cricetinae</term>
<term>Furine (métabolisme)</term>
<term>Lignée cellulaire</term>
<term>Peptide hydrolases (métabolisme)</term>
<term>Protéines de fusion virale (métabolisme)</term>
<term>Protéines virales (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cathepsins</term>
<term>Furin</term>
<term>Peptide Hydrolases</term>
<term>Viral Fusion Proteins</term>
<term>Viral Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cathepsines</term>
<term>Furine</term>
<term>Peptide hydrolases</term>
<term>Protéines de fusion virale</term>
<term>Protéines virales</term>
</keywords>
<keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Chiroptera</term>
</keywords>
<keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Chiroptera</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Cell Line</term>
<term>Chlorocebus aethiops</term>
<term>Cricetinae</term>
<term>Vero Cells</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Animaux</term>
<term>Cellules Vero</term>
<term>Cricetinae</term>
<term>Lignée cellulaire</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Bats of different species play a major role in the emergence and transmission of highly pathogenic viruses including Ebola virus, SARS-like coronavirus and the henipaviruses. These viruses require proteolytic activation of surface envelope glycoproteins needed for entry, and cellular cathepsins have been shown to be involved in proteolysis of glycoproteins from these distinct virus families. Very little is currently known about the available proteases in bats. To determine whether the utilization of cathepsins by bat-borne viruses is related to the nature of proteases in their natural hosts, we examined proteolytic processing of several viral fusion proteins in cells derived from two fruit bat species, Pteropus alecto and Rousettus aegyptiacus. Our work shows that fruit bat cells have homologs of cathepsin and furin proteases capable of cleaving and activating both the cathepsin-dependent Hendra virus F and the furin-dependent parainfluenza virus 5 F proteins. Sequence analysis comparing Pteropus alecto furin and cathepsin L to proteases from other mammalian species showed a high degree of conservation; however significant amino acid variation occurs at the C-terminus of Pteropus alecto furin. Further analysis of furin-like proteases from fruit bats revealed that these proteases are catalytically active and resemble other mammalian furins in their response to a potent furin inhibitor. However, kinetic analysis suggests that differences may exist in the cellular localization of furin between different species. Collectively, these results indicate that the unusual role of cathepsin proteases in the life cycle of bat-borne viruses is not due to the lack of active furin-like proteases in these natural reservoir species; however, differences may exist between furin proteases present in fruit bats compared to furins in other mammalian species, and these differences may impact protease usage for viral glycoprotein processing. </div>
</front>
</TEI>
<affiliations><list><country><li>Australie</li>
<li>Singapour</li>
<li>États-Unis</li>
</country>
<region><li>Kentucky</li>
</region>
</list>
<tree><country name="États-Unis"><region name="Kentucky"><name sortKey="El Najjar, Farah" sort="El Najjar, Farah" uniqKey="El Najjar F" first="Farah" last="El Najjar">Farah El Najjar</name>
</region>
<name sortKey="Dutch, Rebecca Ellis" sort="Dutch, Rebecca Ellis" uniqKey="Dutch R" first="Rebecca Ellis" last="Dutch">Rebecca Ellis Dutch</name>
<name sortKey="Lampe, Levi" sort="Lampe, Levi" uniqKey="Lampe L" first="Levi" last="Lampe">Levi Lampe</name>
</country>
<country name="Australie"><noRegion><name sortKey="Baker, Michelle L" sort="Baker, Michelle L" uniqKey="Baker M" first="Michelle L" last="Baker">Michelle L. Baker</name>
</noRegion>
</country>
<country name="Singapour"><noRegion><name sortKey="Wang, Lin Fa" sort="Wang, Lin Fa" uniqKey="Wang L" first="Lin-Fa" last="Wang">Lin-Fa Wang</name>
</noRegion>
</country>
</tree>
</affiliations>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/SrasV1/Data/Ncbi/Checkpoint
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 002A35 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Ncbi/Checkpoint/biblio.hfd -nk 002A35 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Sante |area= SrasV1 |flux= Ncbi |étape= Checkpoint |type= RBID |clé= pubmed:25706132 |texte= Analysis of cathepsin and furin proteolytic enzymes involved in viral fusion protein activation in cells of the bat reservoir host. }}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Ncbi/Checkpoint/RBID.i -Sk "pubmed:25706132" \ | HfdSelect -Kh $EXPLOR_AREA/Data/Ncbi/Checkpoint/biblio.hfd \ | NlmPubMed2Wicri -a SrasV1
![]() | This area was generated with Dilib version V0.6.33. | ![]() |