SARS Coronavirus Fusion Peptide-Derived Sequence Suppresses Collagen-Induced Arthritis in DBA/1J Mice.
Identifieur interne : 000F51 ( Main/Exploration ); précédent : 000F50; suivant : 000F52SARS Coronavirus Fusion Peptide-Derived Sequence Suppresses Collagen-Induced Arthritis in DBA/1J Mice.
Auteurs : Zu T. Shen [États-Unis] ; Alexander B. Sigalov [États-Unis]Source :
- Scientific reports [ 2045-2322 ] ; 2016.
Descripteurs français
- KwdFr :
- MESH :
- anatomopathologie : Arthrite expérimentale.
- métabolisme : Arthrite expérimentale.
- pharmacologie : Peptides, Protéines de fusion virale.
- traitement médicamenteux : Arthrite expérimentale.
- Animaux, Mâle, Peptides, Protéines de fusion virale, Souris, Virus du SRAS.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Peptides, Viral Fusion Proteins.
- chemistry : SARS Virus.
- drug therapy : Arthritis, Experimental.
- metabolism : Arthritis, Experimental.
- pathology : Arthritis, Experimental.
- chemical , pharmacology : Peptides, Viral Fusion Proteins.
- Animals, Male, Mice.
Abstract
During the co-evolution of viruses and their hosts, the viruses have evolved numerous strategies to counter and evade host antiviral immune responses in order to establish a successful infection, replicate and persist in the host. Recently, based on our model of immune signaling, the Signaling Chain HOmoOLigomerization (SCHOOL) model, we suggested specific molecular mechanisms used by different viruses such as severe acute respiratory syndrome coronavirus (SARS-CoV) to modulate the host immune response mediated by members of the family of multichain immune recognition receptors (MIRRs). This family includes T cell receptor (TCR) that is critically involved in immune diseases such as autoimmune arthritis. In the present study, we provide compelling experimental in vivo evidence in support of our hypothesis. Using the SCHOOL approach and the SARS-CoV fusion peptide sequence, we rationally designed a novel immunomodulatory peptide that targets TCR. We showed that this peptide ameliorates collagen-induced arthritis in DBA/1J mice and protects against bone and cartilage damage. Incorporation of the peptide into self-assembling lipopeptide nanoparticles that mimic native human high density lipoproteins significantly increases peptide dosage efficacy. Together, our data further confirm that viral immune evasion strategies that target MIRRs can be transferred to therapeutic strategies that require similar functionalities.
DOI: 10.1038/srep28672
PubMed: 27349522
Affiliations:
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Shen</name><affiliation wicri:level="2"><nlm:affiliation>SignaBlok, Inc, P.O. Box 4064, Shrewsbury, MA 01545, United States of America.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>SignaBlok, Inc, P.O. Box 4064, Shrewsbury, MA 01545</wicri:regionArea><placeName><region type="state">Massachusetts</region></placeName></affiliation></author><author><name sortKey="Sigalov, Alexander B" sort="Sigalov, Alexander B" uniqKey="Sigalov A" first="Alexander B" last="Sigalov">Alexander B. Sigalov</name><affiliation wicri:level="2"><nlm:affiliation>SignaBlok, Inc, P.O. Box 4064, Shrewsbury, MA 01545, United States of America.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>SignaBlok, Inc, P.O. Box 4064, Shrewsbury, MA 01545</wicri:regionArea><placeName><region type="state">Massachusetts</region></placeName></affiliation></author></analytic><series><title level="j">Scientific reports</title><idno type="eISSN">2045-2322</idno><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Arthritis, Experimental (drug therapy)</term><term>Arthritis, Experimental (metabolism)</term><term>Arthritis, Experimental (pathology)</term><term>Male</term><term>Mice</term><term>Peptides (chemistry)</term><term>Peptides (pharmacology)</term><term>SARS Virus (chemistry)</term><term>Viral Fusion Proteins (chemistry)</term><term>Viral Fusion Proteins (pharmacology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Arthrite expérimentale (anatomopathologie)</term><term>Arthrite expérimentale (métabolisme)</term><term>Arthrite expérimentale (traitement médicamenteux)</term><term>Mâle</term><term>Peptides ()</term><term>Peptides (pharmacologie)</term><term>Protéines de fusion virale ()</term><term>Protéines de fusion virale (pharmacologie)</term><term>Souris</term><term>Virus du SRAS ()</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Peptides</term><term>Viral Fusion Proteins</term></keywords><keywords scheme="MESH" qualifier="anatomopathologie" xml:lang="fr"><term>Arthrite expérimentale</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="drug therapy" xml:lang="en"><term>Arthritis, Experimental</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Arthritis, Experimental</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Arthrite expérimentale</term></keywords><keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Arthritis, Experimental</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Peptides</term><term>Protéines de fusion virale</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Peptides</term><term>Viral Fusion Proteins</term></keywords><keywords scheme="MESH" qualifier="traitement médicamenteux" xml:lang="fr"><term>Arthrite expérimentale</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Male</term><term>Mice</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Mâle</term><term>Peptides</term><term>Protéines de fusion virale</term><term>Souris</term><term>Virus du SRAS</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">During the co-evolution of viruses and their hosts, the viruses have evolved numerous strategies to counter and evade host antiviral immune responses in order to establish a successful infection, replicate and persist in the host. Recently, based on our model of immune signaling, the Signaling Chain HOmoOLigomerization (SCHOOL) model, we suggested specific molecular mechanisms used by different viruses such as severe acute respiratory syndrome coronavirus (SARS-CoV) to modulate the host immune response mediated by members of the family of multichain immune recognition receptors (MIRRs). This family includes T cell receptor (TCR) that is critically involved in immune diseases such as autoimmune arthritis. In the present study, we provide compelling experimental in vivo evidence in support of our hypothesis. Using the SCHOOL approach and the SARS-CoV fusion peptide sequence, we rationally designed a novel immunomodulatory peptide that targets TCR. We showed that this peptide ameliorates collagen-induced arthritis in DBA/1J mice and protects against bone and cartilage damage. Incorporation of the peptide into self-assembling lipopeptide nanoparticles that mimic native human high density lipoproteins significantly increases peptide dosage efficacy. Together, our data further confirm that viral immune evasion strategies that target MIRRs can be transferred to therapeutic strategies that require similar functionalities.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Massachusetts</li></region></list><tree><country name="États-Unis"><region name="Massachusetts"><name sortKey="Shen, Zu T" sort="Shen, Zu T" uniqKey="Shen Z" first="Zu T" last="Shen">Zu T. Shen</name></region><name sortKey="Sigalov, Alexander B" sort="Sigalov, Alexander B" uniqKey="Sigalov A" first="Alexander B" last="Sigalov">Alexander B. Sigalov</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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