Peptide presentation by bat MHC class I provides new insight into the antiviral immunity of bats.
Identifieur interne : 000427 ( PubMed/Curation ); précédent : 000426; suivant : 000428Peptide presentation by bat MHC class I provides new insight into the antiviral immunity of bats.
Auteurs : Dan Lu [République populaire de Chine] ; Kefang Liu [République populaire de Chine] ; Di Zhang [République populaire de Chine] ; Can Yue [République populaire de Chine] ; Qiong Lu [République populaire de Chine] ; Hao Cheng [République populaire de Chine] ; Liang Wang [République populaire de Chine] ; Yan Chai [République populaire de Chine] ; Jianxun Qi [République populaire de Chine] ; Lin-Fa Wang [Singapour] ; George F. Gao [République populaire de Chine] ; William J. Liu [République populaire de Chine]Source :
- PLoS biology [ 1545-7885 ] ; 2019.
Descripteurs français
- KwdFr :
- MESH :
- immunologie : Chiroptera, Interactions hôte-pathogène, Virus à ARN.
- physiologie : Antigènes d'histocompatibilité de classe I.
- virologie : Chiroptera.
- Animaux, Présentation d'antigène.
English descriptors
- KwdEn :
- MESH :
- chemical , physiology : Histocompatibility Antigens Class I.
- immunology : Chiroptera, Host-Pathogen Interactions, RNA Viruses.
- virology : Chiroptera.
- Animals, Antigen Presentation.
Abstract
Bats harbor many zoonotic viruses, including highly pathogenic viruses of humans and other mammals, but they are typically asymptomatic in bats. To further understand the antiviral immunity of bats, we screened and identified a series of bat major histocompatibility complex (MHC) I Ptal-N*01:01-binding peptides derived from four different bat-borne viruses, i.e., Hendra virus (HeV), Ebola virus (EBOV), Middle East respiratory syndrome coronavirus (MERS-CoV), and H17N10 influenza-like virus. The structures of Ptal-N*01:01 display unusual peptide presentation features in that the bat-specific 3-amino acid (aa) insertion enables the tight "surface anchoring" of the P1-Asp in pocket A of bat MHC I. As the classical primary anchoring positions, the B and F pockets of Ptal-N*01:01 also show unconventional conformations, which contribute to unusual peptide motifs and distinct peptide presentation. Notably, the features of bat MHC I may be shared by MHC I from various marsupials. Our study sheds light on bat adaptive immunity and may benefit future vaccine development against bat-borne viruses of high impact on humans.
DOI: 10.1371/journal.pbio.3000436
PubMed: 31498797
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<front><div type="abstract" xml:lang="en">Bats harbor many zoonotic viruses, including highly pathogenic viruses of humans and other mammals, but they are typically asymptomatic in bats. To further understand the antiviral immunity of bats, we screened and identified a series of bat major histocompatibility complex (MHC) I Ptal-N*01:01-binding peptides derived from four different bat-borne viruses, i.e., Hendra virus (HeV), Ebola virus (EBOV), Middle East respiratory syndrome coronavirus (MERS-CoV), and H17N10 influenza-like virus. The structures of Ptal-N*01:01 display unusual peptide presentation features in that the bat-specific 3-amino acid (aa) insertion enables the tight "surface anchoring" of the P1-Asp in pocket A of bat MHC I. As the classical primary anchoring positions, the B and F pockets of Ptal-N*01:01 also show unconventional conformations, which contribute to unusual peptide motifs and distinct peptide presentation. Notably, the features of bat MHC I may be shared by MHC I from various marsupials. Our study sheds light on bat adaptive immunity and may benefit future vaccine development against bat-borne viruses of high impact on humans.</div>
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<Abstract><AbstractText>Bats harbor many zoonotic viruses, including highly pathogenic viruses of humans and other mammals, but they are typically asymptomatic in bats. To further understand the antiviral immunity of bats, we screened and identified a series of bat major histocompatibility complex (MHC) I Ptal-N*01:01-binding peptides derived from four different bat-borne viruses, i.e., Hendra virus (HeV), Ebola virus (EBOV), Middle East respiratory syndrome coronavirus (MERS-CoV), and H17N10 influenza-like virus. The structures of Ptal-N*01:01 display unusual peptide presentation features in that the bat-specific 3-amino acid (aa) insertion enables the tight "surface anchoring" of the P1-Asp in pocket A of bat MHC I. As the classical primary anchoring positions, the B and F pockets of Ptal-N*01:01 also show unconventional conformations, which contribute to unusual peptide motifs and distinct peptide presentation. Notably, the features of bat MHC I may be shared by MHC I from various marsupials. Our study sheds light on bat adaptive immunity and may benefit future vaccine development against bat-borne viruses of high impact on humans.</AbstractText>
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<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Lu</LastName>
<ForeName>Dan</ForeName>
<Initials>D</Initials>
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</AffiliationInfo>
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</AffiliationInfo>
<AffiliationInfo><Affiliation>Faculty of Health Sciences, University of Macau, Macau SAR, China.</Affiliation>
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</AffiliationInfo>
<AffiliationInfo><Affiliation>Institute of Biophysics, Chinese Academy of Sciences, Beijing, China.</Affiliation>
</AffiliationInfo>
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<ForeName>Qiong</ForeName>
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<ForeName>Liang</ForeName>
<Initials>L</Initials>
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</AffiliationInfo>
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</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Wang</LastName>
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<ForeName>George F</ForeName>
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</AffiliationInfo>
<AffiliationInfo><Affiliation>Faculty of Health Sciences, University of Macau, Macau SAR, China.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Beijing Institutes of Life Science, University of Chinese Academy of Sciences, Beijing, China.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China.</Affiliation>
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<Author ValidYN="Y"><LastName>Liu</LastName>
<ForeName>William J</ForeName>
<Initials>WJ</Initials>
<Identifier Source="ORCID">0000-0003-3605-4070</Identifier>
<AffiliationInfo><Affiliation>NHC Key Laboratory of Medical Virology and Viral Diseases, National Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention, Beijing, China.</Affiliation>
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<ArticleDate DateType="Electronic"><Year>2019</Year>
<Month>09</Month>
<Day>09</Day>
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</MeshHeading>
<MeshHeading><DescriptorName UI="D017951" MajorTopicYN="Y">Antigen Presentation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002685" MajorTopicYN="N">Chiroptera</DescriptorName>
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<QualifierName UI="Q000821" MajorTopicYN="N">virology</QualifierName>
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<MeshHeading><DescriptorName UI="D015395" MajorTopicYN="N">Histocompatibility Antigens Class I</DescriptorName>
<QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D054884" MajorTopicYN="N">Host-Pathogen Interactions</DescriptorName>
<QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName>
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<MeshHeading><DescriptorName UI="D012328" MajorTopicYN="N">RNA Viruses</DescriptorName>
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<CoiStatement>The authors have declared that no competing interests exist.</CoiStatement>
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<Day>20</Day>
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