Peptide presentation by bat MHC class I provides new insight into the antiviral immunity of bats
Identifieur interne : 002334 ( Ncbi/Curation ); précédent : 002333; suivant : 002335Peptide 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 [ 1544-9173 ] ; 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.
Url:
DOI: 10.1371/journal.pbio.3000436
PubMed: 31498797
PubMed Central: 6752855
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PMC:6752855Le document en format XML
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<series><title level="j">PLoS Biology</title>
<idno type="ISSN">1544-9173</idno>
<idno type="eISSN">1545-7885</idno>
<imprint><date when="2019">2019</date>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term>
<term>Antigen Presentation</term>
<term>Chiroptera (immunology)</term>
<term>Chiroptera (virology)</term>
<term>Histocompatibility Antigens Class I (physiology)</term>
<term>Host-Pathogen Interactions (immunology)</term>
<term>RNA Viruses (immunology)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term>
<term>Antigènes d'histocompatibilité de classe I (physiologie)</term>
<term>Chiroptera (immunologie)</term>
<term>Chiroptera (virologie)</term>
<term>Interactions hôte-pathogène (immunologie)</term>
<term>Présentation d'antigène</term>
<term>Virus à ARN (immunologie)</term>
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<keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Histocompatibility Antigens Class I</term>
</keywords>
<keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Chiroptera</term>
<term>Interactions hôte-pathogène</term>
<term>Virus à ARN</term>
</keywords>
<keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Chiroptera</term>
<term>Host-Pathogen Interactions</term>
<term>RNA Viruses</term>
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<keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Antigènes d'histocompatibilité de classe I</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>Antigen Presentation</term>
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<keywords scheme="MESH" xml:lang="fr"><term>Animaux</term>
<term>Présentation d'antigène</term>
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<front><div type="abstract" xml:lang="en"><p>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.</p>
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