PDBsum entry 6j2f

Immune system

PDB id: 6j2f

Contents

Protein chains

277 a.a.

98 a.a.

Ligands

ASP-TYR-ILE-ASN-THR-ASN-VAL-LEU-PRO ×2

Waters ×620

PDB id:

6j2f

Name:

Immune system

Title:

Crystal structure of bat (pteropus alecto) mhc class i ptal-n 01:01 In complex with hendra virus-derived peptide hev2

Structure:

Ptal-n 01:01. Chain: a, d. Engineered: yes. Beta-2 microglobulin. Chain: b, e. Engineered: yes. Hev2. Chain: c, f. Engineered: yes

Source:

Pteropus alecto. Black flying fox. Organism_taxid: 9402. Gene: ptal-n. Expressed in: escherichia coli k-12. Expression_system_taxid: 83333. Gene: pal_glean10023531. Synthetic: yes. Hendra virus.

Resolution:

1.90Å R-factor: 0.204 R-free: 0.231

Authors:

D.Lu,K.F.Liu,C.Yue,Q.Lu,H.Cheng,Y.Chai,J.X.Qi,G.F.Gao,W.J.Liu

Key ref:

D.Lu et al. (2019). Peptide presentation by bat MHC class I provides new insight into the antiviral immunity of bats. PLoS Biol, 17, e3000436. PubMed id: 31498797 DOI: 10.1371/journal.pbio.3000436

Date:

01-Jan-19 Release date: 18-Sep-19

Protein chains

A0A125R585  (A0A125R585_PTEAL) -  MHC class I antigen from Pteropus alecto

Seq: 368 a.a.

Struc: 277 a.a.

Protein chains

L5K3Y9  (L5K3Y9_PTEAL) -  Beta-2-microglobulin from Pteropus alecto

Seq: 331 a.a.

Struc: 98 a.a.*

* PDB and UniProt seqs differ at 5 residue positions (black crosses)

DOI no: 10.1371/journal.pbio.3000436

PLoS Biol 17:e3000436 (2019)

PubMed id: 31498797

Peptide presentation by bat MHC class I provides new insight into the antiviral immunity of bats.

D.Lu, K.Liu, D.Zhang, C.Yue, Q.Lu, H.Cheng, L.Wang, Y.Chai, J.Qi, L.F.Wang, G.F.Gao, W.J.Liu.

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.