PDBsum entry 4l8b

Immune system

PDB id: 4l8b

Contents

Protein chains

276 a.a.

98 a.a.

Ligands

ALA-SER-ASN-GLU-HIS-MET-GLU-THR-MET

SO4 ×2

PEG

Metals

_NA

Waters ×136

PDB id:

4l8b

Name:

Immune system

Title:

Crystal structure of the h2db in complex with the np-n5h peptide

Structure:

H-2 class i histocompatibility antigen, d-b alpha chain. Chain: a. Fragment: unp residues 25-304. Synonym: heavy chain h2db, h-2d(b). Engineered: yes. Beta-2-microglobulin. Chain: b. Fragment: unp residues 21-119. Synonym: b2m.

Source:

Mus musculus. Mouse. Organism_taxid: 10090. Gene: h2-d1. Expressed in: escherichia coli. Expression_system_taxid: 469008. Gene: b2m. Synthetic: yes

Resolution:

2.20Å R-factor: 0.199 R-free: 0.232

Authors:

J.Rossjohn,S.Gras

Key ref:

S.A.Valkenburg et al. (2013). Acute emergence and reversion of influenza A virus quasispecies within CD8+ T cell antigenic peptides. Nat Commun, 4, 2663. PubMed id: 24173108 DOI: 10.1038/ncomms3663

Date:

16-Jun-13 Release date: 16-Oct-13

Protein chain

P01899  (HA11_MOUSE) -  H-2 class I histocompatibility antigen, D-B alpha chain from Mus musculus

Seq: 362 a.a.

Struc: 276 a.a.

Protein chain

P01887  (B2MG_MOUSE) -  Beta-2-microglobulin from Mus musculus

Seq: 119 a.a.

Struc: 98 a.a.

DOI no: 10.1038/ncomms3663

Nat Commun 4:2663 (2013)

PubMed id: 24173108

Acute emergence and reversion of influenza A virus quasispecies within CD8+ T cell antigenic peptides.

S.A.Valkenburg, S.Quiñones-Parra, S.Gras, N.Komadina, J.McVernon, Z.Wang, H.Halim, P.Iannello, C.Cole, K.Laurie, A.Kelso, J.Rossjohn, P.C.Doherty, S.J.Turner, K.Kedzierska.

ABSTRACT

Influenza A virus-specific CD8(+) cytotoxic T lymphocytes (CTLs) provide a degree of cross-strain protection that is potentially subverted by mutation. Here we describe the sequential emergence of such variants within CTL epitopes for a persistently infected, immunocompromised infant. Further analysis in immunodeficient and wild-type mice supports the view that CTL escape variants arise frequently in influenza, accumulate with time and revert in the absence of immune pressure under MHCI-mismatched conditions. Viral fitness, the abundance of endogenous CD8(+) T cell responses and T cell receptor repertoire diversity influence the nature of these de novo mutants. Structural characterization of dominant escape variants shows how the peptide-MHCI interaction is modified to affect variant-MHCI stability. The mechanism of influenza virus escape thus looks comparable to that recognized for chronic RNA viruses like HIV and HCV, suggesting that immunocompromised patients with prolonged viral infection could have an important part in the emergence of influenza quasispecies.