Correction to: Two class I genes of the chicken MHC have different functions: BF1 is recognized by NK cells while BF2 is recognized by CTLs

Correction to: Immunogenetics

https://doi.org/10.1007/s00251-018-1066-2

The Figure 3 in the original version of this article was incorrectly published. In this article the top panel of Figure 3 that describes the amino acid sequence alignment is now presented correctly.

Fig. 3

The location of the potential KIR binding region in the BF1 glycoproteins and the location of the potential KIR epitopes of BF1*21 and BF1*13 glycoproteins involved in NK inhibition. Top: Amino acid alignment of the alpha 1 and alpha 2 domains of the BF1 and BF2 class I glycoproteins. The BF1*2 glycoprotein, endogenous to the RP9 cells, aligns more closely with the BF2 glycoproteins than with the BF1 glycoproteins and lacks the signature RSVEVS sequence identified by amino acid residues 68 to 83 present in all other BF1 alleles. The residues aligning with the amino acids of HLA-C that interact with the human NK KIR (68, 71, 74, 75, 78, 79, 83 and 142, 143, 146, 147, 148) are boxed. Bottom: The location of the mutation made in the BF1*21 glycoprotein to convert the RSVEVS to the sequence present in the BF1*2 glycoprotein is shown, the ribbon diagram represents the BF1*21 glycoprotein modeled using Swiss-Model indicating the orientation of the BF1*21 locus specific residues mutated to produce the BF1*21KIRm mutant. The BF amino acid sequences were aligned using the Jotun Hein method in MegAlign7.2.1 (DNASTAR, Madison, WI). The dots indicate amino acid identity with the majority. Amino acid residue numbers of the chicken corresponding to those in human class I are as previously aligned, Hunt and Fulton, 1998

The original article has been corrected.