Corrigendum to "MHC class II DR classification based on antigen-binding groove natural selection" [Biochem. Biophys. Res. Commun. 385 (2009) 137-142] (DOI:10.1016/j.bbrc.2009.04.142);MHC class II DR classification based on antigen-binding groove natural selection

Biochemical and Biophysical Research Communications

Volumn 385, Issue 2, 2009, Pages 137-142

  Takeshima, Shin nosuke ^a   Sarai, Yoshinori ^b   Saitou, Naruya ^c   Aida, Yoko ^a  

^a RIKEN   (Japan)

^b KYUSHU INSTITUTE OF TECHNOLOGY   (Japan)

^c NATIONAL INSTITUTE OF GENETICS   (Japan)

Author keywords

Bovine major histocompatibility complex class II; Canine DLA DRB; Cattle BoLA DRB3; Feline FLA DRB; Human HLA DRB1; Negative selection; Nonsynonymous substitution; Positive selection; Swine SLA DRB; Synonymous substitution

Indexed keywords

AMINO ACID; DNA; HLA DR ANTIGEN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2;

ALLELE; AMINO ACID SUBSTITUTION; ANTIGEN BINDING; ANTIGEN RECOGNITION; ANTIGEN STRUCTURE; ARTICLE; CAT; CONTROLLED STUDY; COW; DNA POLYMORPHISM; DOG; GENETIC VARIABILITY; HUMAN; HUMAN VERSUS ANIMAL COMPARISON; MAJOR HISTOCOMPATIBILITY COMPLEX; MAMMAL; MOLECULAR EVOLUTION; MUTATION RATE; NATURAL SELECTION; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; SPECIES COMPARISON; SWINE;

ANIMALIA; BOS; BOVINAE; CANIS FAMILIARIS; FELIDAE; MAMMALIA; MURINAE; SUIDAE;

EID: 67349141547     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.10.098     Document Type: Erratum

References (18)

1. Jorgensen J.L., Reay P.A., Ehrich E.W., and Davis M.M. Molecular components of T-cell recognition. Annu. Rev. Immunol. 10 (1992) 835-873
2. Germain R.N., and Margulies D.H. The biochemistry and cell biology of antigen processing and presentation. Annu. Rev. Immunol. 11 (1993) 403-450
3. Brown J.H., Jardetzky T.S., Gorga J.C., Stern L.J., Urban R.G., Strominger J.L., and Wiley D.C. Three-dimensional structure of the human class II histocompatibility antigen HLA-DR1. Nature 364 (1993) 33-39
4. Bondinas G.P., Moustakas A.K., and Papadopoulos G.K. The spectrum of HLA-DQ and HLA-DR alleles, 2006: a listing correlating sequence and structure with function. Immunogenetics 59 2007 (2006) 539-553
5. Ota M., Seki T., Kiyosawa K., Furuta S., Hino K., Kondo T., Fukushima H., Tsuji K., and Inoko H. A possible association between basic amino acids of position 13 of DRB1 chains and autoimmune hepatitis. Immunogenetics 36 (1992) 49-55
6. de Vries N., Tijssen H., van Riel P.L., and van de Putte L.B. Reshaping the shared epitope hypothesis: HLA-associated risk for rheumatoid arthritis is encoded by amino acid substitutions at positions 67-74 of the HLA-DRB1 molecule. Arthritis. Rheum. 46 (2002) 921-928
7. Foley P.J., McGrath D.S., Puscinska E., Petrek M., Kolek V., Drabek J., Lympany P.A., Pantelidis P., Welsh K.I., Zielinski J., and du Bois R.M. Human leukocyte antigen-DRB1 position 11 residues are a common protective marker for sarcoidosis. Am. J. Respir. Cell Mol. Biol. 25 (2001) 272-277
8. Alaez C., del Pilar Mora M., Arellanes L., Cano S., Perez-Luque E., Vazquez M.N., Olivo A., Burguete A., Hernandez A., Pedroza M., and Gorodezky C. Strong association of HLA class II sequences in Mexicans with Vogt-Koyanagi-Harada's disease. Hum. Immunol. 60 (1999) 875-882
9. Ettinger R.A., Liu A.W., Nepom G.T., and Kwok W.W. Beta 57-Asp plays an essential role in the unique SDS stability of HLA-DQA1*0102/DQB1*0602 alpha beta protein dimer, the class II MHC allele associated with protection from insulin-dependent diabetes mellitus. J. Immunol. 165 (2000) 3232-3238
10. Zerva L., Cizman B., Mehra N.K., Alahari S.K., Murali R., Zmijewski C.M., Kamoun M., and Monos D.S. Arginine at positions 13 or 70-71 in pocket 4 of HLA-DRB1 alleles is associated with susceptibility to tuberculoid leprosy. J. Exp. Med. 183 (1996) 829-836
11. Davenport M.P., Quinn C.L., Chicz R.M., Green B.N., Willis A.C., Lane W.S., Bell J.I., and Hill A.V.S. Naturally processed peptides from 2 disease-resistance-associated Hla-Dr13 alleles show related sequence motifs and the effects of the dimorphism at position-86 of the Hla-Dr-beta chain. Proc. Natl. Acad. Sci. USA 92 (1995) 6567-6571
12. Klein J., and O'HUigin C. Composite origin of major histocompatibility complex genes. Curr. Opin. Genet. Dev. 3 (1993) 923-930
13. Suzuki Y., and Gojobori T. A method for detecting positive selection at single amino acid sites. Mol. Biol. Evol. 16 (1999) 1315-1328
14. Ando A., Kawata H., Shigenari A., Anzai T., Ota M., Katsuyama Y., Sada M., Goto R., Takeshima S.N., Aida Y., Iwanaga T., Fujimura N., Suzuki Y., Gojobori T., and Inoko H. Genetic polymorphism of the swine major histocompatibility complex (SLA) class I genes, SLA-1, -2 and -3. Immunogenetics 55 (2003) 583-593
15. Nei M., and Gojobori T. Simple methods for estimating the numbers of synonymous and nonsynonymous nucleotide substitutions. Mol. Biol. Evol. 3 (1986) 418-426
16. Jukes T.H., and Cantor C.R. Evolution of protein molecules. In: Monro H.N. (Ed). Mammalian Protein Metabolism III (1969), Academic Press, New York 21-132
17. Kumar S., Tamura K., Jakobsen I.B., and Nei M. MEGA2: molecular evolutionary genetics analysis software. Bioinformatics 17 (2001) 1244-1245
18. Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., and Higgins D.G. The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25 (1997) 4876-4882