Structural insights into the evolution feature of a bony fish CD8αα homodimer

Wang, Junya; Zhang, Nianzhi; Wang, Zhenbao; Wu, Yanan; Zhang, Lijie; Xia, Chun

doi:10.1016/j.molimm.2018.03.023

Cited by 7 publications

(12 citation statements)

References 36 publications

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“…Considering that the relative position of the pMHC-I a3 domain in the carp structure is shifted toward b2m, the binding mode of pMHC-I-CD8 in grass carp was hypothesized to be different from that in humans and mice. Our previous study demonstrated that the identity of CD8 coreceptors among species is low; however, the trend of their topological structure is very similar, and the interaction region between CD8 and pMHC is relatively conservative (38,44). Ma et al (26) suggested that the interaction between MHC-I and CD8 molecules in nonmammals is different from that in mammals based on the analysis of the distances between the CD loop shifts in the structures of nonmammals and mammals.…”

Section: Discussionmentioning

confidence: 96%

“…The assembly of the pAnca-UA*0101 complex in vitro was performed by the dilution renaturation method. The molar ratio of Anca-UA*0101, Anca-b2m, and peptide was 1:1:3, and the inclusion bodies were renatured using a previously described (38) gradual dilution method in refolding buffer for 24 h at 4˚C. Then, the refolded product was concentrated using a 10-kDa-cutoff filter and purified on a Superdex 200 16/60 column followed…”

Section: The Assembly and Purification Of The Panca-ua*0101 Complexmentioning

confidence: 99%

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The Crystal Structure of the MHC Class I (MHC-I) Molecule in the Green Anole Lizard Demonstrates the Unique MHC-I System in Reptiles

Wang

et al. 2021

The Journal of Immunology

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The reptile MHC class I (MCH-I) and MHC class II proteins are the key molecules in the immune system; however, their structure has not been investigated. The crystal structure of green anole lizard peptide–MHC-I–β2m (pMHC-I or pAnca-UA*0101) was determined in the current study. Subsequently, the features of pAnca-UA*0101 were analyzed and compared with the characteristics of pMHC-I of four classes of vertebrates. The amino acid sequence identities between Anca-UA*0101 and MHC-I from other species are <50%; however, the differences between the species were reflected in the topological structure. Significant characteristics of pAnca-UA*0101 include a specific flip of ∼88° and an upward shift adjacent to the C terminus of the α1- and α2-helical regions, respectively. Additionally, the lizard MHC-I molecule has an insertion of 2 aa (VE) at positions 55 and 56. The pushing force from 55-56VE triggers the flip of the α1 helix. Mutagenesis experiments confirmed that the 55-56VE insertion in the α1 helix enhances the stability of pAnca-UA*0101. The peptide presentation profile and motif of pAnca-UA*0101 were confirmed. Based on these results, the proteins of three reptile lizard viruses were used for the screening and confirmation of the candidate epitopes. These data enhance our understanding of the systematic differences between five classes of vertebrates at the gene and protein levels, the formation of the pMHC-I complex, and the evolution of the MHC-I system.

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Section: Discussionmentioning

confidence: 96%

Section: The Assembly and Purification Of The Panca-ua*0101 Complexmentioning

confidence: 99%

The Crystal Structure of the MHC Class I (MHC-I) Molecule in the Green Anole Lizard Demonstrates the Unique MHC-I System in Reptiles

Wang

et al. 2021

The Journal of Immunology

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“…A mutation from K58 to E58 can significantly reduce CD8aa binding and is a potent antagonist of CTL activation. In our study, two types of pCtid-UAA-b2m complexes and grass carp CD8aa homodimers were superimposed based on known HLA-A2-CD8aa complex structures (Figure S5) (Wang et al, 2018). From the perspective of sequence characterization, Ctid-b2m-2 is seemingly more suited than Ctid-b2m-1 to form a salt bridge with the grass carp CD8aa in the same position.…”

Section: Ll Open Access Isciencementioning

confidence: 99%

The Mechanism of β2m Molecule-Induced Changes in the Peptide Presentation Profile in a Bony Fish

Zhang

et al. 2020

iScience

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“…Furthermore, also the T cell education system, concerning the tissue organization of the thymus and the existence of CD4 − CD8 − , CD4 + CD8 + , CD4 + CD8 − and CD4 + CD8 − thymocytes, seems to be similar between teleost fish and mammals [60,71,72,73,74]; the shark thymus may be similarly organized, but has been studied less intensively [145]. Teleost fish classical MHC class II molecules possess conserved residues that in mammals can bind to the TCR co-receptor molecule CD4 on helper/regulatory T cells [27] and teleost fish classical MHC class I molecules possess conserved features that in mammals are involved in binding the TCR co-receptor CD8 on cytotoxic T cells [41,113,146]. The CD8 molecule on mammalian cytotoxic T cells is a heterodimer of an alpha and a beta chain, CD8α and CD8β, and fish have genes for both components [147,148,149,150,151]; the cytoplasmic tail of teleost fish CD8α was shown to have LCK kinase binding properties as known in mammals [152].…”

Section: Functional Analyses Of Fish Classical Mhc Genes and Molecmentioning

confidence: 99%

Major Histocompatibility Complex (MHC) Genes and Disease Resistance in Fish

Yamaguchi

Dijkstra

2019

Cells

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Fascinating about classical major histocompatibility complex (MHC) molecules is their polymorphism. The present study is a review and discussion of the fish MHC situation. The basic pattern of MHC variation in fish is similar to mammals, with MHC class I versus class II, and polymorphic classical versus nonpolymorphic nonclassical. However, in many or all teleost fishes, important differences with mammalian or human MHC were observed: (1) The allelic/haplotype diversification levels of classical MHC class I tend to be much higher than in mammals and involve structural positions within but also outside the peptide binding groove; (2) Teleost fish classical MHC class I and class II loci are not linked. The present article summarizes previous studies that performed quantitative trait loci (QTL) analysis for mapping differences in teleost fish disease resistance, and discusses them from MHC point of view. Overall, those QTL studies suggest the possible importance of genomic regions including classical MHC class II and nonclassical MHC class I genes, whereas similar observations were not made for the genomic regions with the highly diversified classical MHC class I alleles. It must be concluded that despite decades of knowing MHC polymorphism in jawed vertebrate species including fish, firm conclusions (as opposed to appealing hypotheses) on the reasons for MHC polymorphism cannot be made, and that the types of polymorphism observed in fish may not be explained by disease-resistance models alone.

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Structural insights into the evolution feature of a bony fish CD8αα homodimer

Cited by 7 publications

References 36 publications

The Crystal Structure of the MHC Class I (MHC-I) Molecule in the Green Anole Lizard Demonstrates the Unique MHC-I System in Reptiles

The Crystal Structure of the MHC Class I (MHC-I) Molecule in the Green Anole Lizard Demonstrates the Unique MHC-I System in Reptiles

The Mechanism of β2m Molecule-Induced Changes in the Peptide Presentation Profile in a Bony Fish

Major Histocompatibility Complex (MHC) Genes and Disease Resistance in Fish

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