Publications by authors named "Liubao Du"
Article Synopsis
- Bats can carry many zoonotic viruses without showing symptoms, largely due to their unique immune system, especially the MHC-I proteins which are important for fighting viruses.
- The study found that specific amino acid insertions (5AA and 3AA) in the bat MHC-I increase its thermal stability and improve its ability to bind diverse peptides effectively.
- It suggests that these insertions may allow bats to better handle high body temperatures when flying, indicating an evolutionary adaptation to temperature changes, similar to mechanisms observed in other lower vertebrates.
Micropolymorphism significantly shapes the peptide-binding characteristics of major histocompatibility complex class I (MHC-I) molecules, affecting the host's resistance to pathogens, which is particularly pronounced in avian species displaying the "minimal essential MHC" expression pattern. In this study, we compared two duck MHC-I alleles, Anpl-UAA*77 and Anpl-UAA*78, that exhibit markedly different peptide binding properties despite their high sequence homology. Through mutagenesis experiments and crystallographic analysis of complexes with the influenza virus-derived peptide AEAIIVAMV (AEV9), we identified a critical role for the residue at position 62 in regulating hydrogen-bonding interactions between the peptide backbone and the peptide-binding groove.
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