论文原文： SARS-CoV-2-S/DPP4 binding shares key DPP4 residues with that of MERS-CoV-S/DPP4
Here,
bioinformatics approaches combining human-virus protein interaction
prediction and protein docking based on crystal structures have revealed
the high affinity between human dipeptidylpeptidase 4 (DPP4) and the
spike (S) receptor-binding domain of SARS-CoV-2. Intriguingly, the
crucial binding residues of DPP4 are identical to those that are bound
to the MERS-CoV-S.
Although the homology between SARS-CoV-2-S
and MERS-CoV-S RBDs is low (19.1%), they shared identical binding
residues of DPP4 at the interfaces (Figure 1C).
The
features of these residue interactions are very similar to those
mediating the interaction between adenosine deaminase (ADA) and CD26
(ref. 23). By a pairwise comparison, we unexpectedly found that all
those CD26 residues identified in the virus–receptor interface are also
involved in ADA binding, indicating a competition between ADA and the
virus for CD26 receptor. As the ADA–CD26 interaction is shown to induce
co-stimulatory signals in T cells22, this may indicate a possible
manipulation of the host immune system by MERS-CoV through competition
for the ADA-recognition site.
这段文字中的关键内容是： By a pairwise
comparison, we unexpectedly found that all those CD26 residues
identified in the virus–receptor interface are also involved in ADA
binding,
