ABCMdb

ABCD1 p.Val123Ile

None has been submitted yet.

Publications

PMID: 26522770 [PubMed] Kelly JT et al: "Potent antiviral agents fail to elicit genetically-stable resistance mutations in either enterovirus 71 or Coxsackievirus A16."

No. Sentence Comment

26 Sequencing revealed three different VP1 mutants in EV71 (I113L, I113M, I113M/V123I) and one in CVA16 (L113F) (Table 1). Login to comment
27 Virus passaged in a combination of NLD/ GPP3 over 30 passages maintained the I113M/V123I mutations (n &#bc; 1). Login to comment
30 Mutations I113M and V123I are located on the inside of the VP1 pocket and I113 is one of the residues involved in compound binding (Fig. 2B). Login to comment
35 The difference in the lowest free energy of folding (DDGfolding) between the WT and EV71 I113M or V123I mutants was &#fe;0.73 and &#fe; 0.98 kcal/mol, respectively. Login to comment
37 The mutations I113M and V123I appeared to cause a shrinking of the VP1 pocket, with the methionine residue pointing inside, suggesting a steric clash with the Fig. 1. Login to comment
52 Virus/Compound Mutation(s) Number sequenced EV71/NLD I113M (62%), I113L (31%), I113M/V123I (7%) n &#bc; 13 EV71/GPP3 I113M/V123I n &#bc; 4 EV71/ALD I113M/V123I n &#bc; 1 EV71/NLD &#fe; GPP3 I113M/V123I n &#bc; 12 CVA16/GPP3 L113F n &#bc; 10 Fig. 2. Login to comment
62 The two mutated side chains I113M and V123I are shown as grey balls-and-sticks. Login to comment
73 These data suggest that the I113M/V123I mutation prevented compound binding as the thermostability of the resistant isolates was not increased in the presence of NLD. Login to comment
74 The bulkier side chains of the I113M and L113F mutations are predicted to point directly into the pocket, reducing the space available for inhibitor binding and the V123I mutation reduces this further. Login to comment