The N93D mutation of the human T-cell leukemia virus type 1 envelope glycoprotein found in symptomatic patients enhances neuropilin-1 b1 domain binding.
PMID: 34343702
2021
Biochimica et biophysica acta. Proteins and proteomics
Abstract: However, it remains unclear how the SU-N93D mutation affects Nrp1 b1 binding.
Abstract: Our results suggest that the interaction of SU Asp93 with the four residues of Nrp1 b1 renders the high affinity of the N93D mutant for Nrp1 b1 binding during HTLV-1 entry.
Abstract: Recently, the N93D mutation in the Nrp1 b1 binding region of the SU was identified in symptomatic patients with HTLV-1 infections in the Brazilian Amazon.
Abstract: The SU-N93D peptide binds directly to Nrp1 b1 with a binding affinity of 3.5 muM, which is approximately two-fold stronger than wild-type.
Abstract: This stronger binding is likely a result of the interaction between the substituted residue Asp93 of the N93D peptide and the four residues Trp301, Lys347, Glu348
The N93D mutation of the human T-cell leukemia virus type 1 envelope glycoprotein found in symptomatic patients enhances neuropilin-1 b1 domain binding.
Abstract: Of the three most frequent mutations, the previously undescribed N93D mutant was invariably associated with symptomatic cases.
Abstract: The identification of a rare mutation (N93D), present only in symptomatic patients, should also be investigated further as a potential clinical marker.
Abstract: The rare N93D amino acid mutation may be associated with the clinical manifestations of this viral infection.
Result:
Result: All the cases with the N93D mutation also presented pain, sensitivity, and dysautonomia.
Result: Just over half (52.5%; 21) of the 40 samples analyzed in this study presented some type of amino acid mutation, with three types - S72G, N93D and S192P - being recorded most frequently (Table 3).
HTLV1 mutation literature information.
PMID: 
2021
Biochimica et biophysica acta. Proteins and proteomics
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