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Table 2 Mapping amino acid residues in the V3/C3 region associated with neutralization sensitivity

From: Association of mutations in V3/C3 domain with enhanced sensitivity of HIV-1 clade C primary envelopes to autologous broadly neutralizing plasma antibodies

Env-pseudotyped viruses (Env chimeras & point mutants) Fold changes in ID50 Effect
HVTR-PG80v2.eJ7 wild type
HVTR-PG80v2.eJ38 wild type
HVTR-PG80v2.eJ38(v2.eJ7V3/C3) >422 Increase
HVTR-PG80v2.eJ38(v2.eJ7V3-C4) >138 Increase
HVTR-PG80v2.eJ38(v2.eJ7gp41) 0.8 No change
HVTR-PG80v2.eJ38(I307F) 1 No change
HVTR-PG80v2.eJ38(M316A) 1 No change
HVTR-PG80v2.eJ38(P326I) >8 Increase
HVTR-PG80v2.eJ38(N362T) 1 No change
HVTR-PG80v2.eJ7(N332T) 1.2 No change
HVTR-PG80v2.eJ7(E328Q) 1.8 Decrease
HVTR-PG80v2.eJ7(T362N/A364S)* 1.0 No change
  1. * The T362N/A364S double mutations removed the N360 glycan and introduced N362 glycan in PG80v2.eJ7 Env
  2. Potential N-linked glycans are given in italic