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

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

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

* The T362N/A364S double mutations removed the N360 glycan and introduced N362 glycan in PG80v2.eJ7 Env
Potential N-linked glycans are given in italic

ISSN: 1742-4690