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Table 3 Amino acid changes in HIV-1 Env in polyclonal viral pools with high-level PIE12-trimer resistance

From: Characterization of resistance to a potent d-peptide HIV entry inhibitor

Mutation

Codon

Prevalence

Control (%)

W1 (%)

W2 (%)

Notes

T19I

acc → atc

 

44

  

A48T

gca → aca

 

72

57

 

E83K

gaa → aaa

32

20

10

 

N136D

aat → gat

 

99

99

glycosylation site

N136K

aat → aag

47

  

R146K

aga → aaa

 

18

24

 

Δ161–164

  

90

90

V1/V2, glycosylation site

F175L

ttc → ctc

  

67

V1/V2

V200E

gtc → gaa

 

67

  

V255A

gta → gca

  

46

 

N301K

aac → aaa

71

100

99

glycosylation site

S306R

agt → aga

 

64

20

V3

T319A

aca → gca

 

85

  

Δ396–400

  

58

59

V4, glycosylation site

N460I

aat → att

  

17

near CD4 binding site

G464E

ggg → gag

 

82

 

glycosylation site

S465P

tcc → ccc

  

11

 

Q550H

cag → cac

 

92

98

N-trimer, RRE

Q577R

cag → cgg

  

99

PIE12 binding site, RRE

Q577N

cag → aac

 

97

 

V583V

gtg → gta

 

100

100

silent/RRE

A612T

gct → act

 

13

 

glycosylation site, RRE

H643Y

cac → tac

99

46

97

C-peptide

L663F

tta → ttt

 

99

99

 

N674T

aac → acc

  

56

glycosylation site

V693I

gta → ata

  

21

 

A823 V

gct → gtt

 

98

99

 
  1. List of amino acid mutations (point mutant, insertion or deletion) in either resistance pool that occurs at a rate > 10% different than in the control pool. In italic are the mutants that meet the stricter criteria of: (1) high prevalence (≥ 50%) within both resistant populations but not in the control, (2) not silent (except in the RRE, where a silent mutation could impact RNA structure)
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Retrovirology

ISSN: 1742-4690

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