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. 2006 Jan;80(2):821–834. doi: 10.1128/JVI.80.2.821-834.2006

TABLE 1.

Properties of AAV-2 capsid mutants

Mutationa Locationb Capsid synthesisc Heparin bindingd Transductione Mutationa Locationb Capsid synthesisc Heparin bindingd Transductione
None (wild type) ++ ++ 100 ± 11 D529I P ++ ++ 1 ± 0.03*
Q263A P ++ ++ 39 ± 4* D529N P +++ ++ 0.2 ± 0.01*
S264A P ++ ++ 72 ± 5 D529V P ++ ++ <0.0005*
G265A P ++ ++ 0.4 ± 0.1* E530A P ++ ++ 0.9 ± 0.02*
G265D P ++ ++ 1 ± 0.01* E530D P ++ ++ 121 ± 15
S267A P ++ ++ 378 ± 23* E530K P +++ ++ 0.02 ± 0.0*
S267T P ++ ++ 864 ± 42* E530Q P ++ ++ 1 ± 0.04*
N268A P ++ ++ 0.003 ± 0.0003* E531A P ++ ++ 41 ± 4*
N268Q P ++ ++ 0.02 ± 0.002* E531K P ++ ++ 2 ± 0.1*
D269A P ++ ++ 1 ± 0.1* K532A S ++ ++ 157 ± 18*
D269E P ++ ++ 1 ± 0.01* F533A S +++ ++ 83 ± 9
D269N P +++ ++ 9 ± 1* K544A S +++ ++ 79 ± 12
N270A P +++ ++ 94 ± 7 E548A S ++ ++ 105 ± 15
H271A P ++ ++ 10 ± 1* E548K S ++ ++ 1 ± 0.2*
H271F P ++ ++ 0.02 ± 0.001* T550A S +++ ++ 93 ± 15
H271Q P +++ ++ 2 ± 0.1* T550K S ++ ++ 34 ± 1*
H271T P ++ ++ 0.6 ± 0.05* E555A S +++ ++ 20 ± 1*
Q325A C ++ ++ 8 ± 0.2* K556A S ++ ++ 206 ± 37
D327A C ++ ++ 39 ± 3* E574A P +++ ++ 2 ± 0.9*
G328S C ++ ++ 7 ± 1* Q575A P ++ ++ 106 ± 10
T330A C ++ ++ 0.9 ± 0.03 R585A S +++ − 0.2 ± 0.02*
N382A P ++ ++ 3 ± 0.3* R585K S ++ ++ 134 ± 5*
G383A P +++ ++ 0.1 ± 0.0* G586A S ++ ++ 70 ± 11
S384A P + ++ 25 ± 3* G586K S ++ ++ 5 ± 0.3*
Q385A P ++ ++ 14 ± 0.6* N587A S ++ ++ 134 ± 12
S452A S ++ ++ 94 ± 8 N587K S +++ ++ 1 ± 0.2*
T454A S ++ ++ 99 ± 6 R588A S +++ − 1 ± 0.1*
T455A S ++ ++ 91 ± 8 R588K S ++ ++ 139 ± 16*
Q457A S ++ ++ 91 ± 4 Q589A S ++ ++ 118 ± 5
R459A S ++ ++ 271 ± 23* N705A P ++ ++ 98 ± 19
G466R S ++ ++ 1 ± 0.2* N705K P ++ ++ 11 ± 1*
S468A P +++ ++ 61 ± 5* K706A P +++ ++ 3 ± 0.5*
D469A P ++ ++ 5 ± 0.2* V708A P ++ ++ 111 ± 11
R471A P +++ ++ 318 ± 79* V708K P +++ ++ 74 ± 7*
D472A P +++ ++ 75 ± 6 Δ265ins1 P ++ ++ 0.002 ± 0.0001*
R487K S +++ ++ 24 ± 2* Q263A/S264L P ++ ++ 0.004 ± 0.0009*
T491A S +++ ++ 99 ± 13 S267A/N268A P ++ ++ 0.003 ± 0.0*
S492A S ++ ++ 107 ± 15 N497H/S498A S +++ ++ 32 ± 2*
S492T S +++ ++ 103 ± 16 S498A/N495K S ++ ++ 0.004 ± 0.0004*
A493R S ++ +/− 2 ± 0.03* S498A/S631P S ++ + 24 ± 2*
D494A S ++ ++ 9 ± 2* S498A/R729K S ++ + 250 ± 39*
D494E S ++ ++ 302 ± 23* R471A/N497K P, S ++ ++ 1 ± 0.2*
D494N S ++ ++ 5 ± 0.3* R471A/G586A P, S ++ ++ 132 ± 4*
D494Q S ++ ++ 3 ± 0.1* R471A/N587A P, S ++ ++ 373 ± 47*
N496A S ++ ++ 191 ± 38* R471A/N705A P ++ ++ 90 ± 10
N497A S ++ ++ 16 ± 1* N497K/N587A S ++ ++ 0.1 ± 0.01*
N497H S ++ ++ 177 ± 20* E548A/T550A S ++ ++ 95 ± 6
N497K S ++ ++ 0.1 ± 0.0* G586A/N587A S +++ ++ 97 ± 2
S498A S ++ ++ 0.4 ± 0.1* G586A/N705A P, S ++ ++ 117 ± 10
E499A S +++ ++ 40 ± 3* G586K/N705K P, S ++ ++ 0.02 ± 0.002*
W502A P +++ ++ 5 ± 1* N705A/V708A P ++ ++ 65 ± 5*
W502F P +++ ++ 5 ± 0.6* R471A/N497K/E531A P, S ++ ++ 0.8 ± 0.2*
T503A P +++ ++ 0.004 ± 0.0003* R471A/N497K/G586K P, S +++ ++ 0.01 ± 0.001*
T503S P ++ ++ 26 ± 2* R471A/G586A/N705A P, S ++ ++ 424 ± 12*
H509A P NT ++f 0.008f R471A/G586K/N705K P, S ++ ++ 3 ± 0.3*
H509F P ++ ++ 7 ± 1* R484C/G586A/N587A P, S ++ + 0.02 ± 0.002*
H509K P ++ ++ 93 ± 10 R471A/N497K/N587A P, S ++ ++ 0.3 ± 0.01*
H509N P ++ ++ 106 ± 11 R471A/N497K/E531A/N587A P, S +++ ++ 1 ± 0.02*
H509Q P ++ ++ 71 ± 6 R471A/N497K/E531A/ins2 P, S ++ ++ 0.001 ± 0.0001*
G512A P ++ ++ 3 ± 0.6* R471A/N497K/G586K/N705K P, S ++ ++ 0.001 ± 0.0001*
G512P P +++ + 0.005 ± 0.0001* E548A/T550A/G586A/N587A S +++ ++ 114 ± 5
D514A P +++ ++ 57 ± 5* E548A/T550A/G586A/N587A/ N705A/V708A P, S +++ ++ 20 ± 1*
K527A P +++ ++ 53 ± 7*
D528A P ++ ++ 2 ± 0.1* R471A/N497K/E531A/E548A/ T550A/G586A/N587A/ N705A/V708A P, S ++ ++ 0.02 ± 0.001*
D529A P ++ ++ 0.002 ± 0.0004*
D529E P +++ ++ 20 ± 2*
a

In mutations, the first letter is the amino acid in the wild-type AAV-2 capsid, the number is the VP1 amino acid position that was mutated, and the last letter is the mutant amino acid. For Δ265ins1, amino acid 265 was deleted and the sequence DASNDNLSSQSD inserted in its place. ins2 indicates an insertion of the sequence HKDDEAKFFPQ after position 536. Slashes separate the single mutations that are in multiple mutants.

b

Location of mutation. C; cylinder; P, plateau; S, spike.

c

Levels of capsid synthesis were determined by Western blotting of crude lysates. +++, 100 to 400% of the wild-type level; ++, 10 to 100% of the wild-type level; +, 1 to 9% of the wild-type level; NT, not tested.

d

Heparin binding levels. ++, 50 to 100% of the wild-type level; +, 10 to 49% of the wild-type level; +/−, 1 to 9% of the wild-type level; −, <1% of the wild-type level.

e

Transduction of human HepG2 cells in the presence of etoposide. Data are expressed as percentages of wild-type transduction (means ± standard errors of the means). Data are averages from two independent transfections to produce the AAV-2 vector and two transductions to measure titer. *, statistically different from wild-type results (P < 0.05). The lower limit of detection was 0.0005% of wild-type transduction.

f

Data from Opie et al. (34).

HHS Vulnerability Disclosure