TABLE 1.

Ability of potential inhibitors to modulate infection of PHH^a

Potential inhibitor and amt and/or concnb	Relative RNA accumulation (%)c following infection with:
	HDV	HBV	HIV(LS)	HIV(G)
None	100 ± 21	100 ± 34	100 ± 22	100 ± 26
SVP(−)
2 U (0 nM)	228 ± 206	207 ± 94	158 ± 56	253 ± 77
50 U (0 nM)	32 ± 13	44 ± 28	22 ± 11	44 ± 18
SVP(S)
2 U (80 nM)	220 ± 52	170 ± 84	123 ± 62	183 ± 89
50 U (2,000 nM)	13 ± 3	36 ± 21	18 ± 10	27 ± 8
SVP(LS)
2 U (40 nM)	110 ± 51	157 ± 93	209 ± 104	181 ± 112
50 U (1,000 nM)	105 ± 36	89 ± 18	47 ± 6	74 ± 14
S1S2-IA
2 nM	170 ± 117	207 ± 24	138 ± 10	392 ± 42
50 nM	<0.6	0.6 ± 0.6	1.1 ± 0.1	117 ± 6
Peptide
2 nM	25 ± 15	187 ± 33	139 ± 9	409 ± 49
50 nM	<0.6	0.3 ± 0.3	0.9 ± 0.4	75 ± 18

^aPHH were pretreated for 1 h with the indicated potential inhibitor, and then a mixture of four viruses in 5% PEG, along with the potential inhibitor, was added and left for 6 h. The medium was then replaced and the infection allowed for 6 days, after which total RNA was extracted and quantitative real-time PCR assays were used to determine the amount of replication for each of the four viruses.

^bThe three forms of SVP were prepared from the same volumes of medium harvested between days 0 and 3 after transfection of the cells with either empty plasmid [SVP(−)], HBV S plasmid [SVP(S)], or plasmids expressing HBV L and S [SVP(LS)]. The amounts of the three SVP are expressed in arbitrary units. In addition, for SVP(S) and SVP(LS) we used immunoblots relative to protein standards to determine the final concentrations of HBV envelope proteins in the preparations. For the immunoadhesin S1S2-IA, the concentration was determined as previously described (9), while for the chemically synthesized peptide, the concentration was determined for the purified product (17).

^cThe infections were performed in triplicate, and the values are averages and standard deviations.