Infection in vitro, this protein was tested for clinical efficacy in HIV-1-infected individuals; however, no effect on plasma viral loads was observed [13]. Further examination revealed that doses of sCD4 that were significantly higher than those achieved in the clinical trial were required to neutralize primary clinical isolates of HIV-1, in contrast to the relatively sensitive, laboratory-adapte
Coproteins [1]. Binding of gp120 to the receptor, CD4, on the target cell surface induces major conformational changes in the envelope glycoproteins [2]. These changes allow gp120 to bind the viral coreceptor, either CXCR4 or CCR5 [3?]. CD4 binding also induces the formation of a gp41 pre-hairpin intermediate, in which three hydrophobic grooves on the surface of a coiled coil formed by the heptad
Infection in vitro, this protein was tested for clinical efficacy in HIV-1-infected individuals; however, no effect on plasma viral loads was observed [13]. Further examination revealed that doses of sCD4 that were significantly higher than those achieved in the clinical trial were required to neutralize primary clinical isolates of HIV-1, in contrast to the relatively sensitive, laboratory-adapte
Infection in vitro, this protein was tested for clinical efficacy in HIV-1-infected individuals; however, no effect on plasma viral loads was observed [13]. Further examination revealed that doses of sCD4 that were significantly higher than those achieved in the clinical trial were required to neutralize primary clinical isolates of HIV-1, in contrast to the relatively sensitive, laboratory-adapte
GCl2, 25 mM Tris, pH 7.5 and 140 mM NaCl). For pulse activation experiments, the COS-1 cells were incubated with sCD4 (40 mg/ml, 0.8 mM) or 191 (360 mM) suspended in blocking buffer for three minutes, washed three times with blocking buffer and incubated for different time periods until the C34-Ig or 48d antibodies were added (at 40 mg/ml or 1 mg/ml, respectively, for 30 minutes). To study the tem
Ir Immune Defic Syndr. Author manuscript; available in PMC 2013 June 01.Mosam et al.Pagena e, 89 had advanced (but not immediately life threatening) KS and 58 had CD4
To current convention [46]). C34-Ig was produced and purified as previously described [47]. The CD4-Ig fusion protein consists of the first two N-terminal domains of the CD4 molecule and the Fc region of human IgG1. Purification was carried out as described for the C34-Ig molecule [47].mechanism of sCD4 neutralization [17,18]. Resistance to sCD4 may thus arise by a decreased affinity of the envelo
To current convention [46]). C34-Ig was produced and purified as previously described [47]. The CD4-Ig fusion protein consists of the first two N-terminal domains of the CD4 molecule and the Fc region of human IgG1. Purification was carried out as described for the C34-Ig molecule [47].mechanism of sCD4 neutralization [17,18]. Resistance to sCD4 may thus arise by a decreased affinity of the envelo