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Our data demonstrate that HOCl-modified mouse-, bovine- and human serum albumins all bind to the HIV-1 NL4-3 gp120 (LAV) glycoprotein in contrast to non-modified albumin.

Binding of HOCl-modified albumin to gp120 correlated to the blockade of CD4 as well as that of V3 loop specific monoclonal antibody binding.

The concentration of HOCl was monitored by UV spectroscopy (ε = 375 mol/cm liter).

Viral infection was monitored by a standard p24 or X-gal staining assay.Such masking of the viral gp120/gp41 envelope complex might be a simple but promising strategy to inactivate HIV-1 and therefore prevent infection when HOCl-modified serum albumin is applied, for example, as a topical microbicide. Since HIV-1 variability is prodigious, viral escape to all these antiviral substances has been documented and therefore there is a pressing need to find new strategies to efficiently block HIV-1 infection.In 1992, Klebanoff and coworkers [] showed that stimulated polymorphonuclear (PMN) cells released an unknown factor which neutralized HIV-1.The plates were incubated for 1 h at room temperature and then washed 5-times with PBST.To detect gp120-bound r CD4 we used the anti-CD4 mouse monoclonal antibody NCL-CD4-1F6 (Novocastra).

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Bound anti-CD4 antibody was detected by a secondary anti-mouse HRP-antibody conjugate diluted 0 in PBS (Bio Rad).

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