Moore J P, Simpson G, McKeating J A, Burakoff S J, Schreiber S L, Weiss R A
Chester Beatty Laboratories, Institute of Cancer Research, London, United Kingdom.
Virology. 1992 Jun;188(2):537-44. doi: 10.1016/0042-6822(92)90508-m.
The initial step in the infection cycle of human immunodeficiency virus type 1 (HIV-1) involves binding of its surface glycoprotein gp 120 to the T lymphocyte CD4 antigen. CPF-DD is a low molecular weight inhibitor of HIV infectivity that inhibits gp 120 binding to CD4 in vitro (Finberg et al., Science 249, 287-291, 1990). We find, however, that the actions of CPF-DD are not limited to its ability to interfere with gp 120-CD4 binding; its predominant action is to remove the viral envelope from the underlying core. Subsequently the virions disintegrate. Most enveloped viruses tested were inhibited by CPF-DD, but the infectivity of noneneloped viruses was unaffected or only slightly reduced.