Host proteins are incorporated both on and inside human immunodeficiency vi
rus type 1 (HIV-1) virions. To identify cellular proteins inside HIV-1, vir
ion preparations were treated by a protease-digestion technique that remove
s external host proteins, allowing for the study of the proteins inside the
virus. Treated HIV-1 preparations were analyzed by immunoblot, high-pressu
re liquid chromatography, and protein sequence analyses. These analyses ide
ntified several cellular proteins inside HIV-1: elongation factor 1 alpha,
glyceraldehyde-3-phosphate dehydrogenase, HS-1, phosphatidylethanolamine-bi
nding protein, Pin1, Lck, Nm23-H1, and the C-terminal tail of CD43. Several
of these proteins were found as fragments of their full-sized proteins tha
t appear to be generated by our protease treatment of the virions, the HIV-
1 protease, or a cellular protease. Recent advances in cell biology and bio
chemistry have identified some of these proteins as actin-binding proteins.
These results support the hypothesis that actin filaments are incorporated
into the virion and may provide additional clues for the understanding of
the interaction between viral and cellular proteins during assembly and bud
ding. (C) 2000 Academic Press.