Timothy J. Gregory

TL;DR: A newly-constructed antibody-like molecule containing the gp!20-binding domain of the receptor for human immunodeficiency virus blocks HIV-1 infection of T cells and monocytes, making it a good candidate for therapeutic use.

TL;DR: Using in vitro mutagenesis, it is found that deletion of 12 amino acids from this region of gp120 leads to a complete loss of binding and a single amino acid substitution in this region results in significantly decreased binding, suggesting that sequences within this region are directly involved in the binding of gp 120 to the CD4 receptor.

TL;DR: In this paper, soluble, secreted forms of CD4 were produced by transfection of mammalian cells with vectors encoding versions of CD 4 lacking its transmembrane and cytoplasmic domains.

TL;DR: In this paper, the primary human T cell response to HIV was analyzed by isolating from seronegative donors T cell clones specific for HIV gp120, and synthetic peptides were used to address the fundamental problem of how HIV sequence variability affects T cell recognition.

TL;DR: It is shown that a CD4 immunoadhesin can mediate antibody-dependent cell-mediated cytotoxicity (ADCC) towards HIV-infected cells, although, unlike natural anti-gpl20 antibodies, it does not allow ADCC towards uninfected CD4-expressing cells that have bound soluble gpl20 to the CD4 on their surface.