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Abstract
Besides mediating the viral entry process, the human immunodeficiency virus (HIV-1) envelope protein gp41 can bind to many host cell components and regulate cell functions. Using a yeast two-hybrid system, we screened a human bone marrow cDNA library and identified a novel gp41-binding protein, CD74 (the MHC class II-associated invariant chain). Here, we report possible biological effects mediated by interaction between gp41 and CD74. We found that HIV-1 gp41 could bind directly to host CD74 in HIV-1-infected cells, and the peptide 6358 derived from gp41 loop region (aa 597-611) could effectively block the gp41-CD74 interaction. As a result of this binding, recombinant soluble gp41 and gp41 peptide 6358 activated the CD74-mediated ERK/MAPK pathway and significantly enhanced HIV-1 infection in vitro. Conversely, the enhancing effect could be suppressed by the recombinant CD74 extracellular domain. These results reveal a novel mechanism underlying gp41 mediation of HIV-1 infection and replication.
Highlights
We know that the HIV-1 gp41 could change conformation triggered by gp120-CD4 interaction and mediate virus-cell fusion, it is unclear whether gp41 itself can interact with the cell surface proteins to trigger cell signals for regulating viral infection and host cell function
We carried out a yeast two-hybrid screening to discover novel gp41-binding proteins, and we discovered CD74, known as the MHC class II-associated invariant chain
RCD74 Binds to Native Gp41, but Binding Is Blocked by Gp41 Loop Peptide—Because gp41 and CD74 are both membrane proteins, we reasoned that they interact on the cell surface
Summary
To inhibit the enhancing effect, rCD74 was incubated with peptide 6358 and rsgp41 for 1 h before adding to the cells. RCD74 Binds to Native Gp41, but Binding Is Blocked by Gp41 Loop Peptide—Because gp41 and CD74 are both membrane proteins, we reasoned that they interact on the cell surface. Because peptide 6358 and rsgp41 could bind CD74, we tested whether they could activate the ERK/ MAPK pathway.
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