An amphipathic sequence in the cytoplasmic tail of HIV-1 Env alters cell tropism and modulates viral receptor specificity.

Abstract

The human immunodeficiency virus type 1 (HIV-1) 92UG046 Env protein, obtained from a CD4-independent HIV-1 primary isolate (Zerhouni et al., 2004), has the ability to initiate an infection in HeLa cells expressing CD4 when carrying the full-length (FL) Env, but uses CD8 molecules for receptor-mediated entry when carrying a truncated Env (CT84). To determine whether a specific length or structure in the cytoplasmic tail (CT) is responsible for this alteration of tropism, we compared a series of Env constructs with different CT truncations and the presence or absence of an amphipathic alpha- helical sequence. We found that truncated constructs containing the alpha-helical LLP-2 structure in their CT domains conferred a switch from CD4 to CD8 tropism. The results support the conclusion that the structure of the CT domain can play an important role in determining receptor specificity.

• Authors: A N Vzorov, C Yang, R W Compans
• Journal: Acta virologica (Acta Virol) Vol. 59 Issue 3 Pg. 209-20 (Sep 2015) ISSN: 0001-723X [Print] Slovakia
• PMID: 26435143 (Publication Type: Journal Article, Research Support, N.I.H., Extramural)

Chemical References

• Receptors, HIV
• env Gene Products, Human Immunodeficiency Virus

Topics

• Amino Acid Sequence
• Animals
• Cells, Cultured
• Cytoplasm (chemistry)
• HIV-1 (physiology)
• Humans
• Mice
• Molecular Sequence Data
• Protein Structure, Tertiary
• Receptors, HIV (physiology)
• Tropism
• env Gene Products, Human Immunodeficiency Virus (chemistry, physiology)