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  • Title: Analysis of dominant-negative effects of mutant Env proteins of human immunodeficiency virus type 1.
    Author: Iwatani Y, Kawano K, Ueno T, Tanaka M, Ishimoto A, Ito M, Sakai H.
    Journal: Virology; 2001 Jul 20; 286(1):45-53. PubMed ID: 11448157.
    Abstract:
    The Env protein of human immunodeficiency virus type 1 is assembled into a stable trimer, and oligomerization is required for maintenance of viral infectivity. This property of Env suggests that Env mutants may have a dominant-negative effect on virus infectivity. To investigate this possibility, we established a packaging cell line in which both wild-type and mutant Env proteins could be expressed simultaneously in a single cell. We analyzed the effects of two types of Env mutants: cytoplasmic tail-truncated TM mutants and a mutant defective in gp120/gp41 cleavage. The cytoplasmic tail-truncated proteins were found to be incorporated into virions by forming an oligomer with wild-type TM, but could not inhibit the wild-type function. In contrast, phenotypic mixing of cleavage-defective Env with the wild-type protein caused dramatic inhibition of infectivity, indicating that this mutant has a strong dominant-negative phenotype.
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