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2014 ; 16
(5
): 627-638
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Structural insight into HIV-1 restriction by MxB
#MMPMID25312384
Fribourgh JL
; Nguyen HC
; Matreyek KA
; Alvarez FJD
; Summers BJ
; Dewdney TG
; Aiken C
; Zhang P
; Engelman A
; Xiong Y
Cell Host Microbe
2014[Nov]; 16
(5
): 627-638
PMID25312384
show ga
The myxovirus resistance (Mx) proteins are interferon-induced dynamin GTPases
that can inhibit a variety of viruses. Recently, MxB, but not MxA, was shown to
restrict HIV-1 by an unknown mechanism that likely occurs in close proximity to
the host cell nucleus and involves the viral capsid. Here, we present the crystal
structure of MxB and reveal determinants involved in HIV-1 restriction. MxB
adopts an extended antiparallel dimer and dimerization, but not higher-ordered
oligomerization, is critical for restriction. Although MxB is structurally
similar to MxA, the orientation of individual domains differs between MxA and
MxB, and their antiviral functions rely on separate determinants, indicating
distinct mechanisms for virus inhibition. Additionally, MxB directly binds the
HIV-1 capsid, and this interaction depends on dimerization and the N terminus of
MxB as well as the assembled capsid lattice. These insights establish a framework
for understanding the mechanism by which MxB restricts HIV-1.
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