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2010 ; 1
(1
): 48-58
Nephropedia Template TP
gab.com Text
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English Wikipedia
Cryo-electron microscopy reconstructions of two types of wild rabbit hemorrhagic
disease viruses characterized the structural features of Lagovirus
#MMPMID21203997
Hu Z
; Tian X
; Zhai Y
; Xu W
; Zheng D
; Sun F
Protein Cell
2010[Jan]; 1
(1
): 48-58
PMID21203997
show ga
Rabbit hemorrhagic disease was described in China in 1984 and can cause
hemorrhagic necrosis of the liver within two or three days after infection. The
etiological agent, rabbit hemorrhagic disease virus (RHDV), belongs to the
Lagovirus genus in the Caliciviridae family. Compared to other calicivirus, such
as rNV and SMSV, the structure of Lagovirus members is not well characterized. In
this report, structures of two types of wild RHDV particles, the intact virion
and the core-like particle (CLP), were reconstructed by cryo-electron microscopy
at 11 &0A and 17 &0A, respectively. This is the first time the 3D structure of
wild caliciviruses CLP has been provided, and the 3D structure of intact RHDV
virion is the highest resolution structure in Lagovirus. Comparison of the intact
virion and CLP structures clearly indicated that CLP was produced from the intact
virion with the protrusion dissociated. In contrast with the crystal structures
of recombinant Norovirus and San Miguel sea lion virus, the capsomers of RHDV
virion exhibited unique structural features and assembly modes. Both P1 and P2
subdomains have interactions inside the AB capsomer, while only P2 subdomains
have interaction inside CC capsomer. The pseudo atomic models of RHDV capsomers
were constructed by homology modeling and density map fitting, and the rotation
of RHDV VP60 P domain with respect to its S domain, compared with SMSV, was
observed. Collectively, our cryo-electron microscopic studies of RHDV provide
close insight into the structure of Lagovirus, which is important for functional
analysis and better vaccine development in the future.