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2015 ; 112
(13
): 3973-8
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Structural basis for the enhancement of virulence by viral spindles and their in
vivo crystallization
#MMPMID25787255
Chiu E
; Hijnen M
; Bunker RD
; Boudes M
; Rajendran C
; Aizel K
; Oliéric V
; Schulze-Briese C
; Mitsuhashi W
; Young V
; Ward VK
; Bergoin M
; Metcalf P
; Coulibaly F
Proc Natl Acad Sci U S A
2015[Mar]; 112
(13
): 3973-8
PMID25787255
show ga
The great benefits that chemical pesticides have brought to agriculture are
partly offset by widespread environmental damage to nontarget species and threats
to human health. Microbial bioinsecticides are considered safe and highly
specific alternatives but generally lack potency. Spindles produced by insect
poxviruses are crystals of the fusolin protein that considerably boost not only
the virulence of these viruses but also, in cofeeding experiments, the
insecticidal activity of unrelated pathogens. However, the mechanisms by which
spindles assemble into ultra-stable crystals and enhance virulence are unknown.
Here we describe the structure of viral spindles determined by X-ray
microcrystallography from in vivo crystals purified from infected insects. We
found that a C-terminal molecular arm of fusolin mediates the assembly of a
globular domain, which has the hallmarks of lytic polysaccharide monooxygenases
of chitinovorous bacteria. Explaining their unique stability, a 3D network of
disulfide bonds between fusolin dimers covalently crosslinks the entire
crystalline matrix of spindles. However, upon ingestion by a new host, removal of
the molecular arm abolishes this stabilizing network leading to the dissolution
of spindles. The released monooxygenase domain is then free to disrupt the
chitin-rich peritrophic matrix that protects insects against oral infections. The
mode of action revealed here may guide the design of potent spindles as
synergetic additives to bioinsecticides.
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