A viral histone H4 encoded by Cotesia plutellae bracovirus inhibits haemocyte-spreading behaviour of the diamondback moth, Plutella xylostella.
Histone H4 is highly conserved and forms a central-core nucleosome with H3 in eukaryotic chromatin. Its covalent modification at the protruding N-terminal region from the nucleosomal core can change the chromatin conformation in order to regulate gene expression. A viral H4 was found in the genome of Cotesia plutellae bracovirus (CpBV). The obligate host of the virus is an endoparasitoid wasp, C. plutellae, which parasitizes the diamondback moth, Plutella xylostella, and interrupts host development and immune reactions. CpBV has been regarded as a major source for interrupting the physiological processes during parasitization. CpBV H4 shows high sequence identity with the amino acid sequence of P. xylostella H4 except for an extended N-terminal region (38 aa). This extended N-terminal CpBV H4 contains nine lysine residues. CpBV H4 was expressed in P. xylostella parasitized by C. plutellae. Western blot analysis using a wide-spectrum H4 antibody showed two H4s in parasitized P. xylostella. In parasitized haemocytes, CpBV H4 was detected predominantly in the nucleus and was highly acetylated. The effect of CpBV H4 on haemocytes was analysed by transient expression using a eukaryotic expression vector, which was injected into non-parasitized P. xylostella. Expression of CpBV H4 was confirmed in the transfected P. xylostella by RT-PCR and immunofluorescence assays. Haemocytes of the transfected larvae lost their spreading ability on an extracellular matrix. Inhibition of the cellular immune response by transient expression was reversed by RNA interference using dsRNA of CpBV H4. These results suggest that CpBV H4 plays a critical role in suppressing host immune responses during parasitization.
Gad
Wael
W
Department of Bioresource Sciences, Andong National University, Andong 760-749, Republic of Korea.
Kim
Yonggyun
Y
Department of Bioresource Sciences, Andong National University, Andong 760-749, Republic of Korea.
D000107:Acetylation; D000818:Animals; D001483:Base Sequence; D002465:Cell Movement; D002467:Cell Nucleus / Q000378:metabolism; D015536:Down-Regulation; D005814:Genes, Viral; D006434:Hemocytes / Q000502:physiology*; D006657:Histones / Q000502:physiology*; D007814:Larva / Q000276:immunology / Q000469:parasitology; D008969:Molecular Sequence Data; D009036:Moths / Q000276:immunology* / Q000469:parasitology; D018071:Polydnaviridae / Q000737:chemistry* / Q000235:genetics; D016415:Sequence Alignment; D014764:Viral Proteins / Q000235:genetics / Q000378:metabolism*; D014863:Wasps / Q000737:chemistry / Q000502:physiology / Q000821:virology
D006657:Histones; D014764:Viral Proteins