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In the recent past, virus-like particles (VLPs) research has received extensive attention in various fields such as vaccine preparation, drug delivery, gene therapy and material sciences. Especially, the recombinantly expressed VLPs of HcRNAV (single standard RNA viruses infecting bivalve killing dinoflagellate, Heterocapsa circularisquama) is considered a potent carrier for harmful algal bloom suppression. The HCRNAV strains were divided in two types; HcRNAV34 (UA-type) and HcRNAV109 (CY-type), based on their complementary strain-specific infectivity. The capsid proteins of the viruses contain variable amino acid regions, which may be related to their specific host infectivity. The structural gene sequence encoding the capsid proteins of HcRNAV34 and HcRNAV109 were obtained from Genbank [accession number; AB218608 and AB218609.1]. The genes (orf-2) encoding the capsid proteins were obtained by gene syntheses, which optimized the codon usages of the genes for efficient translation in E.coli. The DNA fragment (orf-2) containing the full-length capsid genes of HcRNAV34 and HcRNAV109 were cloned into the expression vector, pET30a(+), contain the 6 x His tag. The expression of the orf-2 in the vector and chaperone was induced by IPTG in E. coli BL21(DE3). SDS-PAGE analysis showed that this expression system is capable of producing significant levels of VLPs. Also, the over-expressed proteins were detected by western blotting using anti-histidine polyclonal antibody. VLPs were purified using Ni-NTA affinity column chromatography. In the present study, the possibility of controlling of the harmful algal blooming in the sea by specific recombinant VLPs which has host specificity was investigated. Host specificity and specific cell destruction of the HcRNAV34 and HcRNAV109 VLPs were investigated against H. circularisquama strains under microscopy by encapsulating the particles with FITC. It was packed into VLPs by dissociation and re-association processes. The HcRNAV34VLPs encapsulating FITC specifically attached and destroyed the cells of H. circularisquama HU9433-P and HA92-1 which are the hosts of the HcRNAV34 strains. In contrast, the capsid of HcRNAV109 exhibited specific affinity to H. circularisquamastrain HY9423. These results indicate that the recombinant VLPs has considerably high host specificity and is compatible with a common viral property of host specific infection.