In this study, the near-complete genome sequence of the novel reassortant H1N2 influenza A virus strain A/swine/Korea/KS60/2016 is reported. Sequences of the hemagglutinin (HA), neuraminidase (NA), and polymerase basic 2 (PB2) genes were analyzed, revealing that the isolates contain segments from previous Korean swine H1N2 strains. Additionally, the remaining genes of this strain originated from human H1N1 strains in 2009.

Canine parvovirus (CPV) remains a leading infectious cause of death in canines, especially in young puppies. Though vaccination is being carried out regularly, immunization failures occur, and puppies may be exposed to infection. Virus-like particles (VLPs) act like a subunit vaccine, mimicking the structure of authentic viruses. Therefore, VLPs have the potential to be used as vaccine candidates. Since Viral Protein 2 (VP2), a major structural protein of CPV, is the crucial antigen for CPV, the purpose of this study was to produce a recombinant VP2 of new canine parvovirus-2a using the baculovirus expression system in SF9 insect cells. The results revealed that recombinant VP2 assembles to form VLPs with antigenic properties similar to those of natural CPV, the recombinant VLP can produce a hemagglutination assay (HA) titer (1:210) in SF9 cells. Expression of the recombinant 6-His-tagged VP2 in SF9 cells was confirmed by western blotting. These findings suggest that the recombinant VP2 expressed in this study could be used as an efficient subunit vaccine against CPV infection.

Porcine parvovirus 2 (PPV2) was recently detected in the Republic of Korea. This paper reports two near-complete genome sequences of PPV2 identified for the first time in the lung tissue of aborted pig fetuses.

Influenza A virus (IAV) causes respiratory disease in birds and mammals, including pigs and humans. Infection by IAV in pigs increases not only economic losses in the swine industry but also the emergence of novel IAV variants via gene reassortment, which is important due to the susceptibility of both birds and humans to IAV. This study provides serological data obtained during a study to detect IAV infections in pigs in the Republic of Korea during 2018 and 2019. A total of 1,559 samples were collected from 74 domestic pig farms. Hemagglutination inhibition (HI) assays were performed using the A/Swine/Korea/25-13(H1N1), A/Swine/Korea/E102 (H1N2), and A/Swine/Korea/Cy10/2007 (H3N2) viruses as antigens. The HI assay results showed that 266 of the 1,559 samples were seropositive (17.0%). Among these, H1N1, H1N2, and H3N2 comprised 7.3% (114), 6.0% (93), and 8.8% (137) of the 1,559 samples, respectively. Co-infections of H1N1/H1N2, H1N1/H3N2, H1N2/H3N2 and H1N1/H1N2/H3N2 were observed in 2.1% (31), 1.5% (23), 1.5% (24), and 0.8% (13) of the 1,559 samples, respectively. Interestingly, IAV infections were detected in all nine provinces of the country.

In this study, antibody responses after vaccination against equine influenza were investigated among 1,591 horses in the Republic of Korea using the hemagglutination inhibition (HI) test. Equine influenza has not occurred since 2011 and a commercial vaccine against H3N8 has been used. The equine influenza virus, A/equine/South Africa/4/03 (H3N8), was used as the antigen in the HI assay. The mean seropositive rate was 90.5% in 2019. Except for stallion whose seropositive rate was 78.5%, all seropositive rates of other horse types were over 90%. Regionally, except for Gangwon-do and Jeju-do whose seropositive rates were 89.0% and 87.1%, all seropositive rates in other provinces were over 90%. In the future, more through vaccination against equine influenza needs to be done based on this investigation result.

Viral protein 2 (VP2), which is the structural protein of parvovirus, can produce virus-like particles (VLPs) by a self-assembly process in vitro, making VLPs attractive vaccine candidates. VP2 of canine parvovirus (CPV) is responsible for neutralizing antibodies in immunized animals. In this study, VP2 protein of canine parvovirus-2c was expressed using a baculovirus expression system and assembled into parvovirus-like particles in insect cells. The results show that VP2 proteins assembled into virus-like particles (VLPs) with antigenic properties similar to those of natural CPV and a high hemagglutination (HA) titer (1:27). The recombinant 6-His-tagged VP2 protein with a molecular mass of about 65 kDa was detected by anti-His antibody and anti-PPV serum. This study provides a foundation for the application of VP2 protein in the clinical diagnosis of CPV and in the vaccination against CPV.